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1212 Ashley Circle, Suite 4
Bowling Green, KY 42104
At Frank L. Duncan, D.D.S we offer a range of treatment options for sleep apnea. If snoring or obstructed breathing is a problem, call Dr. Duncan today to learn how we can help you breathe easier.
Left untreated, sleep apnea can cause serious health problems, so contact us now to schedule an examination.
Safe, anxiety-free dentistry with Bowling Green area dentist Dr. Frank Duncan means you can have dental treatments done quickly while you're lightly sedated, with little or no discomfort.
You no longer have to tolerate feeling uncomfortable, hiding your smile, or putting off dental work because of a busy schedule. You'll feel relaxed during your dental appointment, and relieved that your oral health is in good hands.
Frank L. Duncan, D.D.S is pleased to offer long-term financing for our qualified Bowling Green area dental patients. We realize that some dental treatments are easier to pay off over time. We want to help make it possible for you to have the smile you've always wanted.
Dr. Duncan provides secure implant dentures in the Bowling Green area. Implant retained dentures won't slip, and are a long-lasting solution to missing teeth.
You'll talk, eat and smile with more confidence. Your self esteem will return with your new natural-looking teeth.
With oral conscious sedation, Bowling Green area sedation dentist Frank Duncan, D.D.S. is medically able to attend to your dental needs for a longer period of time. This means you can combine all or many of your dental appointments into one. If you are in need of extensive dental work or multiple treatments are necessary, oral sedation dentistry may be the most efficient and hassle-free option for you to consider.
130 Thompson Poynter Road
London, KY 40741
A beautiful smile can brighten your life! If you are continuously hiding your chipped, stained, or cracked teeth from others, it's time for a change! Michael Trosper, D.M.D., a trusted London area dentist, can fix chips, cracks, and stains to reveal a great new smile - and a new you. You'll look so good you'll wonder why you waited so long!
London area cosmetic dentist Michael Trosper, D.M.D. has extensive experience creating beautiful smiles. They're one of the first things people notice about you.
Our professional team will be happy to discuss your aesthetic dentistry options. The attractive results you'll get from Pepperhill Dental Care can change your life!
Don't let untreated dental problems get you down. Rebuild your confidence with a beautiful new smile. From simple treatments that make a big difference, to more extensive work, unveiling the smile you were meant to have can have profound life-changing effects. Serving the London, KY area and offering cosmetic dentistry, Dr. Trosper can help you develop an affordable treatment plan you'll feel good about.
Most major credit cards are accepted at Pepperhill Dental Care in the London area. Types of cards accepted include Visa, MasterCard, and Discover Card.
London area restorative dentistry at Pepperhill Dental Care can produce natural-looking results. If you have a damaged or missing tooth, we can help.
Our highly skilled team will assess your need for a crown, bridge, implant or other procedure to restore or improve your smile. Our goal is to provide quality dental care for your life-long oral health.
10515 Meeting St. #104
Prospect, KY 40059
Caicedo, Ricardo D.D.S.
501 S Preston St # 35d
Louisville, KY, 40202-1701
Shields, Daniela K D.D.S.
3429 Lone Oak Rd # 1
Paducah, KY, 42003-5775
(270) 683-5344
Kelly, Emily D.D.S.
7214 Dixie Hwy
Louisville, KY, 40258-3720
teeth whitening coupons in Brentwood 37027
dental veneers cost in Logan Utah
temporary cosmetic teeth in Union City 94587
When you decide to have crowns done, especially if they involve your front teeth, you will want to be able to give your input regarding how the final crowns will look. One way to do this is with temporary dental crowns. When your teeth are prepared for crowns, the dentist will place temporary dental crowns for you to wear while the final crowns are being made.
There are some differences between temporary dental crowns and final crowns that you should be aware of. Temporary dental crowns are made of a different material, usually some sort of a plastic or acrylic. Since these materials are not as strong as your own teeth, you will have to be careful of what you eat. You should avoid hard foods such as nuts, and tough foods such as bagels or French bread.
Another difference is that temporary dental crowns are cemented on with a dental cement. The reason for this is that the cosmetic dentist will need to be able to remove the temporary dental crowns when it is time to cement the permanent ones. Since the cement is not as strong, sticky foods may cause them to come loose.
If your temporary dental crowns come off or are loose, you should call your dentist so that they can be re-cemented. It is important not to wait, as the tooth may be sensitive, it may move, or, if a long enough period of time passes, the tooth may get decay. As far as home care, your temporary dental crowns should be cleaned with a toothbrush, just like your own teeth. When flossing, though, it is important to floss towards the gums and then slide the floss out by one end rather than lifting it back up through the teeth. This will help ensure that your temporary dental crowns do not come off while flossing.
By Greggory Kinzer, DDS, MSD
Cosmetic dentists aren't all white coats and Novocaine. There is both art and science in a dentist's day. Case in point: what appears to be more or less routine restoration of missing or broken teeth - a dental crown or a dental bridge - is akin to principles of architecture.
Think of the arch of your mouth like the roof of a house. Each element of the structure relies on another. If a rafter breaks, the entire building will, sooner or later, buckle. So it is with your teeth.
The mouth is balanced; teeth function together. One missing tooth can cause permanent changes in your bite. Neighboring teeth drift into the empty space. The opposing tooth will actually grow longer and longer, further frustrating normal chewing. You'll tend to favor one side of your mouth over another. This old house is eventually doomed.
Dentists, then, are believers in tooth restoration and dental crowns. With all the new materials cosmetic dentistry offers today, virtually any mouth can be restored to good working order. A tooth that might have been lost five years ago now has many options for renewed vitality.
And the cosmetic results that can be achieved are, well, awesome. When it comes to new dental technologies, take advantage. Your cosmetic dentist will be there when you're ready to go for it.


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A driver in Edmonton resigned after a three-year-old girl was left sleeping on her school bus Wednesday morning.
The child did not get off the bus when it arrived at Mother Theresa Elementary School in central Edmonton where the girl attends a preschool program.
When the bus returned two and half hours later, the little girl was still on board.
"Police are confident that the little girl fell asleep. She probably slipped down on the seat a bit, so she was not visible, and she was asleep for the two and a half hours that the bus was not at the school," said Lori Nagy from Edmonton Catholic Schools.
The school's principal called police, and the female driver was interviewed. Police said they believe the child was not harmed and aren't pursing the matter any further.
Millie Smith, office administrator with RL Smith Transportation, said she is concerned that the driver did not check the bus to make sure everyone had gotten off.
"One of our daily routines is for the drivers to do a walkthrough after they've dropped off their students at the school," she said. "We will be meeting with our drivers over the next week to again go over this procedure."
Smith said the bus was parked at the driver's home, which is where drivers take their vehicles after they do a run.
Smith said the driver, who has been at the company since September, resigned immediately after the child had been found.
The driver had passed all criminal checks.
But the school district says it has serious concerns about how the bus company handled the incident.
"Only 20 children could sit on that bus, and yet the bus was not checked," Nagy said. "Really, that is inexcusable."
Nagy said the school board's contract with its bus carriers stipulates that buses are checked to make sure every student has gotten off.
Nagy said that Edmonton Catholic Schools board will be looking at all the options to ensure this doesn't happen again, including possibly looking for another bus carrier.
Nagy said she doesn't know what steps the school took to notify the parents. She said that will be part of the board's investigation.

subset: commoncrawl


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The 2011 recruiting class for the state of Texas was known as the year of the running back with over 30 running backs garnering D-1 scholarships offers. This year could be a big year for offensive ...
