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Spa in New Orleans, Louisiana with Reviews & Ratings - YP.comFind People•Advertise With UsBrowseFind PeopleFeatured CollectionsRestaurantsAutomotiveHome ImprovementHealth & WellnessAttorneysPeople Searched For...Childrens Hospital Adolescent Behavioral Health UnitHotel MonteloneFire Water Damage RestorationBurglar Alarm CompaniesDental Assistant SchoolsCriminal Law AttorneysPersonal Injury Law AttorneysSelf StorageNursing SchoolsTerminixPrinting ServicesMold Testing ConsultingMedical Assistant SchoolsDentistsPest Control ServicesHair ReplacementMoversBmw DealershipVirtual Office SpaceTicketmasterAmtrak Train StationLowesCna ClassesAdvertise with usWe have plenty of solutions to help you grow your businessWhat do you want to find?Search by business name, or keywordnearWhere? Address, ZIP Code, or NeighborhoodMy current locationSearchSign In•JoinHomeNew Orleans, LASpaNew Orleans SpaSort:Most RelevantMost RelevantDistanceRatingName (A - Z)FiltersFiltersMore NeighborhoodsAlgiersAudubonBayou St. JohnBehrmanBlack PearlBywaterCentral Business DistrictCentral CityCentral City - GardenCity ParkDillardEast CarrolltonEast RiversideFairgroundsFrench QuarterFrench Quarter - CBDFrench Quarter - CbdFreretGentillyGentilly TerraceLakeviewLeonidasLower Garden DistrictMarignyMid-CityNew Orleans East AreaTall Timbers - BrechtelUptownUptown - CarrolltonWest RiversideDoneClear AllMore CategoriesAromatherapyBarbersBeauty SalonsBody Wrap SalonsChiropractors & Chiropractic ServicesCosmetics & PerfumesCosmetologistsDay SpasHair BraidingHair RemovalHair StylistsHair Supplies & AccessoriesHealth ClubsHealth ResortsMake-Up ArtistsMassage ServicesMassage TherapistsMedical SpasNail SalonsPhysicians & SurgeonsSkin CareSpas & Hot TubsSports Medicine & Injuries TreatmentSwimming Pool 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services collectionInaccurate Result?11.Peaceful Buddha Day Spa4145 Canal StNew Orleans, LA 70119(504) 322-2482Day SpasNail SalonsMassage TherapistsWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?12.Fifth Element Spa1215 N Broad StNew Orleans, LA 70119(504) 483-7722Day SpasMedical SpasBeauty SalonsWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?13.Spa ZeebaServices5926 Magazine StNew Orleans, LA 70115(504) 302-9643Day SpasMedical SpasBeauty SalonsWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?14.A Touch of Beauty Day Spa7701 Hampson StNew Orleans, LA 70118(504) 865-1318Day SpasBeauty SalonsWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?15.Halo Suites Day SpaServices3863 Gentilly Blvd.New Orleans, LA 70122(504) 218-7456Day SpasMake-Up ArtistsHair RemovalWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?16.Spa AtlantisServices(4)740 Gravier StNew Orleans, LA 70130(504) 566-8088Day SpasBeauty SalonsCosmetologistsWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?17.Planet BeachServicesView all 16 Locations301 Burgundy StNew Orleans, LA 70112(504) 525-8266Day SpasTanning SalonsSkin CareWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?18.Aveda Paris Parker Salon & SpaServices(2)4900 Prytania StNew Orleans, LA 70115(504) 891-8874Day SpasMedical SpasHair StylistsWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?19.Serenitea-Relax105 Tchoupitoulas StNew Orleans, LA 70130(626) 863-4501Day SpasMedical SpasWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?20.Shine Spa And Specialties421 N Carrollton AveNew Orleans, LA 70119(504) 486-0999Day SpasMedical SpasHealth ResortsDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?21.Bonus Image Aesthetics Apm6042 Magazine StNew Orleans, LA 70118(504) 909-1490Day SpasMedical SpasSkin CareDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?22.Jardin De Beaute1521 Saint Charles AveNew Orleans, LA 70130(504) 247-0037Day SpasBeauty SalonsDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?23.RMDs Aesthetics & Med Spa225 N Jefferson Davis PkwyNew Orleans, LA 70119(504) 486-7070Day SpasBeauty SalonsDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?24.One On One Day Spa5961 Bullard Ave #2New Orleans, LA 70128(504) 324-3596Day SpasBeauty SalonsMassage TherapistsDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?25.Amore Therapeutics504 Elmira AveNew Orleans, LA 70114(504) 701-4575Day SpasMassage TherapistsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?26.Royal Nubian Skincare StudioNew Orleans, LA 70119(504) 373-0573Day SpasHair RemovalMassage TherapistsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collection27.The Woodhouse Day Spa - New Orleans, LAServices(3)4030 Canal St.New Orleans, LA 70119(504) 482-6652Day SpasBeauty SalonsHair RemovalWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?28.Family Nails and SPaServices4829 prytania st.New Orleans, LA 70115(504) 896-1005Day SpasBeauty SalonsNail SalonsWebsiteDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?29.Le Visage Day Spa(1)8110 Hampson StNew Orleans, LA 70118(504) 265-8018Day SpasBeauty SalonsNail SalonsDirectionsMore InfoRooms & Rates »Add to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collection30.Nola Bliss MassageServices1717 Pauger St.New Orleans, LA 70116(504) 615-9414Day SpasMassage TherapistsWebsiteDirectionsMore InfoRooms & Rates »Sponsored LinksShowing1-30
of 206results12345NextIf we're missing a business and you'd like to make a suggestion, please do! Add a business.Add a New CollectionOops! There was a problem saving the new custom collection.Please try again.Collection Name cannot be emptyUpload a Photo(optional)Remaining Characters: 100Remaining Characters: 500CancelSaveMap ViewFeatured Day Spasin New Orleans, LouisianaAdd to mybookRemove from mybookAdded to your travel collection!Error when adding to travel collectionThis business was removed from the travel collectionInaccurate Result?Hotel Monteleone(16)214 Royal StNew Orleans, LA 70130(504) 434-4137Luxury in the French QuarterWebsiteReservationsDirectionsMore InfoAdd to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?Georgy's Salon & Spa701 W Esplanade Ste A AveKenner, LA 70065(504) 229-6101Creating A New Style With HairWebsiteCouponsServices OfferedDirectionsMore InfoAdd to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?Timeless Beauty Day Spa and Salon(1)3422 Cleary AveMetairie, LA 70002(504) 371-5680WebsiteDirectionsMore InfoAdd to mybookRemove from mybookAdded to your health collection!Error when adding to health collectionThis business was removed from the health collectionInaccurate Result?Spa Aria214 Royal StNew Orleans, LA 70130(504) 613-0697WebsiteDirectionsMore InfoAdd to mybookRemove from mybookAdded to your health collection!Error when adding to health collectionThis business was removed from the health collectionInaccurate Result?Center For Longevity & Wellness The(1)3601 Houma BlvdMetairie, LA 70006(504) 885-7360Contact Us For InformationWebsiteDirectionsMore InfoAdd to mybookRemove from mybookAdded to your services collection!Error when adding to services collectionThis business was removed from the services collectionInaccurate Result?Pennys Brazilian Wax & Spa(2)4221 S Carrollton AveNew Orleans, LA 70119(504) 941-7552Pennys Brazilian Wax & Spa offer the best prices i...YP AdDirectionsMore InfoSponsored New Orleans SpaPhoneWebsiteMoreAboutAbout UsSite FeedbackContact UsAdvertise with UsCareers - We're HiringEngineering BlogLegal

