Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection - Wikidata - wikimedia - TriplyDB

Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection

Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection

http://www.wikidata.org/entity/Q27638985

about

Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex Adhesive Pili in UTI Pathogenesis and Drug Development Perspective: Adhesion Mediated Signal Transduction in Bacterial Pathogens Structural Basis for Mechanical Force Regulation of the Adhesin FimH via Finger Trap-like β Sheet Twisting Structure-Based Drug Design and Optimization of Mannoside Bacterial FimH Antagonists The Structure of the PapD-PapGII Pilin Complex Reveals an Open and Flexible P5 Pocket Solution NMR structure of BT_0084, a conjugative transposon lipoprotein from Bacteroides thetaiotamicron Structural insights into the biogenesis and biofilm formation by the Escherichia coli common pilus Structure ofStreptococcus agalactiaetip pilin GBS104: a model for GBS pili assembly and host interactions Structural insight in histo-blood group binding by the F18 fimbrial adhesin FedF Structural Sampling of Glycan Interaction Profiles Reveals Mucosal Receptors for Fimbrial Adhesins of Enterotoxigenic Escherichia coli Mechanisms of hemorrhagic cystitis.The tyrosine gate of the bacterial lectin FimH: a conformational analysis by NMR spectroscopy and X-ray crystallography Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding.Elevated shear stress protects Escherichia coli cells adhering to surfaces via catch bonds from detachment by soluble inhibitors.A structure-based sliding-rebinding mechanism for catch bonds.Differentiation and developmental pathways of uropathogenic Escherichia coli in urinary tract pathogenesis.Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions.The bacterial fimbrial tip acts as a mechanical force sensor Integrin-mediated host cell invasion by type 1-piliated uropathogenic Escherichia coli.Systems biology approach for mapping the response of human urothelial cells to infection by Enterococcus faecalis.FimH forms catch bonds that are enhanced by mechanical force due to allosteric regulation.Pathogenic potential of emergent sorbitol-fermenting Escherichia coli O157:NM.Type 1 fimbriae, a colonization factor of uropathogenic Escherichia coli, are controlled by the metabolic sensor CRP-cAMP Taurolidine antiadhesive properties on interaction with E. coli; its transformation in biological environment and interaction with bacteria cell wall Complete genome sequence of Crohn's disease-associated adherent-invasive E. coli strain LF82.Virulence plasmid harbored by uropathogenic Escherichia coli functions in acute stages of pathogenesis.Transcriptional response of E. coli upon FimH-mediated fimbrial adhesion.Effect of trimethoprim-sulfamethoxazole on recurrent bacteriuria and bacterial persistence in mice infected with uropathogenic Escherichia coli Diversification of the Salmonella fimbriae: a model of macro- and microevolution.Clonal analysis reveals high rate of structural mutations in fimbrial adhesins of extraintestinal pathogenic Escherichia coli.Transposon mutagenesis identifies uropathogenic Escherichia coli biofilm factors.Specific association of lectin LecB with the surface of Pseudomonas aeruginosa: role of outer membrane protein OprF.Point mutations in FimH adhesin of Crohn's disease-associated adherent-invasive Escherichia coli enhance intestinal inflammatory response.Characterization of urinary tract infection-associated Shiga toxin-producing Escherichia coli.Adhesion and entry of uropathogenic Escherichia coli.Structural biology of the chaperone-usher pathway of pilus biogenesis The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes.Allosteric catch bond properties of the FimH adhesin from Salmonella enterica serovar Typhimurium.Inhibition and Reversal of Microbial Attachment by an Antibody with Parasteric Activity against the FimH Adhesin of Uropathogenic E. coli