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Herpes simplex virus type 1 (HSV-1) glycoprotein C (gC) blocks complement activation, and glycoprotein E (gE) interferes with IgG Fc-mediated activities. While evaluating gC- and gE-mediated immune evasion in human immunodeficiency virus (HIV)-HSV-1-coinfected subjects, we noted that antibody alone was more effective at neutralizing a strain with mutations in gC and gE (gC/gE) than a wild-type (WT) virus. This result was unexpected since gC and gE are postulated to interfere with complement-mediated neutralization. We used pooled human immunoglobulin G (IgG) from HIV-negative donors to confirm the results and evaluated mechanisms of the enhanced antibody neutralization. We demonstrated that differences in antibody neutralization cannot be attributed to the concentrations of HSV-1 glycoproteins on the two viruses or to the absence of an IgG Fc receptor on the gC/gE mutant virus or to enhanced neutralization of the mutant virus by antibodies that target only gB, gD, or gH/gL, which are the glycoproteins involved in virus entry. Since sera from HIV-infected subjects and pooled human IgG contain antibodies against multiple glycoproteins, we determined whether differences in neutralization become apparent when antibodies to gB, gD, or gH/gL are used in combination. Neutralization of the gC/gE mutant was greatly increased compared that of WT virus when any two of the antibodies against gB, gD, or gH/gL were used in combination. These results suggest that gC and gE on WT virus provide a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL, or gD-gH/gL interactions and that one function of virus neutralization is to prevent interactions between these glycoproteins.
Herpes simplex virus type 2 (HSV-2) infection is a significant risk factor for the acquisition of human immunodeficiency virus (HIV) (27, 39, 42). Individuals who are seropositive for HSV-2 have a twofold increased risk of acquiring HIV (39). Acquisition rates appear greatest following the initial HSV-2 infection, when HSV-2 reactivation is most frequent (3, 29, 40). Currently, 17% of adults in the United States are infected with HSV-2, with much greater prevalence rates in parts of South America and Africa (33, 44). While less is known about the epidemiological link between HSV-1 and HIV, studies suggest similar interactions (5, 6).
HSV-1 encodes glycoproteins involved in evading immunity, which is mediated by antibody or complement (22). Glycoprotein C (gC) binds complement component C3b, preventing the activation of the complement cascade (9, 11, 15, 19, 30, 31). Glycoproteins E and I (gE and gI) form a high-affinity receptor that binds the Fc region of immunoglobulin G (IgG), inhibiting complement activation and antibody-dependent cellular cytotoxicity (8, 10). HSV-1 strains that are defective in either IgG Fc or C3b binding or both due to targeted mutations in gC and gE are less virulent than the WT or marker-rescued viruses (23-26).
We were interested in determining whether antibody and complement levels are maintained at high enough concentrations in HIV-infected individuals to neutralize an HSV-1 strain with mutations in gC and gE (gC/gE) that is defective in immune evasion. If so, strategies aimed at blocking the immune evasion properties of gC and gE in HIV-infected subjects coinfected with HSV may represent a novel approach to preventing HSV recurrences (7, 20, 21).
We evaluated HIV-HSV-1-coinfected subjects and unexpectedly demonstrated that antibodies from -coinfected and HSV-1-monoinfected subjects had a greater neutralizing activity against an HSV-1 gC/gE mutant than against a WT virus. Since HSV-1-neutralizing antibodies primarily target the viral glycoproteins that are required for virus entry, we compared the neutralization of gC/gE mutant and WT viruses, using antibodies to gB, gD, or gH/gL, used either alone or in combination (16, 17, 34, 35, 38). We demonstrated that antibodies against each glycoprotein used alone showed neutralization activity that was comparable for both viruses; however, used in combination, antibodies were significantly more active against the gC/gE mutant than the WT virus. These results support a protective role for gC and gE on the WT virus in preventing antibodies from blocking interactions between gB, gD, and gH/gL.
African green monkey kidney cells (Vero) were grown in Dulbecco's modified Eagle's medium supplemented with 10% heat-inactivated fetal bovine serum, 2 mM l-glutamine, 10 mM HEPES (pH 7.3), 20 μg/ml gentamicin, and 1 μg/ml amphotericin B (Fungizone; Life Technologies, Rockville, MD). Pools of purified virus were prepared by infecting Vero cells at a multiplicity of infection range of 2 to 5. Supernatant fluids 24 h postinfection were harvested for cell-free virus and centrifuged onto a 5% to 70% sucrose gradient (13). Virus-containing fractions were isolated and dialyzed against Dulbecco's phosphate-buffered saline (PBS) with Ca2+ and Mg2+, aliquoted, and stored at −70°C.
The WT strain, HSV-1 NS, is a low-passage clinical isolate obtained from an infected child (12). Mutant viruses derived from the NS strain, NS-gCΔC3 and NS-gE339, and the double mutant NS-gCΔC3,gE339 have been described previously (20, 24-26). The gC mutant virus NS-gCΔC3 has a deletion from amino acid 275 to 367, resulting in a loss of C3b binding (23). The gE mutant virus NS-gE339 has a four-amino-acid insertion at gE amino acid 339, resulting in the loss of IgG Fc binding (26). The gC/gE double-mutant virus NS-gCΔC3,gE339 contains both the gC and gE mutations in a single virus (20, 24).
Sera from HIV subjects at various stages of HIV disease (CD4 count, <200/μl, 200 to 500/μl, >500/μl) were obtained from the Clinical Core Laboratory of the University of Pennsylvania Center for AIDS Research. Sera were tested for antibodies to HSV-1 and HSV-2 by using a HerpeSelect 1 and 2 enzyme-linked immunosorbent assay (ELISA) IgG (Focus Technologies, Cypress, CA), which is a glycoprotein G-based assay that can detect type-specific IgG antibodies. Samples that were antibody positive to HSV-1 and antibody negative to HSV-2 (HSV 1+/2−) were selected for further evaluation. HIV-seronegative sera were obtained from healthy volunteers who participated in the GlaxoSmithKline HSV-2 glycoprotein D adjuvant (gD2) placebo-controlled vaccine trial (36). Sera selected were from HSV 1+/2− subjects who did not receive the gD2 vaccine. Subject consent was obtained prior to the study, and the University of Pennsylvania Human Subjects Committee approved the use of human sera for this research.
Patient IgG was purified from sera, using HiTrap protein G columns according to the manufacturer's instructions (Amersham Biosciences, Uppsala, Sweden). Fractions containing protein were pooled, dialyzed against PBS at 4°C, concentrated, and stored in aliquots at −20°C. IgG was purified from rabbits inoculated with the purified baculovirus proteins gB, gC, gD, gH/gL, or gI (2, 28, 32). The antibody to gI was produced in rabbits, using baculovirus-expressed gI amino acids 24 to 264 as the antigen (H. M. Friedman, unpublished). Pooled human IgG was purchased from the Michigan Department of Public Health, Lansing, that was prepared from the sera of thousands of HIV-negative donors (26).
Purified virus at a final concentration of 106 PFU/ml was incubated in 50 μl with an equal volume of 1% HSV 1+/2− serum treated with EDTA to inactivate the complement or with PBS for 1 h at 37°C (13, 14). Viral titers remaining were determined by plaque assay on Vero cells. Antibody neutralization was calculated as the difference between the titers of virus that was incubated with PBS and that of virus incubated with EDTA-treated serum to inactivate the complement. In some assays, pooled human IgG or rabbit antibodies to the purified baculovirus proteins gB, gC, gD, gH/gL, or gI were used (2, 24, 28, 32, 37).
Purified WT and gC/gE mutant viruses, each at 2 × 105, 1 × 106, and 4 × 106 PFU, were run on 4 to 15% sodium dodecyl sulfate-polyacrylamide gels, transferred to Immobilon-P transfer membranes (Millipore Corp., Bedford, MA), and detected using polyclonal rabbit antibodies to gB, gC, gD, gE, gH/gL, gI, and VP5 (2, 21, 28, 32, 37, 41). Horseradish peroxidase-conjugated goat anti-rabbit IgG and enhanced chemiluminescence (Amersham Pharmacia, Piscataway, NJ) were used to visualize the primary antibodies. Densitometry analyses were performed using a ScanMaker i900 (Microtek Lab Inc., Carson, CA) unit to compare relative protein concentrations.
Student's t test (Microsoft Excel software) was used to determine P values. Results were considered significant at a probability (P) value of <0.05.
To identify HIV subjects coinfected with HSV-1 (HSV 1+/2−), we tested serum for antibodies to HSV-1 and HSV-2 from the first 133 subjects enrolled in the Center for AIDS Research Clinical Core database, for whom both serum and CD4 T-cell counts were available. Overall, 39% had CD4 T-cell counts of >500/μl, 28% had 200 to 500/μl, and 33% had counts of <200/μl. Twenty-eight percent of subjects were seropositive for HSV-1 and seronegative for HSV-2 (HSV 1+/2−), 23% were HSV 1−/2+, 41% were doubly seropositive (HSV 1+/2+), and 8% were doubly seronegative (HSV 1−/2−). Sera from HSV 1+/2− subjects were selected for further analysis.