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1 selected item: 18039987
Arch Intern Med. 2007 Nov 26;167(21):2296-303.
Grover SA1, Lowensteyn I, Joseph L, Kaouache M, Marchand S, Coupal L, Boudreau G; Cardiovascular Health Evaluation to Improve Compliance and Knowledge Among Uninformed Patients (CHECK-UP) Study Group.
McGill Cardiovascular Health Improvement Program and the Divisions of General Internal Medicine and Clinical Epidemiology, The Montreal General Hospital, Department of Medicine, McGill University, Montreal, Canada. steven.grover@mcgill.ca
Despite increasing evidence that treating dyslipidemia reduces cardiovascular events, many patients do not achieve recommended lipid targets.
To determine whether showing physicians and patients the patient's calculated coronary risk can improve the effectiveness of treating dyslipidemia in a primary care setting, patients were randomized to receive usual care or ongoing feedback regarding their calculated coronary risk and the change in this risk after lifestyle changes, pharmacotherapy, or both to treat dyslipidemia. Outcomes, based on intention-to-treat analysis, included changes in blood lipid levels, coronary risk, and the frequency of reaching lipid targets.
Two hundred thirty primary care physicians enrolled 3,053 patients. After 12 months of follow-up, 2,687 patients (88.0%) remained in the study. After adjustment for baseline lipid values, significantly greater mean reductions in low-density lipoprotein cholesterol levels and the total cholesterol to high-density lipoprotein cholesterol ratio were observed in patients receiving risk profiles (51.2 mg/dL [to convert to millimoles per liter, multiply by 0.0259] and 1.5, respectively) vs usual care (48.0 mg/dL and 1.3, respectively), but the differences were small (-3.3 mg/dL; 95% confidence interval [CI], -5.4 to -1.1 mg/dL; and -0.1; 95% CI, -0.2 to -0.1, respectively). Patients in the risk profile group were also more likely to reach lipid targets (odds ratio, 1.26; 95% CI, 1.07 to 1.48). A significant dose-response effect was also noted when the impact of the risk profile was stronger in those with worse profiles.
Discussing coronary risk with the patient is associated with a small but measurable improvement in the efficacy of lipid therapy. The value of incorporating risk assessment in preventive care should be further evaluated.
Prediction is difficult, particularly about the future. [Arch Intern Med. 2007]
Using cardiovascular age equivalent to close the treatment gap for dyslipidemia. [Arch Intern Med. 2007]
Informing patients of their coronary risk. [Arch Intern Med. 2008]
10.1001/archinte.167.21.2296

type: global

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Transfer of property through GPA from Monday | delhi | Hindustan Times
Transfer of property through GPA from Monday
Updated: Jul 19, 2013 23:32 IST
Delhi residents will be able to transfer and register properties on general power of attorney (GPA) from next week. At a function in Nangloi on Friday, Chief Minister Sheila Dikshit announced that the Delhi government had decided to allow registration of properties through GPA “most likely from Monday”. Lakhs of people living in co-operative housing societies and Delhi Development Authority flats will benefit from this order.
In May 2013, the Delhi High Court struck down an internal circular of the state government issued in April, 2012, which restricted property transactions through GPA. On October 12, 2011, the apex court had ruled that sale transactions carried in the name of GPA will have no legal sanctity and immovable property can be sold or transferred only through registered deeds. Following the order, the Delhi government had put a stop on property transactions through GPA in April last year. “The Delhi government circular banning sale of properties on GPA was set aside by the high court in May this year. After taking the opinion of the law and revenue departments, the government finally sent the proposal to the Lieutenant Governor for his consent and notification,” a senior Delhi government official said. The revenue department’s circular stated: “No transfer of property will take place until a clear sale deed is executed and duly registered by the executants in the office of the registrar/sub-registrar.”
Transaction through GPA was common for properties without a clear title. more from delhi

value: This website is an Indian English-language daily newspaper introduced and founded in 1924 by Sunder Singh Lyallpuri, founder-father of the Akali movement and the Shiromani Akali Dal in the Punjab Province. It played integral roles in the Indian independence movement as a nationalist daily.


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Lorraine Allen Condolences | Sign the Guest Book | Bloomfield-Cooper Jewish Chapels in partnership with the Dignity Memorial network
Restore Guest Book for Lorraine Allen

value: This website is a United States-based website founded in 1998, the world's largest commercial provider of online memorials. The Web site hosts obituaries and memorials for more than 70 percent of all U.S. deaths.


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Gunderson Dedicates Habitat Roof Pilot Project -- PORTLAND, Ore., June 1, 2011 /PRNewswire/ --
Gunderson Dedicates Habitat Roof Pilot Project
PORTLAND, Ore., June 1, 2011 /PRNewswire/ -- Commissioner Dan Saltzman presided over the dedication of Gunderson LLC's new Habitat Roof pilot project yesterday morning at its Portland manufacturing site on NW Front Avenue. The 1,000 square foot roof is believed to be the first of its kind in the surrounding industrial area and will be used to study the feasibility of creating habitat value on such roofs. The roof was fabricated and erected by Gunderson employees and received its inspiration from Bureau of Environmental Services activities in this area.
Mark Eitzen, general manager and vice president of Gunderson LLC, said, "We could not have completed the project without guidance from the Ecoroof Program at the Bureau of Environmental Services and the accelerated building permit process facilitated by the Bureau of Development Services, which allowed us to take advantage of the current growing season. Technical assistance was received from the dedicated members of the local Greenroof Info Think-Tank (GRiT). We are excited to help lead the way in measuring habitat value created by such roofs and hope to apply the lessons learned to the 900,000+ square feet of existing roof at Gunderson."
In his dedication presentation, Commissioner Saltzman said, "We are happy that our bureaus could support this positive example of promoting improvement in the environment and supporting business objectives at Gunderson. We hope that we can continue working together to create many more such opportunities at Gunderson and elsewhere at industrial sites." Gunderson will commence construction on the second phase of the pilot project this summer. The second phase will be approximately 2.5 times larger than the first phase. About Gunderson LLC
Gunderson, located on a deepwater facility on the Willamette River, currently employs over 700 personnel. The Company recently celebrated its twenty-fifth anniversary under Greenbrier ownership. Gunderson is an active participant in the Working Waterfront Coalition (WWC), an organization of businesses concerned about the environmental health and economic vitality of the Portland harbor. About The Greenbrier Companies, Inc.
Greenbrier (NYSE: GBX), (www.gbrx.com), headquartered in Lake Oswego, Oregon, is a leading supplier of transportation equipment and services to the railroad industry. Greenbrier builds new railroad freight cars in its three manufacturing facilities in the U.S. and Mexico and marine barges at its U.S. facility. It also repairs and refurbishes freight cars and provides wheels and railcar parts at 37 locations across North America. Greenbrier builds new railroad freight cars and refurbishes freight cars for the European market through both its operations in Poland and various subcontractor facilities throughout Europe. Greenbrier owns approximately 9,000 railcars, and performs management services for approximately 216,000 railcars.
See more news releases in Railroads and Intermodal Transportation Transportation, Trucking & Railroad Environmental Products & Services 2014


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Pringles Sweet Corn Limited Edition 5.5 oz never filled | eBay
Details about Pringles Sweet Corn Limited Edition 5.5 oz never filled
Pringles Sweet Corn Limited Edition 5.5 oz never filled
shawn10301975 (924 )
PRINGLES Limited Edition REUBEN Flavor - 5.5 Oz Potato Chips - Exp 2021 Sealed
Four(4)PRINGLES ROASTED TURKEY FLAVOR LIMITED EDITION 5.5 oz Six (6) cans
Pringles PICKLE RICK and MORTY LIMITED EDITION 5.5 oz NEW SEALED Pack Of 2 Cans
NEW Pringles Pringoooals 2020 Sweet Chilli Kicker Flavor Limited Edition Tube
Lot Of 3 Pringles PICKLE RICK & Morty LIMITED EDITION 5.5 oz NEW SEALED
Pringles - Roasted Turkey Flavor - Limited Edition - 5.5oz - Exp 12/2020 Lot 2
124124672030
Last updated on Mar 21, 2020 13:58:21 PDT View all revisions
Style: chips Flavor: Sweet Corn
Packaging: Tube Country/Region of Manufacture: United States


text: Share on Facebook Share on TwitterTrending on Scout2017 UCLA National Signing Day HQHands, Wilkes and McDonald's Full RostersBig Commitments From the WeekendThree-Star DB Branden Smith Recaps UCLA Visit3 Months of BRO for the Price of 1!Share & Embed2018 4-star ATH Radley-Hiles Talks Move Full StoryBruin Report Online Top StoriesMonday UCLA Mini-Recruiting BuzzJan. 16 -- Two more weeks to National Signing Day, and the UCLA coaches are back on the road visiting recruits. Jim Mora has fired up the private plane to see a four-star midwest…by Tracy PiersonBruin Report Online1:38 PMUCLA Hoops Up to No. 3 in AP PollJan. 16 -- After earning its first Pac-12 road sweep since coach Steve Alford took the helm, the UCLA men's basketball team moved up a spot in the latest Associated Press top 25…by BRO StaffBruin Report Online11:28 AMThree-Star DB Branden Smith Recaps UCLA VisitJan. 16 -- Lancaster (Calif.) Paraclete defensive back Branden Smith officially visited UCLA over the weekend. Could a decision be coming soon?by Greg BigginsBruin Report Online10:58 AM3 Months of BRO for the Price of 1!It's the last 2 weeks before National Signing Day, and you'll want to know everything about UCLA's potential Final Four hoops team. Now's the best time to get a great deal on BRO,…by BRO StaffBruin Report Online5:00 PMBig Commitments From the WeekendJan. 16 -- Scout takes a look at some of the bigger commitments around the country on the first official visit weekend after the dead period...by Brandon HuffmanBruin Report Online11:12 AMHands, Wilkes and McDonald's Full RostersJan. 16 -- Two UCLA signees, point guard Jaylen Hands and small forward Kris Wilkes, were named to the McDonald's All-American Game Sunday night...by Tracy PiersonBruin Report Online10:00 AMMora Releases Comment About Klemm FiringJan. 16 -- UCLA coach Jim Mora issues a statement on the firing of offensive line coach Adrian Klemm...by BRO StaffBruin Report Online9:32 AMBreaking NewsPossible Visit by Recruit Committed ElsewhereJan. 16 -- The new offensive coordinator, Jedd Fisch, has initiated contact with a U.S. Army All-American who is committed to another program, but he could officially visit UCLA...by Tracy PiersonBruin Report Online9:00 AM2017 UCLA National Signing Day HQIt's your one-stop shot to get everything about UCLA National Signing Day 2017 with Bruin Report Online's latest recruiting news, commitments, buzz, rumors and more leading up to…by BRO StaffBruin Report Online8:15 AMWhat Is Next After PSU Commit's UCLA Visit?Jan. 16 -- Pittsburgh Central Catholic offensive guard and Penn State commit C.J. Thorpe discusses his UCLA visit...by Brian DohnBruin Report Online8:05 AMBreaking NewsNews on New OL Coach, Changes to UCLA StaffJan. 16 -- With UCLA in the market for a new offensive line coach, we've heard the name of a potential candidate, and we have details on other possible changes on the UCLA coaching…by Tracy PiersonBruin Report Online6:27 AM2018 4-star ATH Radley-Hiles Talks MoveJan. 16 -- New Bradenton (Fla.) IMG Academy 2018 cornerback Bookie Radley-Hiles talked at the U.S. Army Combine about moving to Florida from the West Coast and playing in next…by Brandon HuffmanBruin Report Online4:59 AMLoad More