The neutralizing activity of the antibody was determined by using a 1:100 dilution of serum (1%) that was treated with EDTA to inactivate complement. Antibody neutralized both the WT virus and the gC/gE mutant virus at all stages of HIV disease; however, antibody neutralization of the gC/gE mutant virus was greater than that of the WT virus for each of the four groups tested (Fig. (Fig.1).1). We previously reported that gC and gE protect the virus from neutralization because these glycoproteins inhibit complement activation. Much higher concentrations of neutralizing antibodies were used in the current study than in our previous reports (20, 24). Nevertheless, we were surprised to find that antibody alone had a greater effect on the gC/gE mutant than on the WT virus.
To further evaluate the enhanced neutralization of the gC/gE mutant virus by antibody, a dose-response experiment was performed using serial twofold dilutions of pooled human IgG. At 25, 50, and 100 μg/ml, the pooled human IgG neutralized more of the gC/gE mutant virus than the WT virus, demonstrating 0.6, 1.0, and 2.0 log10 differences, respectively, at increasing concentrations of IgG (Fig. (Fig.2).2). At 200 μg/ml, the IgG totally neutralized both viruses. Therefore, the gC/gE mutant virus was more readily neutralized than the WT virus by HSV antibodies in a dose-dependent fashion.
Additional studies were performed to evaluate the unexpected finding that antibody had a greater neutralizing effect on the gC/gE mutant virus than it did on the WT virus. One possible explanation for the greater susceptibility of the gC/gE mutant virus to antibody is that the mutant virus may incorporate fewer HSV-1 glycoproteins into the virion envelope. If this occurs, fewer antibody molecules would be required to neutralize the virus, since fewer target glycoproteins are present. We performed Western blotting and densitometry analysis using 2 × 105, 1 × 106, or 4 × 106 PFU purified WT or gC/gE mutant virus in alternating lanes of the gel to evaluate the relative concentrations of the glycoproteins, including those essential for virus entry, gB, gD, and gH/gL. Analysis of the HSV-1 capsid protein VP5 was included to ensure comparable loading of the WT and gC/gE mutant virus particles on the gel (18). We detected some differences in the relative concentrations of HSV-1 glycoproteins expressed on the WT and the gC/gE mutant viruses; however, concentrations of gB, gD, and gH/gL were slightly higher on the gC/gE mutant than on the WT virus, suggesting that the greater neutralizing activity of the mutant virus is not caused by lower concentrations of target glycoproteins (Fig. (Fig.33).
Another possible explanation for the increased antibody neutralization of the mutant virus is that the mutation in the HSV-1 IgG Fc receptor (FcγR) contributes to the enhanced neutralization. Figure Figure4A4A shows the possible mechanisms by which the HSV-1 FcγR may interfere with antibody neutralization. By binding the Fc domain of IgG, the HSV-1 FcγR on the WT virus may prevent the F(ab′)2 domain from interacting with its target antigen (Fig. (Fig.4A,4A, at the left of the WT model). In contrast, the gE mutation in the gC/gE mutant virus eliminates FcγR activity, which may facilitate interactions between the F(ab′)2 domain and the antibody target, resulting in greater neutralization.
To evaluate this possibility, pooled human IgG was used to compare the neutralization of a gE mutant strain that is defective in FcγR activity with that of a gC mutant virus that has an intact FcγR. If the viral FcγR inhibits neutralization, we postulated that the mutant virus with an intact FcγR would be less neutralized than the mutant virus with a defective FcγR. Viruses were incubated with PBS or 100 μg/ml pooled human IgG as the source of HSV antibodies. Antibody was equally effective at neutralizing the FcγR-intact and the FcγR-defective viruses and was even more active against the gC/gE double-mutant virus (Fig. (Fig.4B).4B). Therefore, a nonfunctional viral FcγR does not explain the increased susceptibility of the gC/gE mutant virus to neutralization mediated by antibody alone. In addition, since the gC/gE double-mutant virus was neutralized more readily than either of the single-mutant viruses from which it was derived, we conclude that the mutations in gC and gE both contribute to increasing the susceptibility of the gC/gE mutant virus to neutralizing antibody.
We next performed assays to compare neutralization of the WT and the gC/gE mutant viruses following incubation with rabbit antibodies that interact with gB, gD, or gH/gL, and as controls, antibodies to gC and gI that are dispensable glycoproteins for virus entry were included. Antibodies to gB and gD and, to a lesser extent, to gH/gL neutralized both viruses in a dose-dependent fashion, while antibodies to gC and gI had little neutralizing activity against either virus (Fig. (Fig.5).5). Surprisingly, we detected minimal differences between the neutralization of the WT virus and that of gC/gE mutant virus by antibodies to gB, gD, or gH/gL, except when anti-gD IgG was used at 30 μg/ml (Fig. (Fig.5C).5C). The results shown were from experiments performed once at each IgG concentration; however, experiments were performed three additional times using anti-gD IgG at 30 μg/ml, and the differences between results for the gC/gE mutant and WT viruses were reproducible (1.5 log10 greater neutralization of the gC/gE mutant than of the WT virus, mean of four determinations; P < 0.01) (results not shown). Experiments were repeated two to three additional times using anti-gB, anti-gD, or anti-gH/gL IgG at 10 μg/ml, which showed no differences between the two viruses (results not shown). Therefore, with the exception of gD at 30 μg/ml, the antibodies to the individual glycoproteins failed to demonstrate differences in neutralization between the two viruses.
Since the human sera used in Fig. Fig.11 and and22 contained antibodies to multiple glycoproteins, we performed neutralization experiments using antibodies in combinations. We combined 5 μg/ml of anti-gB IgG with 5 μg/ml anti-gD IgG, 5 μg/ml anti-gB with 5 μg/ml anti-gH/gL, or 5 μg/ml anti-gD with 5 μg/ml anti-gH/gL and detected much greater neutralization activity of the gC/gE mutant virus than of the WT virus (Fig. (Fig.6).6). This result was striking since, when antibodies were used alone at twofold higher concentrations (10 μg/ml), none of the antibodies showed greater neutralization of the gC/gE mutant virus (Fig. 5A, C, and D). As a control, antibodies to a glycoprotein required for entry were combined with one that is dispensable. Five micrograms of anti-gD IgG per milliliter and 5 μg/ml anti-gI IgG were combined, which showed no enhanced neutralization of the gC/gE mutant virus (Fig. (Fig.6).6). Therefore, the results suggest that the gC and gE mutations expose domains on glycoproteins that interact with one another during the entry process.
An interesting finding in the current study was that gC and gE protected the WT virus from antibody neutralization. Our prior studies failed to detect significant differences between antibody neutralization of the WT virus and that of the gC/gE mutant viruses. A possible explanation for the differing results is that in the prior studies, we intentionally used low antibody concentrations so that the antibody neutralized the WT virus by only ~50% (0.3 log10) (20, 24). This approach enabled us to optimize the assay to detect the added neutralizing effects of complement (20, 24). At low antibody concentrations, neutralization of the gC/gE mutant virus was only slightly greater than that of the WT virus (20). In contrast, the current study used antibody from individual donors at a 1:100 dilution of serum. The range of neutralizing antibody titers in the sera varied, but overall, the neutralizing titers were much higher than in our prior studies, since antibody alone neutralized, on average, ~2 log10 WT virus compared with 0.3 log10. At these higher antibody concentrations, differences between the neutralization of the WT virus and that of the gC/gE mutant virus were readily apparent.
Studies to explain the greater antibody neutralization of the gC/gE mutant than the WT virus demonstrated that fewer glycoprotein targets for neutralizing antibodies on the gC/gE mutant virus or the lack of IgG Fc binding to the mutant virus does not explain the enhanced neutralization. Antibodies that targeted only gB, gD, or gH/gL demonstrated little difference in neutralizing activity against the WT virus or the gC/gE mutant virus; however, when antibodies to these essential entry glycoproteins were used in combinations, we detected enhanced neutralization of the gC/gE mutant virus.
We postulate that the combinations of antibodies prevented the interactions between gB, gD, and gH/gL that are required for virus fusion with cell membranes and subsequent entry of virus into cells. Since neutralization was enhanced by each combination of antibodies to the entry molecules (gB-gD, gB-gH/gL, and gD-gH/gL), our results suggest that gB interacts with gD, gB interacts with gH/gL, and gD interacts with gH/gL. Recently, bimolecular complementation was used to evaluate cell-cell fusion mediated by gB, gD, and gH/gL. The results demonstrated that gB interacts with gD and gD interacts with gH/gL, and when gD binds to its receptor, gB interacts with gH/gL (1). Therefore, our results are entirely consistent with these observations. In addition, our results suggest that to effectively block the interactions between gB, gD, and gH/gL, antibodies must bind to more than one of the entry molecules and that gC and gE on the WT virus provide a shield that prevents the antibodies from interfering with gB-gD, gB-gH/gL, or gD-gH/gL interaction (Fig. (Fig.77).
Anti-gD IgG, when used at 30 μg/ml, was an exception to the requirement for combinations of antibodies that revealed differences between the WT and gC/gE mutant viruses. We postulate that at this high concentration of gD antibody, a critical domain of interaction between gD and either gB or gH/gL was interrupted. Experiments that use monoclonal antibodies targeted to particular domains on gB, gD, or gH/gL will be required to further define the domains of interaction unmasked in the gC/gE mutant virus.
Studies using chemical cross-linkers previously demonstrated that gC forms heterooligomers with gD, gB, and gH/gL, which suggests that gC epitopes are in close proximity to these other glycoproteins (17). Epitope masking of neutralizing domains has been described as an evasion strategy for HIV-1 gp120, in which the gp120 variable domains V1 to V3 shield conserved neutralizing epitopes elsewhere on gp120 (4, 43). Our results extend these findings to include the herpesvirus family and demonstrate masking of neutralizing domains by neighboring glycoproteins.
We previously reported that the HSV-1 FcγR protects the virus by antibody bridging, which blocks functions mediated by the IgG Fc domain, while gC binds C3b to inhibit complement activation (8, 10, 11, 15, 23-26). The current study reveals an additional immune evasion mechanism in which gC and gE prevent antibodies from disrupting the interactions between gB, gD, and gH/gL. The relative importance of these diverse immunity evasion strategies cannot be assessed by the current study; however, based on our prior results, we postulate that the virus may use different mechanisms depending on antibody concentrations (20, 24). Our findings also reveal a novel mechanism for HSV-1 neutralization by suggesting that antibodies prevent interactions between viral glycoproteins required for fusion and entry.
This work was supported by Public Health Service grants AI33063 and T32-AI07324 from the National Institute of Allergy and Infectious Diseases, by DE14152 from the National Institute of Dental and Craniofacial Research, and HL28220 from the National Heart Lung and Blood Institute.
We thank Roselyn Eisenberg and Gary Cohen for providing the rabbit antibodies to gB, gD, gH/gL, and VP5, the University of Pennsylvania Center for AIDS Research clinical core for providing serum from HIV subjects, and Robert Gross for advice on the sample sizes for the various HIV-HSV-1 coinfection cohorts.
Published ahead of print on 14 May 2008.
PubMed Central Canada is a service of the Canadian Institutes of Health Research (CIHR) working in partnership with the National Research Council's national science library in cooperation with the National Center for Biotechnology Information at the U.S. National Library of Medicine(NCBI/NLM). It includes content provided to the PubMed Central International archive by participating publishers.


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(Aladdin Theater, 3017 SE Milwaukie) Earlier this year, Unknown Mortal Orchestra dropped their second album of brain-melting underwater psych-funk, and now the Portland trio plays its first hometown show since the record's release. They've been setting alight stages across the country, and are ready to do the same for a hometown crowd. NED LANNAMANN Also, read our article on UMO.
(Mississippi Studios, 3939 N Mississippi) Low is going on two decades now. The years have flown by for many of us, but it's been a sllooooowww ride for this band from Duluth, Minnesota. Low's association with bands like Codeine and Galaxy 500 earned them the "slowcore" tag from critics, one the band itself doesn't particularly care for. With a few exceptions (and producers), they've never veered too far from that sound. The band's latest, The Invisible Way, was produced by Jeff Tweedy, which makes perfect sense. Like Wilco, it's lush, gorgeous, slow, and inoffensive. Opening is Thalia Zedek, who's also been known to be a little mopey. But her excellent new record Via is noisy in all the right places, and will definitely make you feel good. MARK LORE


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text: I'm looking for a notification tone I had with Ultimate Droid called Soft. It sounds like a sonar bing or a golf club. I forgot to get it before I went to cyanogenmod. Can anyone help me find a place to get it? I can't seem to find it anywhere.


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News aggregator
Dumping Iron in the Pacific Ocean Won't Fix Our Climate - Gizmodo
Phylogenetic placement re-re-visited
Disclaimer: I banged this out fast from existing scripts to help some folks, but haven't tested it yet. Will do that shortly, in the meantime, be careful!
I use phylogenetic placement, namely the program pplacer, in a lot of my publications. It is also a core part of of the paprica metabolic inference pipeline. As a result I field a lot questions from people trying to integrate pplacer into their own workflows. Although the Matsen group has done an excellent job with documentation for pplacer, guppy, and taxtastic, the three programs you need to work with to do phylogenetic placement from start to finish (see also EPA), there is still a steep learning curve for new users. In the hope of bringing the angle of that curve down a notch or two, and updating my previous posts on the subject (here and here), here is a complete, start to finish example of phylogenetic placement, using 16S rRNA gene sequences corresponding to the new tree of life recently published by Hug et al. To follow along with the tutorial start by downloading the sequences here.
You can use any number of alignment and tree building programs to create a reference tree for phylogenetic placement. I strongly recommend using RAxML and Infernal. After a lot of experimentation this combination seems to be produce the most correct topologies and best supported trees. You should be aware that no 16S rRNA gene tree (or any other tree) is absolutely "correct" for domain-level let alone life-level analyses, but nothing in life is perfect. While you're installing software I also recommend the excellent utility Seqmagick. Finally, you will need a covariance model of the 16S rRNA gene to feed into Infernal. You can find that at the Rfam database here.