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Reasons you shouldn't hate Panthers left tackle Byron Bell - NFC South - ESPN
David T. Foster, III / Charlotte Observer/MCTByron Bell feels the 'hate' from fans341dDavid NewtonChuck Burton/APPanthers GM Dave Gettleman: Roster is stronger now than a year ago17hDavid NewtonSaints have several candidates to replace Junior Galette, but all have questions2dMike TriplettAndrew Weber/USA TODAY SportsDrew Brees burns the midnight oil in classic story3dMike TriplettAP Photo/Ted S. WarrenSteve Gleason returns to Washington for high school reunion3dMike TriplettScott Cunningham/Getty ImagesJunior Galette on Saints release: 'The worst call they've ever made'3dMike TriplettJonathan Bachman/APSaints deserve to be ripped and applauded after dumping Junior Galette4dMike TriplettESPN.com/David NewtonPanthers WR Kelvin Benjamin at playing weight, ready to go4dDavid Newton2015 Atlanta Falcons training camp preview5dVaughn McClure2015 New Orleans Saints training camp preview5dMike Triplett2015 Carolina Panthers training camp preview5dDavid Newton2015 Tampa Bay Buccaneers training camp preview5dPat YasinskasDon Juan Moore/Getty ImagesTampa Bay Buccaneers 53-man roster projection5dPat YasinskasGregory Shamus/Getty ImagesNew Orleans Saints 53-man roster projection5dMike TriplettAP Photo/Phelan M. EbenhackAtlanta Falcons 53-man roster projection5dVaughn McClureDon Juan Moore/Getty ImagesTampa Bay Buccaneers starting lineup projection5dPat YasinskasByron Bell feels the 'hate' from fans8/21/20140 SharesEmailComment
Joined ESPN in 2006Follow on Twitter0 SharesEmailPrintCommentCHARLOTTE, N.C. -- Byron Bell believes there's a large group of Carolina Panthers fans who dislike him, based on the way he has been heckled since giving up 3½ sacks last season against Buffalo.He believes many hate him not only for those sacks but because he's an unknown from a non-traditional football school who now has the most high-profile job on the Panthers' offensive line. Bell doesn't like the scorn, but he chalks it up to human nature.Byron Bell will start the season protecting Cam Newton's blind side. David T. Foster, III / Charlotte Observer/MCT"People are people," Carolina's new left tackle said. "People hate on Jesus. ... The man walked on water and they still didn't like him. I'm not comparing myself to our Lord and savior, but I'm just telling you that's how people are."The 6-foot-5, 340-pound Bell has an underdog story you'd think fans would embrace. He still drives a used truck -- which he doesn't even use on game days. He is known to walk to games at Bank of America Stadium and stop to talk to fans or take pictures with them if they ask. He gave his size 17 cleats to a fan every other practice during training camp in Spartanburg, South Carolina, and stopped to sign autographs every day.He arrived in Carolina in 2011 as an undrafted rookie out of New Mexico. He was forced into the starting lineup at right tackle when Jeff Otah was injured. Bell kept that job for most of three seasons. When left tackle Jordan Gross retired, Bell earned the right to replace him by beating out Nate Chandler. Bell prepared by trimming 15 pounds and going to Ohio to work with his former boxing coach to improve his footwork.Bell will protect quarterback Cam Newton's blind side this season, which means scrutiny from fans and the media will be considerable. The ridicule could intensify. But Panthers coach Ron Rivera is in his corner."He really is a likable guy," Rivera said. "I wish people would try to understand the situation and circumstances in which he came into this league. I don't think he's been given a fair shake."Rivera understands. He felt hated at times when he played linebacker for the Chicago Bears."I've been the guy that has been blamed, 'Ah, hell, he got beat for a touchdown,'" Rivera said. "Then you put the tape on and you sit down and the coach goes, 'Hey Ron, nice job trying to pick up that guy that was somebody else's.'"Rivera is passionate about this. He believes in his players and stands up for them, particularly when he feels they've been wronged.He believes Bell has been wronged, and refers again to the Buffalo game in Week 2."Some of it was him, some of it was another player, some of it was on the quarterback," Rivera said. "This is a team game, and people have to understand that."Rivera wishes people could get to know the Bell he knows."I just like his personality," he said. "He's a fun-loving guy. He's low-key. He's mellow. He's not gregarious. He's not out there. I think people mistake that."The criticism has hardened Bell to a degree. It also has driven him to become better. He has become better, and will be rewarded as a free agent next season for it."I'm not satisfied until it's my last snap in the National Football League," Bell said. "My biggest fear is getting cut. I feel like if I keep working I'll be here for a while, but I'm never satisfied."Naysayers are going to say what they want. The only people that matter in my life are God, my family and this team. At the end of the day, I'm fine."

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70 best Smoothies images on Pinterest | Clean eating meals, Smoothie recipes and Healthy eats
70 Pins323 Followers

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Content tagged "industrial-reconversion-and-renewal-project-irrp"
S. Giorgetti, Industrial… 1 year ago, 44,088 views, 0 comments

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THE Vendee AND Surrounding Area With THE Pays DE Retz Angela Bird | eBay
The Vendee and Surrounding Area: With the Pays De Retz-Angela Bird	|
Item number:320942367476
16 May, 2013 19:57:00 AEST View all revisions
ISBN:9780954580322
Publisher:Malnoue Publications


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Apartment great, - Review of 042 WEDDING 15, Berlin, Germany - TripAdvisor
Apartment great, - 042 WEDDING 15
“Apartment great,”
QXJ1XzdfeVVp
Review of 042 WEDDING 15
We had to collect the key from a nearby hotel, where the staff were supposed to speak English - unfortunately the man on reception spoke very little and was unable to accurately describe where the apartment was located. There were no instructions with the key, or sent by email. The apartment was a 20 minute walk from the hotel, but the initial finding of it took about 45 minutes.
The apartment is on the 5th floor, there is a 'small' lift - but not for the claustrophobic! The apartment itself was more than adequate, very clean and comfortable; it made for a good base. The nearest U-bahn was approximately a 10 minute walk away so location wise it was good. Lidl across the road, and Penny (another supermarket) a couple of doors up the street so obtaining provisions was easy. We ate out most of the time but not in Wedding so I can't comment on the local restaurants.
BUT....the wi-fi did not work; fortunately I have a 4G phone but my friends did not, which made planning our days out difficult due to limited internet access. Also, the TV reception was poor - not that we watched it particularly, only wanted to catch up the news.
Liked least: Wi-fi did NOT work!