The workflow will follow these steps:
- Create an alignment of the reference sequences with Infernal
- Create a phylogenetic tree of the alignment
- Create a reference package from the alignment, tree, and stats file
- Proceed with the phylogenetic placement of your query reads
Create an alignment of the reference sequences
The very first thing that you need to do is clean your sequence names of any wonky punctuation. This is something that trips up almost everyone. You should really have no punctuation in the names beyond "_", and no spaces!tr " -" "_" < hug_tol.fasta | tr -d "%\,;():=.\\*[]\"\'" > hug_tol.clean.fasta
Next create an alignment from the cleaned file. I always like to degap first, although it shouldn't matter.## Degap seqmagick mogrify --ungap hug_tol.clean.fasta ## Align cmalign --dna -o hug_tol.clean.align.sto --outformat Pfam 16S_bacteria.cm hug_tol.clean.fasta ## Convert to fasta format seqmagick convert hug_tol.clean.align.sto hug_tol.clean.align.fasta
Build the reference tree
At this point you should have a nice clean DNA alignment in the fasta format. Now feed it to RAxML to build a tree. Depending on the size of the alignment this can take a little bit. I know you've read the entire RAxML manual so of course you are already aware that adding additional cpus won't help…raxmlHPC-PTHREADS-AVX2 -T 8 -m GTRGAMMA -s hug_tol.clean.align.fasta -n ref.tre -f d -p 12345
I like having a sensibly rooted tree; it's just more pleasing to look at. You can do this manually, or you can have RAxML try to root the tree for you.raxmlHPC-PTHREADS-AVX2 -T 2 -m GTRGAMMA -f I -t RAxML_bestTree.ref.tre -n root.ref.tre
Okay, now comes the tricky bit. Clearly you'd like to have some support values on your reference tree, but the Taxtastic program that we will use to build the reference tree won't be able to read the RAxML stats file if it includes confidence values. The work around is to build a second tree with confidence values. You will feed this tree to Taxtastic with the stats file from the tree we already generated.## Generate confidence scores for tree raxmlHPC-PTHREADS-AVX2 -T 8 -m GTRGAMMA -f J -p 12345 -t RAxML_rootedTree.root.ref.tre -n conf.root.ref.tre -s hug_tol.clean.align.fasta
Now we can use the alignment, the rooted tree with confidence scores, and the stats file without confidence scores to create our reference package.taxit create -l 16S_rRNA -P hug_tol.refpkg --aln-fasta hug_tol.clean.align.fasta --tree-stats RAxML_info.ref.tre --tree-file RAxML_fastTreeSH_Support.conf.root.ref.tre
Align the query reads
At this point you have the reference package and you can proceed with analyzing some query reads! The first step is to align the query reads in exactly the same fashion as the reference sequences. This is important as the alignments will be merged later.## Clean the names tr " -" "_" < query.fasta | tr -d "%\,;():=.\\*[]\"\'" > query.clean.fasta ## Remove any gaps seqmagick mogrify --ungap query.clean.fast ## Align cmalign --dna -o query.clean.align.sto --outformat Pfam 16S_bacteria.cm query.clean.fasta
Now we use the esl-alimerge command, included with Infernal, to merge the query and reference alignments.## Merge alignments esl-alimerge --outformat pfam --dna -o query.hug_tol.clean.align.sto query.clean.align.sto hug_tol.refpkg/hug_tol.clean.align.sto ## Convert to fasta seqmagick convert query.hug_tol.clean.align.sto query.hug_tol.clean.align.fast
Phylogenetic placement
Now we're on the home stretch, we can execute the phylogenetic placement itself! The flags are important here, so it's worth checking the pplacer documentation to insure that your goals are consistent with mine (get a job, publish some papers?). You can probably accept most of the flags for the previous commands as is.pplacer -o query.hug_tol.clean.align.jplace -p --keep-at-most 20 -c hug_tol.refpkg query.hug_tol.clean.align.fasta
At this point you have a file named query.hug_tol.clean.align.jplace. You will need to use guppy to convert this json-format file to information that is readable by human. The two most useful guppy commands (in my experience) for a basic look at your data are:## Generate an easily parsed csv file of placements, with only a single placement reported for each ## query read. guppy to_csv --point-mass --pp -o query.hug_tol.clean.align.csv query.hug_tol.clean.align.jplace ## Generate a phyloxml tree with edges fattened according to the number of placements. guppy fat --node-numbers --point-mass --pp -o query.hug_tol.clean.align.phyloxml query.hug_tol.clean.align.jplace
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Another victim of science funding
Or rather the lack thereof. I was very disappointed to receive an email yesterday that BioCyc, a popular database of enzymes and metabolic pathways in model organisms, is moving to a subscription model. The email is posted below in its entirety (to assist in the request to spread the word). With this move BioCyc cements the pattern established several years ago by the Koyoto Encyclopedia of Genes and Genomes (KEGG). I don't begrudge the architects of these databases for moving behind a paywall; as the BioCyc principal investigator Peter Karp notes below, developing and maintaining a high-quality biological database is time and resource intensive, and skilled curators are expensive. I do think however, that moving these resources to a subscription-based model does a disservice to the research community and is not in the public interest. While it was not the responsibility of US funding agencies to ensure the long-term viability and accessibility of KEGG, BioCyc is in their court. In my opinion the failure of NSF and NIH to adequately support community resources amounts to a dereliction of duty.
As noted in the letter below one of the challenges faced by database designers and curators is the tradition of peer review. At its best the peer review process is an effective arbitrator of research spending. I think that the peer review process is at its best only under certain funding regimes however, and suspect that the current low rates of federal funding for science do not allow for fair and unbiased peer review. This is particularly the case for databases and projects whose return on investment is not evident in the short term in one or two high-impact publications, but in the supporting role played in dozens or hundreds or thousands of studies across the community over many years. Program officers, managers, and directors need to be cognizant of the limitations of the peer review process, and not shy away from some strategic thinking every now and again.
My first experience with BioCyc came in my first year of graduate school, when I was tentatively grappling with the relationship between gene and genome functions and the ecology of cold-adapted microbes. Like many academic labs around the country the lab I was in was chronically short on funds, and an academic license for expensive software (e.g. CLC Workbench) or a database subscription (á la KEGG or BioCyc – both were thankfully free back in those days) would have been out of the question. Without these tools I simply would have had nowhere to start my exploration. I fear that the subscription model creates intellectual barriers, potentially partitioning good ideas (which might arise anywhere) from the tools required to develop them (which will only be found in well-funded or specialist labs).
Viva community science!
Dear Colleague,
I am writing to request your support as we begin a new chapter in the development of BioCyc.
In short, we plan to upgrade the curation level and quality of many BioCyc databases to provide you with higher quality information resources for many important microbes, and for Homo sapiens. Such an effort requires large financial resources that — despite numerous attempts over numerous years — have not been forthcoming from government funding agencies. Thus, we plan to transition BioCyc to a community-supported non-profit subscription model in the coming months.
Our Goal
Our goal at BioCyc is to provide you with the highest quality microbial genome and metabolic pathway web portal in the world by coupling unique and high-quality database content with powerful and user-friendly bioinformatics tools.
Our work on EcoCyc has demonstrated the way forward. EcoCyc is an incredibly rich and detailed information resource whose contents have been derived from 30,000 E. coli publications. EcoCyc is an online electronic encyclopedia, a highly structured queryable database, a bioinformatics platform for omics data analysis, and an executable metabolic model. EcoCyc is highly used by the life-sciences community, demonstrating the need and value of such a resource.
Our goal is to develop similar high-quality databases for other organisms. BioCyc now contains 7,600 databases, but only 42 of them have undergone any literature-based curation, and that occurs irregularly. Although bioinformatics algorithms have undergone amazing advances in the past two decades, their accuracy is still limited, and no bioinformatics inference algorithms exist for many types of biological information. The experimental literature contains vast troves of valuable information, and despite advances in text mining algorithms, curation by experienced biologists is the only way to accurately extract that information.
EcoCyc curators extract a wide range of information on protein function; on metabolic pathways; and on regulation at the transcriptional, translational, and post-translational levels.
In the past year SRI has performed significant curation on the BioCyc databases for Saccharomyces cerevisiae, Bacillus subtilis, Mycobacterium tuberculosis, Clostridium difficile, and (to be released shortly) Corynebacterium glutamicum. All told, BioCyc databases have been curated from 66,000 publications, and constitute a unique resource in the microbial informatics landscape. Yet much more information remains untapped in the biomedical literature, and new information is published at a rapid pace. That information can be extracted only by professional curators who understand both the biology, and the methods for encoding that biology in structured databases. Without adequate financial resources, we cannot hire these curators, whose efforts are needed on an ongoing basis.
Why Do We Seek Financial Support from the Scientific Community?
The EcoCyc project has been fortunate to receive government funding for its development since 1992. Similar government-supported databases exist for a handful of biomedical model organisms, such as fly, yeast, worm, and zebrafish.
Peter Karp has been advocating that the government fund similar efforts for other important microbes for the past twenty years, such as for pathogens, biotechnology workhorses, model organisms, and synthetic-biology chassis for biofuels development. He has developed the Pathway Tools software as a software platform to enable the development of curated EcoCyc-like databases for other organisms, and the software has been used by many groups. However, not only has government support for databases not kept pace with the relentless increases in experimental data generation, but the government is funding few new databases, is cutting funding for some existing databases (such as for EcoCyc, for BioCyc, and for TAIR), and is encouraging the development of other funding models for supporting databases [1]. Funding for BioCyc was cut by 27% at our last renewal whereas we are managing five times the number of genomes as five years ago. We also find that even when government agencies want to support databases, review panels score database proposals with low enthusiasm and misunderstanding, despite the obvious demand for high-quality databases by the scientific community.
Put another way: the Haemophilus influenzae genome was sequenced in 1995. Now, twenty years later, no curated database that is updated on an ongoing basis exists for this important human pathogen. Mycobacterium tuberculosis was sequenced in 1998, and now, eighteen years later, no comprehensive curated database exists for the genes, metabolism, and regulatory network of this killer of 1.5 million human beings per year. No curated database exists for the important gram-positive model organism Bacillus subtilis. How much longer shall we wait for modern resources that integrate the titanic amounts of information available about critical microbes with powerful bioinformatics tools to turbocharge life-science research?