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Impacts of protein–protein interaction domains on organism and network complexity
Journal ListGenome Resv.18(9); 2008 SepPMC2527699
Genome Res. Sep 2008; 18(9): 1500–1508. doi: 10.1101/gr.068130.107PMCID: PMC2527699Impacts of protein–protein interaction domains on organism and network complexityKai Xia,1 Zheng Fu,1 Lei Hou, and Jing-Dong J. Han2Chinese Academy of Sciences, Key Laboratory of Molecular Developmental Biology, Center for Molecular Systems Biology, Institute of Genetics and Developmental Biology, Beijing 100101, China1These authors contributed equally to this work.2Corresponding author.E-mail nc.ca.sciteneg@nahdj; fax 86-10-64845797.Author information ► Article notes ► Copyright and License information ►Received June 26, 2007; Accepted May 16, 2008.Copyright © 2008, Cold Spring Harbor Laboratory PressThis article has been cited by other articles in PMC.AbstractIt has been a puzzle that genome or proteome sizes are not correlated with the complexity of the organisms. Although alternative splicing and noncoding and regulatory elements explain some of the differences, the complexity of the protein interaction network and regulatory network may provide additional explanations. Here, we collected 642 domains that mediate protein–protein interactions (PPIs) and examined the evolution of the PPI domains and its impact on organismal complexity and PPI network complexity. In agreement with previous more general studies of protein domains, a significant expansion of PPI domains per proteome was found in metazoa. We also found both the number and coverage of PPI domains per protein increased. However, a better correlation with complexity was seen with increasing PPI domain coverage per protein, so that proteins in complex organisms are more compact and specialized in PPI. Such a structural adaptation of the proteins is correlated with the number of interactions that the proteins can make in PPI networks, and seems to be a more favorable way to increase network connectivity than other structural adaptations.Genome size is not always proportional to the genetic complexity. For example, Xenopus laevis and human have essentially the same genome size while they have a magnitude of difference in complexity, estimated by the number of cell types in an organism. This puzzling phenomenon, dubbed as the “C-value paradox,” refers to the lack of correlation between the complexity of an organism and its DNA content (C-value) (Futuyma 2005). In terms of gene number, human has about 20,000 ~ 25,000 genes, just a little more than the worm Caenorhabditis elegans, whereas C. elegans has about 29 cell types and human 169. These phenomena lead to the question “why do humans have so few genes?” (Pennisi 2005)One explanation is that alternative splicing makes up the difference in gene number, and therefore in complexity, by providing alternative isoforms to carry out different functions. However, so far, most alternatively spliced isoforms have been found to have similar, if not identical, functions (Lopez 1998; Smith and Valcarcel 2000; Graveley 2001). A second factor, which is considered to be a major factor contributing to the paradox is the “dark matter,” or the noncoding and regulatory elements in the genome (Gerstein et al. 2007; Prasanth and Spector 2007). Besides these two, a third alternative answer to this question is that humans have a much more complex molecular interaction network (Koonin and Galperin 2003), that is, the connections in the network are greater in number and much more intricate and dynamic in pattern, despite a similar number of nodes to lower organisms. Here, we present our study from the perspective of protein–protein interaction (PPI) networks, or the interactome networks.PPI functions have been found to be enriched in domain superfamilies whose abundance in a proteome (the number of proteins containing a superfamily of domains in a proteome) correlates with organismal complexity (Vogel and Chothia 2006). In this study, we specifically examined whether expansion of PPI domains in general is a major factor contributing to organismal complexity. Further are changes at the individual protein level involved, which might directly link organismal complexity to network complexity. Specifically, does an increase in PPI domain number, length, or coverage per protein also contribute to organismal complexity, and could these structural adaptations increase organismal complexity through increasing PPI network complexity?We collected 642 protein domains that are involved in PPI and compared the domain compositions of proteins in 19 different organisms ranging from Kluyveromyces lactis to Homo sapiens, as well as two plants, Oryza sativa and Arabidopsis thaliana. We also included a slime mold, Dicytostelium discoideum, as a transition point between unicellular organisms and metazoan (Supplemental Table 1). Surprisingly, we found that specialization and compaction of PPI domain-containing proteins through increasing coverage of PPI domains per protein are potentially the most significant structural changes associated with organism complexity (measured as number of cell types in an organism) and network complexity (measured as number of PPIs of a protein).ResultsCollection of PPI domainsA protein domain is a structural unit that often folds independently of the rest of the protein (David and Nelson 2005). We determined each protein’s domain architecture as annotated by InterPro (Mulder et al. 2005), an integrated domain database that combines a number of detection methods and annotations currently from 11 databases. PPI domains are those that can recognize exposed sites on their binding partners. Here, we obtained a list of PPI domains through four sources: (1) annotated to be involved in protein domain–domain interactions by the Database of Domain Interaction & Bindings Database (DDID), (2) have a GO term of “protein (any protein) binding” in the InterPro domain gene ontology (GO) annotation database, (3) labeled as “experimentally proven to be involved in PPI” in the InterPro Interactions field, (4) have protein binding or interaction function described in the InterPro domain description or literature. This results in 642 PPI domains that are found in the 19 organisms. The 642 PPI domains are selected from all protein families listed in the InterPro database without any prior selection for a particular family or representatives of a small number of families. PPI domains are annotated solely based on whether they are experimentally determined or annotated by DDIB and InterPro as domains participating in PPI. These domains, together with the source of evidence supporting their PPI function, are listed in Supplemental Table 2. Because the SwissProt database contains only experimentally validated polypeptide sequences, it may be more biased than proteins predicted from genomic sequences, such as those in the TrEMBL database, which is developed to complement the SwissProt entries. We therefore based the analyses on UniProt proteins, which is a combination of SwissProt and TrEMBL protein entries.We first looked for any evolutionary trend of PPI domains among the 19 species (Supplemental Table 1). Compared with unicellular organisms, the percentage of PPI domain-containing proteins increases dramatically in multicellular animals, indicating a big expansion of PPI domains at the proteome level upon the transition from unicellular to metazoan organisms (Fig. 1A). We listed the proportions of proteins unannotated for any domain to examine whether a particular organism is significantly under- or overannotated for domain structures as compared with Saccharomyces cerevisiae or human. If so (proportions test P < 0.05), the organism’s name is marked with an asterisk or a pound sign in Figure 1A. It indicates that rice, Candida albicans, Neurospora crassa, and Dictyostelium discoideum are significantly underannotated, and Arabidopsis, fission yeast, zebrafish, frog, rat, mouse, and cow are significantly overannotated. To control for the annotation differences, we excluded all of the proteins with no domain annotation from our analysis. For example, the percentage of proteins having PPI domains versus the total proteins that have at least one annotated domain is shown in Figure 1A. Different accuracy of different genome and proteome sequences and annotations is bound to remain one cause of variation between organisms, even when significantly reduced by considering only the domain-annotated portion of the proteomes. Therefore, we studied not only the change between yeast and human, but also those in 17 other different species to derive statistically valid conclusions that are independent of annotation variations. In addition, wherever possible, we included the non-PPI domains as controls for any potential domain annotation biases. If the PPI and non-PPI domains have the same trend, bias must be considered.Figure 1.Evolutionary structural adaptations toward PPI domain expansion at the individual protein level. (A) The percentage of proteins with PPI domains (maroon blocks), other non-PPI domains (cyan blocks) among all proteins with domain annotation in each organism ...Thirty-seven percent of the PPI domains are specific to metazoa (“metazoan specific”), whereas only 8% of the PPI domains are specific to unicellular organisms. Ten percent of them are “expanded” proteome-wide in metazoa, that is, an increased fraction of a metazoan proteome contains these domains. Measured by the dN/dS of each domain (Methods), both “metazoan specific” and “expanded” PPI domains seem to evolve faster than non-PPI domains and other PPI domains (Supplemental Data; Supplemental Fig. 1; Supplemental Tables 3, 4). The abundance distribution and the evolutionary rates are consistent with the previous findings that PPI functions are enriched among protein superfamilies whose expansions correlate with organismal complexity. Protein domains with signaling and regulatory functions have been repeatedly found highly expanded in various metazoan proteomes (Kirschner and Gerhart 1998; Rubin et al. 2000; Lander et al. 2001; Pawson and Nash 2003; Vogel and Chothia 2006). We also found that PPI domains specific to or expanded in metazoa preferentially participate in signaling and regulation (Supplemental Data; Supplemental Table 5).Expansion of PPI domains in individual proteinsPPI domain content of individual proteins directly dictates what proteins they interact with and what PPI network they construct. We therefore examined whether the PPI domains are also expanded at the level of individual proteins through three types of structural changes: domain number, domain length, and domain coverage (see below for definition). We examined the whole collection of PPI domains on a protein, not just any particular domains. We also analyzed non-PPI domains as a whole collection to compare with PPI domains and control for study bias in higher organisms.Different domains often have distinct functions, so that a protein with multiple domains may have more opportunities to interact with other proteins or small molecules to carry out additional functions. We first calculated the percentage of proteins with single or multiple PPI domains in different proteomes (Fig. 1B). We found that through evolution, multicellular organisms tend to have larger fractions of proteins with multiple PPI domains compared with the fractions of proteins with a single PPI domain, but that the fraction of proteins containing multiple non-PPI domains does not increase relative to that of single non-PPI domain-containing proteins (Fig. 1C). We then examined the relationship of PPI domain number increase on individual proteins to organismal complexity, estimated by the number of cell types in an organism (Vogel and Chothia 2006).To ensure the robustness of the analysis and to rule out the possibility that only small proportions of proteins are responsible for the results, we randomly divided the proteins in each organism into 10 nonoverlapping groups, and carried out leave-one-out analysis and boxplot analysis. By leaving one group out and examining the remaining nine groups as a combination, we obtained one correlation to organismal complexity for each nine-group combination (Fig. 1D). This would detect differences in the correlations obtained using different datasets. By boxplot, the variations among all of the 10 different datasets were visualized and considered when examining a correlation between two variables. The average non-PPI domain number per protein is slightly anticorrelated with organismal complexity, or the number of cell types in an organism (Supplemental Fig. 2A), while the PPI domain number per protein is highly correlated with organismal complexity (Fig. 1D). Similar results can be seen if all 10 groups were analyzed together with the variations among different groups taken into account (Supplemental Fig. 3A,B).Increased coverage by PPI domains on proteinsIn addition to an increase in PPI domain number per protein, we also found that in complex organisms PPI domain-containing proteins become more compact or packed with PPI domains. By “compactness,” we refer to proteins with smaller fractions of domain-free regions that lack any domain. These domain-free regions are not necessarily the disordered regions, which can frequently appear inside DNA-binding and protein-binding domains, especially on signaling proteins (Dunker et al. 2005). Thus, compactness does not necessarily correspond to the tightness in proteins’ three-dimensional packing. To examine such “compactness” quantitatively, we defined a metric “domain coverage” to quantify the functional compactness of protein domain architecture. It is defined as the percentage of a protein covered by certain protein domains over its entire length. Domain coverage then represents the percentage of the functional regions within the full length of a protein. It can be calculated by the following formula:
Higher domain coverage value, when all of the domains are included, implies a compact protein with fewer nonfunctional regions over its primary structure. PPI domain coverage, that is, the percentage of the entire length of a protein occupied by PPI domains, may also indicate whether a protein is more specialized with fewer non-PPI domains.We used heatplots to visualize the evolutionary trend of the PPI and non-PPI domain coverage (Fig. 1E,F). In addition to the rise of multi-PPI domain proteins in higher organisms, proteins shifted from being enriched at low PPI domain coverage in lower organisms and plants to being enriched at high coverage in animals (Fig. 1E). In cow and human, >20% of the annotated proteins have PPI domain coverage near 100 (Fig. 1E). In contrast, the non-PPI domain coverage does not change (Fig. 1F). In addition, the shift is not gradual; instead, it is from one extreme (0%–20%) to the other (90%–100%). The fractions with medium coverage remain almost constant (Fig. 1E), whereas the fractions between 0%–20% and 90%–100% change. This suggests that if a protein acquires a PPI domain or function, it tends to become specialized, so that it contains few other domains and domain-free sequences (Fig. 1E). For example, a whole category of adaptors and scaffold proteins specialized for PPI, such as GRB2, has high PPI domain coverage and is expanded greatly in higher organisms. Non-PPI domain coverage is not correlated with organismal complexity (Supplemental Fig. 2B), whereas PPI domain coverage is highly correlated with organismal complexity, even more so than the average PPI domain number (Fig. 1G). Both the leave-one-out and boxplot analyses produced similar results (Fig. 1G; Supplemental Fig. 3C,D).We also examined whether an increase in average domain length can explain the increase in PPI domain coverage. As shown in Figure 1H, the average length of PPI domain is slightly correlated to organismal complexity, whereas that of the non-PPI domain is negatively correlated to organismal complexity (Supplemental Fig. 2C), indicating that the PPI domain length increase is small, but not attributable to annotation bias, and may contribute to the increase in domain coverage and organismal complexity to a small extent (Supplemental Fig. 3E,F).How does a protein increase its domain coverage or compactness through evolution? We selected 2629 groups of orthologous proteins that have orthologs in at least five metazoan species and explored the change of protein structure within each group (Fig. 2; Methods). Here, we put forward four possible explanations for the increase of PPI domain coverage on proteins through evolution. The first is PPI domain length increase (Figs. 1H, ,2A).2A). The second is that some orthologous proteins gradually lose the domain-free sequences (not occupied by known protein domain) on their N termini (Fig. 2B), C termini (Fig. 2C), or in the middle of the protein