How it Will Work and How You Can Support BioCyc
The tradition whereby scientific journals receive financial support from scientists in the form of subscriptions is a long one. We are now turning to a similar model to support the curation and operation of BioCyc. We seek individual and institutional subscriptions from those who receive the most value from BioCyc, and who are best positioned to direct its future evolution. We have developed a subscription-pricing model that is on par with journal pricing, although we find that many of our users consult BioCyc on a daily basis — more frequently than they consult most journals.
We hope that this subscription model will allow us to raise more funds, more sustainably, than is possible through government grants, through our wide user base in academic, corporate, and government institutions around the world. We will also be exploring other possible revenue sources, and additional ways of partnering with the scientific community.
BioCyc is collaborating with Phoenix Bioinformatics to develop our community-supported subscription model. Phoenix is a nonprofit that already manages community financial support for the TAIR Arabidopsis database, which was previously funded by the NSF and is now fully supported [2] by users.
Phoenix Bioinformatics will collect BioCyc subscriptions on behalf of SRI International, which like Phoenix is a non-profit institution. Subscription revenues will be invested into curation, operation, and marketing of the BioCyc resource.
We plan to go slow with this transition to give our users time to adapt. WeÕll begin requiring subscriptions for access to BioCyc databases other than EcoCyc and MetaCyc starting in July 2016.
Access to the EcoCyc and MetaCyc databases will remain free for now.
Subscriptions to the other 7,600 BioCyc databases will be available to institutions (e.g., libraries), and to individuals. One subscription will grant access to all of BioCyc. To encourage your institutional library to sign up, please contact your science librarian and let him or her know that continued access to BioCyc is important for your research and/or teaching.
Subscription prices will be based on website usage levels and we hope to keep them affordable so that everyone who needs these databases will still be able to access them. We are finalizing the academic library and individual prices and will follow up soon with more information including details on how to sign up. We will make provisions to ensure that underprivileged scientists and students in third-world countries arenÕt locked out.
Please spread the word to your colleagues — the more groups who subscribe, the better quality resource we can build for the scientific community.
Peter Karp
Director, SRI Bioinformatics Research Group
[1] http://www.nature.com/nature/journal/v527/n7576_supp/full/527S16a.html
[2] http://database.oxfordjournals.org/content/2016/baw018.long


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Happy carving


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By guyshithappensto - / Saturday 22 May 2010 02:41 / United States
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Top comments
Good to know. Fat FMLs are funny! Ugh.
Ms_Jessie22 | 8
Oh geez OP, you should def work on that :/
WingsFan80 | 4
lose weight time
Littlemuffinbox | 6
Uhh.. That might be a problem. Could you imagine actually swimming in fat? That'd be pretty nasty xD
Well fat can be pretty liquidy. My cats fat flops around like a water balloon and feels like pudding.
Dammit op. You're not helping this fat Amurican stereotype.
chip_twoseven | 0
YDI for being fat
nbspike3_fml | 0
agree with Jess ydi
lovej4ever | 0
hahaha win for the family Guy reference #1 :)
Valentina_Baby | 7
this made me giggle :]
yokotaneko | 0
um, actually jdub, you're quite wrong. It's called dry drowning, and it is very possible. way to make yourself look stupid whilst calling an intelligent person stupid.
suppressed08 | 2
I don't have fat arms, and that's happened to me once or twice. so OP might not be THAT fat. still deserves it though :P
ladiesman14 | 0
did u mean u almost drowned in your drool while being suffocated by your arm fat ? i guess thats possible.
Ms_Jessie22 | 8
39- How about this: you STFU! I'm tired of you harrassing me on every FML. I like my pic and I'm not changing it, so leave me the fuck alone.
Giorgio272 | 2
another I am fat fml. so boring, lose some weight and get laid. NEXT FML.
jadedwaitress | 0
I hit ydi the moment I saw that OP fell asleep in class. Yes, I understand school is not always the most interesting thing, but even on 36 hours without sleep I wouldn't fall asleep in class.
kirbcheck76 | 3
I like the new pic Ms Jess
melissamoshh | 0
ewww I had a teacher with arm fat and I sat next to the board so her jiggle would just like, hang in my face...
chemqueen20 | 0
for yoko; Dry drowning occurs when a person's lungs become unable to extract oxygen from the air, due primarily to: Muscular paralysis Puncture wound to the torso (affecting ability of diaphragm to create respiratory movement) Changes to the oxygen-absorbing tissues Persistence of laryngospasm when immersed in fluid Prolonged exposure to any gas that is not inherently toxic, but that displaces oxygen from the lungs. (e.g. methane) Overdose of free water (solute free) which leads to decreased sodium in the blood hyponatremia which leads to massive swelling in the brain. The person may effectively drown without any sort of liquid. In cases of dry drowning in which the victim was immersed, very little fluid is aspirated into the lungs. The laryngospasm reflex essentially causes asphyxiation and neurogenic pulmonary edema (œdema). Dry drowning can occur clinically, or due to illness or accident. I don't think the OP was dry drowning or it'd be a more serious health problem. it was more like suffocating. sooo, do you're research before you try to make other people feel stupid ;D
zakkyzebra | 11
now I see why treadmills were made. for fat fucks like you. get on one
deannamarie12 | 0
Hmm, if that's a problem OP, hit the gym.
smmrgrl | 0
umm she doesn't HAVE to be fat.. I mean some girls say ooo i'm so fat and they're actually very very skinny. on top of that I'm really skinny (according to wii fit I'm "underweight" bah all lies xD I'm normall) anyways..and I've drowned or suffocated or w.e you wanna call it in my own fat....
IslandLove | 0
lol fat fmls are funny
Gorsbug823 | 0
what's your problem 39
cherrypieguy | 0
you didn't drown you asphexiated
Rambo881xx | 0
it's possible while being unconsious to accedently close your oral cavety with your head on your arm
No this could be true I've almost cut off my breathing with my arm accidently and I weigh less than 120 lbs.
myownenemy | 0
you can drown in any liquid, dumbass.
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Dandruff (Seborrhea)
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Share house
Share house
3 Bedrooms
3 Beds
2 Bathrooms
2 Baths
|Room Type
|Private room
|Shared bathroom
|Length of Stay
|Minimum 6 months
|Anyone welcome
|Weekly rent
|4 weeks rent
|Not included in rent
|Available but not included in rent
|Off street parking
Large room in new modern extension, with loads of cupboard space. Ducted heating and aircon, modern kitchen. Large open plan living area. Sunny private yard - landscaped, lawn mowing included in rent, utilities and internet not included. Close to park, train, tram, eastern freeway and shops. Sharing with Mel (Melissa), a 30 yr old landscape gardener and Amanda, a school teacher. This house will suit a discerning person who likes a quiet area and a quality house to live in. Preferably somebody who works full time. Sorry, no couples or pets. Excellent coffee place at end of street and best pizza in Melbourne close at hand. Bedroom has built in robes, you will need your own bed. Non smoker please. Please phone Amanda for more details or to arrange a time to visit.
I live up the front in the older section of the house, you share the new back section.
off street parking available.
minimum stay 6 months
Prefer someone aged between 25 and 45


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|19 Jul 2016
Microsoft Windows 10 Pro 64-bit Multiprocessor
Problem installing new PSU
My PC suddenly started to power off intermittently. After much googling I decided the problem was probably with my 10 year old Trust PSU so I bought a new Corsair VS550. Having installed the new unit, to my dismay when I switched on absolutely nothing happened - the system was dead as a dodo. All suggestions for solution gratelfully received. Have been unable to find UK (or any) phone number for Corsair. Anyone know one?
Windows 7 home premium SP1, Foxonn motherboard M61PMV, Corsair VS550 PSU
|My System Specs
|19 Jul 2016
Windows 7 Home Premium 64 bit sp1
The first thing to check is whether all leads are plugged in & fully seated. Also make sure all leads are plugged into the correct sockets. It often needs quite a hard push to get some of the plugs to seat properly.
The last Corsair PSU that I bought had instructions on the box showing what all leads are for & where they should go.
My Corsair PSU has a power switch on it, so be sure that is switched on.
|My System Specs
|19 Jul 2016
Windows 7 Professional 64bit
Are you sure that the outlet isn't at fault?
|My System Specs
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problem when installing CFW (64-bit)
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hi i just built a new pc when i try to do a custom install there is no hard drive detected but it is detected in my bios although when loading into the bios it says smart capable but command failed my system processor - 1055t amd phenom II x6 motherboard- msi 870a fuzion graphic card-2 his...
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text:
Independence Daily Reporter, Monday, May 9, 1910, Pg. 5:
William McDougall, well known in Montgomery county, died at his home in Cherryvale yesterday. Mr. McDougall was born in New York, Dec. 16, 1834, and was 75 years, four months and twelve days.
He is survived by his wife and two daughters, Mrs. Jeff Griffin and Mrs. Elmer Newton and one son, William McDougall of Idaho.
For many years he has been a faithful member of the United Brethren church of Coal Creek and also a member of the Independence Post of the Grand Army of the Republic, comrades of which will act as pall bearers.
The funeral services will be conducted by Rev. C. H. Jones at Mount Hope cemetery on Wednesday morning about 11 o'clock, the body arriving at the cemetery via 10:25 interurban car.
South Kansas Tribune, Wednesday, May 11, 1910, Pg. 5:
Death came to Comrade W. J. McDougall at his home in Cherryvale, Sunday morning, after a long illness in his 76th year.
Comrade McDougall was born in New York state, Dec. 16, 1834. While a young man he came West, and when President Lincoln called for men he was in Colorado and heeded the call enlisting in the Second Colorado Volunteers. Early in '70 or '71 he came to this county and got a claim southeast of Independence a few miles, where he was ever known as a first-class, public spirited citizen. In 1887 he was converted and became a member of the United Brethren church at Coal Creek and ever lived a Christian life. In latter years he had much sickness and at one time Elder Jones was called, and to him he expressed not only his faith but his readiness to go and be with the Master. After his recovery and not being able to work on the farm Mr. and Mrs. McDougall bought property and moved to Cherryvale where he has been confined to his home most of the time, anxiously waiting the summons. It was his request that his comrades of the McPherson Post have charge of the interment and that his former faithful pastor, Rev. C. H. Jones speak to the living at the funeral.
The remains were brought over from Cherryvale this morning and the procession followed it from the trolley line to Mount Hope, where Brother Jones made a short address and he was laid to rest with the honors of the Grand Army of Republic.
He is survived by his widow, two daughters, Mrs. Jeff Griffin of this vicinity, Mrs. Elmer E. Newton of Argentine, and one son, William McDougall of Joseph, Idaho.
Contributed by Mrs. Maryann Johnson
a Civil war researcher and a volunteer in the Kansas Room of the Independence
Public Library, Independence, Kansas.
Contributed by Mrs. Maryann Johnson a Civil war researcher and a volunteer in the Kansas Room of the Independence Public Library, Independence, Kansas.


text:
Research Assistant Professor and Extension Specialist
- Emma Lookabaugh, Ph.D. Dissertation topic: Production factors that influence the interaction between Pythium aphanidermatum and poinsettia in commercial greenhouse systems
- Michael Cannon, M.S. Thesis topic: Yield loss due to Sclerotinia blight of peanut
- Amy Taylor, Master of Plant Pathology
- Chutsuda Junsopa, visiting scholar from Khon Kaen University, Thailand
- Emma Lookabaugh, M.S. 2013. Thesis title: Understanding the impact of Pythium species on floricultural crops in North Carolina
- Sarah Rurak, M.S. 2009. Thesis title: Evaluation of Biological and Other Novel Seed and Soil Treatments for Organic Peanut Production. Current position: Ph.D. student, Cornell University
- Damon Smith, Ph.D. 2007, M.S., 2004. Thesis title: Biology and Epidemiology of Sclerotinia minor on Peanut (Arachis hypogaea L.). Current position: Assistant Professor, University of Wisconsin
- Laura Duffie, M.S. 2003. Effects of intercropping corn and peanut on peanut leaf spot management and the spatial and temporal epidemiology of Cercospora arachidicola. Current position: USDA-APHIS
1976 B.S. Plant Pathology, Colorado State University
1980 M.S. Plant Pathology, North Carolina State University
1983 Ph.D. Plant Pathology, North Carolina State University
Pythium in Floricultural Crops (Emma Lookabaugh)
North Carolina is a major producer of floricultural crops and Pythium is frequently diagnosed on floricultural samples submitted to the Plant Disease and Insect Clinic (PDIC). Greenhouses in North Carolina previously had not been systematically sampled for the presence of Pythium. The severity of the problem, the Pythium species involved, and the extent of mefenoxam resistance in greenhouse populations were unknown. To address these questions, graduate student Emma Lookabaugh collected herbaceous ornamentals exhibiting symptoms of Pythium root rot from 18 greenhouses in 14 counties in North Carolina. Isolates were identified to species by sequencing of the ITS rDNA region. More than half of the 277 isolates collected were resistant to mefenoxam. Resistant and sensitive strains were found within the same greenhouse and species. We plan to use the results of this research to provide mefanoxam resistance screening services to growers through the Plant Disease and Insect Clinic.
Peanut diseases
Peanuts are grown on about 90,000 acres in North Carolina. The crop is affected by several serious diseases, including leaf spots, southern stem rot, Sclerotinia blight, Cylindrocladium black rot, and Spotted wilt. My research aims to develop integrated disease management tactics that take advantage of host resistance and weather-based disease advisories to minimize the use of fungicides and other pesticides in peanut production. Currently, I am focusing on developing reduced input disease control methods that can be used on the new partially resistant cultivars Bailey, Sugg, Sullivan and Wynne. I work with peanut breeder Dr. Tom Isleib in evaluation of disease resistance in new breeding lines. I also work with Dr. David Jordan to understand the impacts of cultural practices on disease development and crop health.
Extension & Outreach
Plant Disease and Insect Clinic
I serve as the Director of the Plant Disease and Insect Clinic at NCSU. The clinic is staffed with two full-time plant disease diagnosticians, Shawn Butler and Mike Munster, and full-time entomologist, Matt Bertone. Graduate student Emma Lookabaugh diagnoses diseases of tomatoes and other crops. The clinic provides diagnostic training for County Agents and Master Gardeners and uses social media (Facebook, Twitter, and Blog) for outreach to a wide audience of Extension personnel, farmers, nurseries, and homeowners.
As part of a team that includes Dr. David Jordan in Crop Science, Dr. Rick Brandenburg in Entomology, and county extension personnel, I have extension responsibilities for peanut diseases. We prepare educational materials, conduct field testing, and participate in grower meetings, demonstrations and field days. In addition, in cooperation with the North Carolina State Climate office, I provide daily peanut disease advisories for peanut growers in North Carolina.
Peanut Information
Agricultural Chemicals Manual
Peanut Risk Management
Peanut Disease Photos
Peanut Disease Advisories -click on this link to view today's weather based disease advisories and for information on how to interpret advisories. You may contact Dr. Shew to receive daily advisory emails.
Peanut Scouting Manual – IPM Center
Selected Publications
Junsopa, C., Jogloy, S., Saksirirat, W., Songsri, P, Kesmala, T., Pathanothai, A., Shew, B.B. 2016. Inoculation with Sclerotium rolfsii, cause of stem rot in Jerusalem artichoke, under field conditions. Eur. J. Plant Pathology Doi 10.1007/s/0658-016-089-1
Boudreau, M.A., B. B. Shew, and L.E. Duffie. 2015. Impact of intercropping on epidemics of groundnut leaf spots: defining constraints and opportunities through a 7-year field study. Plant Pathology Doi 10.1111/ppa.12440.
Lookabaugh, E.C., Ivors, K.M., Shew, B.B. 2015. Mefenoxam sensitivity, aggressiveness, and identification of Pythium species causing root rot on floriculture crops in North Carolina. Plant Disease 99:1550-1558.