during evolution. The third explanation is the loss of non-PPI domains. The fourth is the replacement of the domain-free regions with new functional domains (Fig. 2D). Among the 191 ortholog groups that have PPI domains in at least five metazoan species and are found to increase in PPI domain coverage during evolution (Spearman rank correlation coefficient [RCC] of PPI domain coverage to organismal complexity > 0.6), loss of non-PPI domains or decrease in non-PPI domain length (RCC to organismal complexity < −0.55) together accounts for a minimal 3.7% of the cases. Whereas trimming the domain-free sequences (RCC to organismal complexity > 0.55, RCCs are the same below) contributes the most to PPI domain coverage increase (51.3%), followed by increasing PPI domain length (31.4%) and PPI domain number (10.5%).Figure 2.Examples of increasing domain coverage on orthologous proteins through evolution. PPI domain length increase (A), loss of the domain-free sequences at orthologous proteins’ N termini (B), C termini (C), and PPI domain insertion (D) that contribute ...Other proteins bear no clear sequence similarities across many species. We found that for all of the proteins in the 19 organisms, reduced domain-free regions best explain an increase of PPI domain coverage on a protein than any other factors (linear regression R2 = 0.724). Increased PPI domain length contributes slightly to PPI domain coverage increase (linear regression R2 = 0.119). All other factors contribute very little to it (linear regression R2 < 0.1). Hence, removing the sequences outside of any functional domains to make the protein become more functionally compact is the most common way to enrich for PPI domains and to increase PPI domain coverage at the protein level.Structural changes at the protein level are also consistent with the expansion at the proteome level. The proteins containing “Expand” or “Metazoan Specific” PPI domains apparently have higher PPI domain number and coverage, but not longer PPI domains than those having the PPI domains that are “Common” to unicellular organisms, metazoa, and plants, or “Shrink” in multicellular organisms, with the proteins having “Metazoan Specific” PPI domains display the highest PPI domain coverage overall (Table 1; P-values are listed in Supplemental Table 6).Table 1.Structural and network properties of proteins containing PPI domains of different evolutionary profilesThese results indicate that domain-free regions are more dispensable (David and Nelson 2005). In complex organisms, there is a selection for new, more, and slightly longer PPI domains, and fewer domain-free sequences in the metazoan PPI domain-containing proteins.PPI domain coverage and PPI network complexityAt the molecular level, the correlation between protein structural complexity and organismal complexity might correlate with complexity of protein–protein or protein–nucleic acid interaction networks. To investigate this hypothesis, the relationship of PPI domain arrangements in individual proteins to the complexity of their PPI network was examined. The most straightforward way to increase network complexity is to increase the interaction degrees (k) of proteins, that is, the number of interactions a protein makes in a network. Interaction degree is therefore a most simple measurement of network complexity. We studied the high-quality PPI networks constructed from literature-based human PPIs collected by the Human Protein Reference Database (HPRD) (Peri et al. 2003) and from the core yeast PPI data set curated by the Database of Interacting Proteins (DIPcore) (Xenarios et al. 2000).We examined whether the expansion of PPI domains in a protein is correlated with the protein-interaction degrees of the protein in PPI networks. We compared a protein’s interaction degree against each of the following variables: PPI and non-PPI domain number, PPI and non-PPI domain coverage, and PPI and non-PPI domain length. Again, we applied both leave-one-out and boxplot analyses to ensure the robustness of results and to exclude the effects due to a smaller number of outliers (Fig. 3; Supplemental Figs. 4, 5). Among the six variables, PPI domain coverage has the highest correlation with protein interaction degree (Fig. 3A,B; Supplemental Figs. 4, 5), more than between PPI domain number and degree (Fig. 3C,D; Supplemental Fig. 5), and between PPI domain length and degree (Fig. 3E,F). Testing the significance of the association by linear regression indicates that only PPI domain coverage per protein is significantly correlated with the PPI degree of the protein. This is in agreement with PPI domain coverage being the factor most correlated to organismal complexity (Fig. 1). When the proteins in PPI networks were separated into hubs (k ≥ 5) and non-hubs (k < 5), it is obvious that compared with non-hubs, hubs have small shifts to higher PPI domain number (Fig. 4A,B) and large shifts to higher PPI domain coverage (Fig. 4C,D) in both yeast and human PPI networks.Figure 3.Relationships of PPI domain coverage, number, and length to PPI degrees by leave-one out analysis. The average human and yeast PPI degrees of proteins in each of the nine out of 10 group combinations within each interval of PPI domain coverage (A,B), ...Figure 4.Distribution of PPI domain number and PPI domain coverage among human and yeast protein hubs and non-hubs. Proteins in human (A,B) and yeast (C,D) PPI networks are divided into hubs (k ≥ 5) and non-hubs (k < 5). The fraction of hubs and ...An increase of PPI interaction degree with an increase in the number of PPI domains on a protein would be naturally expected. But why does PPI domain coverage rather than the number of PPI domains per protein significantly correlate with PPI degrees? We wondered whether it was due to the constraints (e.g., structural constraints) for a protein to gain more domains than to increase coverage. Consistent with this hypothesis, we found that proteins with high domain number are rare in a proteome (5.2% proteins in human and 1.1% in yeast with domain number > 3), and the proportion of proteins decreases sharply as the number of PPI domains on the proteins increases, suggesting that there are constraints for the protein to gain a domain. In contrast, although the proteins with low PPI domain coverage are more common, the distribution of PPI domain coverage is much flatter than the distribution of domain number (Fig. 4), suggesting relaxed constraints. Consequently, there can be a larger number of hubs having high PPI domain coverage than having high PPI domain number (Fig. 4).DiscussionOur main finding is that PPI domain coverage provides the best genome-wide predictor of organismal complexity yet reported. PPI domain coverage is also highly correlated with PPI degree. This suggests that complexity of PPI may be required for organismal complexity.Why does PPI domain coverage correlate better with organismal complexity than with PPI network degree if network complexity is required for organismal complexity? It cannot be excluded that PPI domain coverage might be able to affect organismal complexity independently of PPI network complexity. For example, PPI domains could also be associated with and contribute to the complexity of the regulatory network and metabolic networks, albeit probably more indirectly. However, we note that correlations to PPI network complexity might be underestimated because the PPI network is made noisy by false-positive PPIs, because the network datasets are incomplete, or because PPI degree is an oversimplified measurement for network complexity. These factors could also explain why all of the parameters we measure correlate less significantly with network complexity than with organismal complexity. If such limitations to the network statistics could be overcome, association of other factors to PPI degree might surface.Our results suggest that, although an increase in interaction degree could be achieved by an increase in either PPI domain number or PPI domain coverage, the increase in domain coverage is a more frequent means to increase PPI degree. The preference for increasing PPI domain coverage versus PPI domain number suggests protein structure constraints on network connectivity. It will be important to explore the molecular relationship between network complexity and PPI domain coverage in the future.Our findings argue that, in addition to the possible contribution of alternative splicing, increased complexity in