Isleib, T.G., Milla-Lewis, S.R., Pattee, H.E., Copeland, S.C., Zuleta, M.C., Shew, B.B., Hollowell, Sanders, T.H., Dean, L.O. Hendrix, K.W., Balota, M., Chapin, J.W., and Monfort, W.S. 2015. Registration of 'Sugg' Peanut. J. Crop Regist. 9:44-52
Jordan, D.L., P. D. Johnson, T. Corbett, J. Schultheis, B. Shew, R. Brandenburg, W. Ye. 2014. Peanut response to crop rotations including clary sage, snap bean, and sweet potato. Crop Manag. doi:10.2134/CM-2014-0038-RS
Drake, W.L., D. L. Jordan, P. D. Johnson, B. B. Shew, R. L. Brandenburg, T. Corbett. 2014. Peanut response to planting date, tillage, and cultivar in North Carolina. Agronomy Journal 106: 486-490
Isleib, T.G., B.B. Shew, S.R. Milla-Lewis, W.B. Dong, S.C. Copeland, C. Arellano. 2013. Stability analysis of incidence of tomato spotted wilt in virginia-type peanut cultivars and breeding lines. Peanut Sci. 40:24-30.
Chahal, G.S., D.L. Jordan, B.B. Shew, R.L. Brandenburg, J.D. Burton, and D. Danehower. 2012. Interactions of Agrochemicals Applied to Peanut; Part 2: Effects on Fungicides. Crop Protectionhttp://dx.doi.org/10.1016/j.cropro.2012.05.008
Partridge-Telenko, D.E., J. Hu, D. M. Livingstone, B. B. Shew, P. M. Phipps, and E. A. Grabau. 2011. Sclerotinia Blight Resistance in Virginia-Type Peanut Transformed with a Barley Oxalate Oxidase Gene. Phytopathology 101: 786-793.
Ruark, S.J., and Shew, B.B. 2010. Evaluation of microbial, botanical, and organic treatments for control of peanut seedling diseases. Plant Dis. 84:445‐454.
Isleib, T.G., Milla-Lewis, S.R., Pattee, H.E., Copeland, S.C., Zuleta, M.C., Shew, B.B., Hollowell, J.E., Sanders, T.H., Dean, L.O., Hendrix, K.W., Balota, M. 2010. Registration of Bailey Peanut. Journal of Plant Registrations 5:1-13.
Carley, D.S., Jordan, D.L., Shew, B.B., Sutton, T.B., Dharmasri, L.C., and Brandenburg, R.L. 2009. Influence of Digging Date and Fungicide Program on Canopy Defoliation and Pod Yield of Peanut (Arachis hypogaea L.). Peanut Science 36:77‐84.
Jordan, D. L., Fisher, L. R., Shew, B. B., Marshall, T., Johnson, P. D., Ye, W., and Brandenburg, R. L. 2009. Comparison of cropping systems including corn, peanut, and tobacco in the North Carolina Coastal Plain. Crop Management doi:10.1094/CM‐2009‐0612‐01‐RS.
Smith, D.L., Garrison, M.C., Hollowell, J.E., Isleib, T.G., and Shew, B.B. 2008. Evaluation of application timing and efficacy of the fungicides fluazinam and boscalid for control of Sclerotinia blight of peanut. Crop Protection 27:823‐833.
Hollowell, J.E., Isleib, T.G., Tallury, S.P., Copeland, S.C. and Shew, B.B. 2008. Screening of virginia‐type peanut breeding lines for resistance to Cylindrocladium Black Rot and Sclerotinia Blight in the greenhouse. Peanut Science 35: 18‐24.
Cantonwine, E.G., A. K. Culbreath, B. B. Shew, and M. A. Boudreau. 2008. Efficacy of organically acceptable fungicides for management of early and late leaf spot of peanut. Plant Health Progress doi:10.1094/PHP‐0317‐03‐RS.
Jordan, D.L., B.B. Shew, J.S. Barnes, T. Corbett, J. Alston, P.D. Johnson, W. Ye, and R.L. Brandenburg. 2008. Pest reaction, yield, and economic return of peanut cropping systems in the North Carolina coastal plain. Crop Management doi:10.1094/CM‐2008‐1008‐01‐RS.
Jordan, D.L., J.S. Barnes, T. Corbett, C.R. Bogle, P.D. Johnson, B.B. Shew, S.R. Koenning, W. Ye, and R.L.Brandenburg. 2008. Crop response to rotation and tillage in peanut‐based cropping systems.Agron. J. 100:1580‐1586.
Smith, D.L, J.E. Hollowell, T.G. Isleib, and B. B. Shew. 2007. A site‐specific, weather‐based disease model for Sclerotinia blight of peanut. Plant Dis. 91:1436‐1444.
Isleib, T.G., P.W. Rice, S.C. Copeland, R.W. Mozingo II, J.B. Graber, B. Shew, D.L. Smith, H. Melouk, and H.T. Stalker. 2006. Registration of N96076L peanut germplasm. Crop Sci. 46:2329‐2330.
Smith, D.L., J.E. Hollowell, T.G. Isleib, and B.B. Shew. 2006. Analysis of factors that influence the epidemiology of Sclerotinia minor on peanut. Plant Dis. 90:1425‐1432.
Hollowell, J.E. and B.B. Shew. 2005. First Report of Sclerotinia minor on Allium vineale in North Carolina. Plant Dis. 89:908. Published on‐line as DOI: 10.1094/PD‐89‐0908C.
Hollowell, J.E. and B. B. Shew. 2005. First Report of Sclerotinia minor on Sida spinosa in North Carolina. Plant Dis. 89:1128. Published on‐line as DOI: 10.1094/PD‐89‐1128A.
J.E. Hollowell and B.B. Shew. 2004. First report of Carolina geranium as a host of Sclerotinia minor. Plant Disease 88: 312.
J.E. Hollowell and B.B. Shew. 2004. First report of common chickweed as a host of Sclerotium rolfsii. Plant Disease 88: 426.
Hollowell, J.E., B.B. Shew, M.A. Cubeta, and J.W. Wilcut. 2003. Weed species as hosts of Sclerotinia minor in peanut fields. Plant Disease 87:198‐199.
Hollowell, J.E., B.B. Shew, and T.G. Isleib. 2003. Evaluating isolate aggressiveness and host resistance from peanut leaflet inoculations with Sclerotinia minor. Plant Disease 87:402‐406.
Lemay, A.V., J.E. Bailey, and B.B. Shew. 2002. Resistance of peanut to Sclerotinia blight and the effect of acibenzolar‐S‐methyl and fluazinam on disease incidence. Plant Disease 86: 1315‐1317.
Stalker, H.T., M.K. Beute, B.B. Shew, and K.R. Barker. 2002. Registration of two root‐knot nematoderesistantpeanut germplasm lines. Crop Sci. 42:312‐313.
Stalker, H. T., M. K. Beute, B. B. Shew, and T. G. Isleib. 2002. Registration of five leaf spot‐resistant peanut germplasm lines. Crop Sci. 42:314‐316.
Selected Technical Reports
Shew, B.B. 2015. Response of peanut diseases in North Carolina to spray programs with labeled fungicides, 2014. Plant Dis. Mgt. Rep. 9
Shew, B.B. 2015. Response of peanut diseases in North Carolina to in-furrow inoculation and fungicide applications, 2014. Plant Dis. Mgt. Rep. 9
Shew, B.B. 2014. Evaluation of Abound, Convoy, and Folicur for stem rot control on stevia in North Carolina, 2014. Plant Dis. Mgt. Rep. 9
Shew, B.B. 2013. Evaluation of experimental fungicides for peanut disease control in North Carolina, 2013. Plant Dis. Mgt. Rep. 8
Shew, B.B. 2011. Evaluation of Abound plus Alto for control of peanut diseases in North Carolina, 2011. Plant Dis. Mgt. Rep. 6
Shew, B.B. 2011. Evaluation of Fontelis and Topguard for control of peanut diseases in North Carolina, 2011. Plant Dis. Mgt. Rep. 6
Shew, B.B. 2011. Evaluation of spray programs with labeled fungicides for the control of peanut diseases in North Carolina, 2012. Plant Dis. Mgt. Rep. 6
Shew, B.B., B.B. 2010. Evaluation of Topguard and other fungicides for the control of peanut diseases in North Carolina, 2009. Plant Dis. Mgt. Rep. 4
Shew, B.B., B.B. 2010. Evaluation of in-furrow and foliar fungicides for control of peanut diseases in North Carolina, 2009. Plant Dis. Mgt. Rep. 4


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