the higher organisms may also be attributable to protein structures that allow a protein to be more compact, specialize in PPI, and achieve more interactions among the same number of network nodes. From the network point of view, an increase in alternative splicing forms is a means of adding nodes to the network, whereas PPI domain expansion on individual proteins is a means of adding edges to the network. Increasing edges is a much more efficient way to increase complexity compared with increasing nodes, as the number of potential edges is the square of the number of nodes in a network (Papin et al. 2005).MethodsDatasetsAll domain information was downloaded from the InterPro ftp site (ftp://ftp.ebi.ac.uk/pub/databases/interpro/) on September 5, 2007. After parsing the XML file, we obtained the entire structural information of each protein, including its family, domain, repeat, binding site, active site, post-translational modification site, and annotated Gene Ontology information. An InterPro domain is an independent structural unit, which can be found alone or in conjunction with other domains or repeats and an InterPro repeat is a region that is not expected to fold into a globular domain on its own (Mulder et al. 2005) (ftp://ftp.ebi.ac.uk/pub/databases/interpro/user_manual.txt). To avoid excluding useful structural information of proteins, we define the word “Domain” in this work as a functional and structural unit that is confirmed by an InterPro domain entry, InterPro family entry, or InterPro repeat entry. InterPro combines a number of databases, and we chose PANTHER, Pfam, PIRSF, PRINTS, ProDom, PROSITE, SMART, and TIGRFAMs as the domain architecture data sources. These databases use different methodologies to identify proteins’ domain architecture, and they may give rise to different domain lengths and domain numbers at the same stretch of sequence on a protein. We used the longest functional or structural segment within an InterPro domain/family/repeat annotation to represent the boundary of the domain.Domain coverage depends on the correctness of domain boundaries as given by InterPro, which might not be always accurate. But, there is no apparent bias toward a larger boundary for higher organisms or for higher degree proteins, as indicated by the lack of correlation of non-PPI domain length or coverage with organismal complexity or PPI degree. Comparatively, it is easier to find scenarios where the domain number bias is introduced by study and annotation bias, but again, both can be controlled by non-PPI domains.All of the protein data were downloaded from UniProt (ftp://ftp.uniprot.org/pub/databases/uniprot/current_release/knowledgebase/complete/) on September 5, 2007.HPRD data set was downloaded from www.hprd.org on March 7, 2005.The yeast core data set (DIPcore) was downloaded from http://dip.doe-mbi.ucla.edu on June 22, 2006.We combined the DDIB (http://www.biosino.org/DIDWeb/index.htm) PPI domains, Pawson’s collection of protein interaction domains (http://pawsonlab.mshri.on.ca/), the InterPro domain description, the InterPro experimentally confirmed PPI domain annotation, and the GO annotations (ftp://ftp.ebi.ac.uk/pub/databases/interpro/interpro2go) for the InterPro domain, family, and repeat to arrive at the 642 protein–protein interaction domains (Supplemental Table 2).The orthologous proteins were downloaded from Inparanoid database (http://inparanoid.sbc.su.se).TaxonomyInterPro has 13,383 organisms, and most of them only have a very limited number of proteins in the database. We selected the 19 eukaryotic organisms based on the following criteria: (1) nearly intact proteome; (2) model animals or organism for genetics analysis; (3) the full genome sequences are due to finish soon. Dictyostelium discoideum is a slime mold that grows up with an independent unicellular form; however, they aggregate together by releasing cAMP to signal each other and generate a multicellular structure in response to an unfavorable environment such as starvation (Postma et al. 2004). Hence, we chose D. discoideum as a transitional species between unicellular organisms and multicellular organisms. The identifier, scientific name, and common name of the 19 organisms selected are shown in Supplemental Table 1. The phylogeny is determined by NCBI Taxonomy (http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Root) and Tree of Life web project (http://tolweb.org/tree/).Leave-one-out and boxplot analysisProteins in each organism were randomly divided into 10 nonoverlapping groups of an approximately equal number of proteins. The average domain number (DN), domain coverage (DC), or domain length (DL) was calculated 10 times for each organism (to test association to organismal complexity) or within each interval of DN, DC, or DL (to test association to PPI degree, whose average was also calculated), using a different nine out of the 10 groups (leaving one group out) each time. The boxplots were generated by using all of the average values in each of the 10 groups for an organism (to test association to organismal complexity) or within an interval of DN, DC, or DL (to test association to PPI degree). Same procedures were applied to both PPI domains and non-PPI domains.dN/dS calculationdN/dS was calculated by the YN00 program (Yang and Nielsen 2000) using the DNA sequences of PPI domains in orthologous pairs of proteins between human and mouse. Ortholog pairs are obtained from Inparanoid database (http://inparanoid.sbc.su.se). Only the highest ranking orthologous pair in each ortholog group was considered as orthologs, so that each ortholog protein belongs to one and only one ortholog group. For each shared PPI domain on orthologs, we first extracted the amino acid sequences of the human and mouse domains, and then aligned them by ClustalW with default parameters to match the domain sequences. After replacing the amino acid sequences by their corresponding DNA sequences defined in Ensembl Genome Database (www.ensembl.org), the human and mouse DNA sequences of a domain on a pair of orthologs between the two organisms were used as input to the YN00 program with default parameters.PCC, RCC, and regression calculationPearson correlation coefficients (PCC), Spearman rank correlation coefficients (RCC), linear regressions, or boxplots were calculated or plotted using R (http://www.r-project.org/). PCC and RCC both measure the degree of association between two variables and are defined as PCC = ((Xi − X)(Yi − Y)/(n − 1)SxSy), where Sx and Sy are the standard deviations of variables X and Y, respectively, n is the length of the vector, and RCC = 1 − 6∑(d2/n(n2 − 1)), where d2 is the difference in statistical rank of corresponding variables and is an approximation to the exact PCC. Their values range between −1 and 1, with 1 signifying perfect correlation, –1 perfect anticorrelation, and 0 no association. For linear regression, y = ax + b, P-values for slope measures the significance of the association between two variables, R2 for the regression tests the goodness of fit of the data to the regression model.GO enrichment testEnrichment was determined by Fisher exact test, followed by Benjamini-Hochberg correction as described previously (Xia et al. 2006) for multiple hypothesis testing on all the annotated InterPro ID in the InterPro ID to GO term mappings.AcknowledgmentsWe thank Tony Pawson (Mount Sinai Hospital) for a discussion that inspired this project. We thank Nicholas Baker (Albert Einstein College of Medicine) for editing the manuscript, Nansheng Jack Chen (Simon Fraser University) for critical reading of the manuscript, Ziheng Yang (University College London) and Rasmus Nielson (UC Berkeley) for helpful suggestions on evolutionary rate analysis, and Liang Du and Jine Li for domain annotations. We also thank the anonymous reviewers for their valuable suggestions. This work was supported by grants from the China National Science Foundation (grant nos. 30588001 and 30620120433), National Basic Research Program of China (2006CB910700), and funds from the Chinese Academy of Sciences to J.-D.J.H.Footnotes[Supplemental material is available online at www.genome.org.]Article published online before print. Article and publication date are at http://www.genome.org/cgi/doi/10.1101/gr.068130.107.ReferencesDavid L., Nelson M.M.C., Nelson M.M.C. Lehninger principles of biochemistry, 4th ed. W.H. Freeman & Co; New York: 2005. 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