P2860

Q24645503-868A9F30-E83F-40B0-99D4-82EFBCA25A5F Q26752944-B48AD82A-8EA2-446E-A315-6171B6DB052A Q26768433-9803D3D8-8B04-4B49-8085-2F6E8DEE7DE4 Q27661696-C8F649E6-99A4-43F9-A2EF-E103D189489C Q27661999-18BF5C52-3CD8-4531-96B8-789605FE494B Q27673568-0BE3E21B-8614-4E4C-B971-9A45F32F9360 Q27675795-52DD806E-B166-47A0-8E4D-852B979B1014 Q27677402-76B5C52E-E09E-40C2-81F9-2919415864FD Q27678225-544318BE-EE35-4C5A-BD81-CE2809EDFE1D Q27681777-845B2D9A-E5DE-40A3-9834-B69D09248EA8 Q27683816-3FAC2AE8-561E-493C-BF76-77E6C63A31BA Q27686784-BFB000AB-8933-4A71-BF38-C4B6B6347B2E Q27700666-6EEB898B-8422-4067-BA80-32C9C886F088 Q30399333-294188F6-E314-40EB-A07C-27822639663E Q30477190-213E769D-8ECC-4D02-878D-A6264BC8701C Q30478974-4E787BFC-62EA-4E82-8FD9-22A2CAA4DAEB Q30515509-A180FB5E-3ED0-4033-B833-C3457D6B6CA9 Q30838228-F43D89BB-B938-4F5C-AB36-7ECC11AE9CBD Q31009798-DD587DC1-3809-4F43-85F0-4DF20CD11CFD Q33290835-0B763967-BCA2-444B-A56C-AD98079A4652 Q33307854-33BD9752-2AC9-4CAE-9491-807BB6B4F07A Q33320807-40744542-F48C-46DF-80BC-3403B39177D9 Q33381487-A6EF322D-303E-458F-A03E-0A967F66C055 Q33410780-2458DD90-8227-494A-8EAC-FB421BAD0F32 Q33529088-151FA371-87F6-4BC3-8A5E-1C968FCB84E6 Q33700512-9AFE75C4-9173-4AC9-83C6-3E989E9CFA39 Q33769094-D3214E3A-40C4-4EC8-BF40-E5BDE8959237 Q33834461-6F417F81-F303-4AB4-B698-9B75026A413D Q34259004-6489A802-071E-401F-883B-787FA9C6C55F Q34305601-00CA63EB-48D7-4792-96E0-861C056700F0 Q34398964-F797A65A-48FE-4FA0-8FD8-E3BA067C1443 Q34415785-0513028E-CE88-4F09-9C24-32B226267D6F Q34442310-82328A6A-D8F2-4275-AE79-F171CAEA78DA Q34565942-B3D07AE4-ACF1-44ED-90DB-46FD70277C06 Q34596075-184FB192-3F94-4D44-83A0-6253F6D001A2 Q34655354-64D451F1-4FC6-4089-8EE6-BDC811B90B1A Q35007461-24BBEAC9-F91F-4596-90D6-BF1296DAF4A0 Q35103730-3EBB07AF-0CCE-46B9-BFF3-53B5260E5992 Q35515981-37E2221A-8FD0-4E77-AD69-4111C66CB254 Q35606583-EEB4ECC3-23A7-4BC0-A54C-75A090397473

P2860

Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection

http://www.wikidata.org/entity/Q27638985

description

2002 nî lūn-bûn

@nan

2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Structural basis of tropism of ...... during urinary tract infection

@ast

Structural basis of tropism of ...... during urinary tract infection

@en

Structural basis of tropism of ...... during urinary tract infection

@nl

type

label

Structural basis of tropism of ...... during urinary tract infection

@ast

Structural basis of tropism of ...... during urinary tract infection

@en

Structural basis of tropism of ...... during urinary tract infection

@nl

prefLabel

Structural basis of tropism of ...... during urinary tract infection

@ast

Structural basis of tropism of ...... during urinary tract infection

@en

Structural basis of tropism of ...... during urinary tract infection

@nl

P1433

Q27638985-A9F9D8FB-1E25-49BC-8255-392D84CF23ED

P1476

Q27638985-0D79D3EA-943F-4A4B-B73E-EE3626E2693D

P2093

Q27638985-03D1A19E-00CE-4762-962C-3FC1C50B6FB6

Q27638985-20976689-F968-49FE-AE18-870E82F1C0AB

Q27638985-39AE43E3-2F53-4A82-94AD-3BAB863BE189

Q27638985-4336C77A-E855-48ED-B759-AD7288D47EA5

Q27638985-53D10319-6C2E-4C11-AEF9-B789923D8EC9

Q27638985-5BA75D32-0988-4C04-90DB-77E74BED17E8

Q27638985-675A77FD-2D3D-4BEC-B1EE-540779BA2B23

Q27638985-CF6F5509-0E5B-40B5-850F-5E17E1D967DB

Q27638985-D4FD8C5F-AFBF-48BD-B9D2-CB3CC99E9C48

P2860

Q27638985-01100EF0-A183-4A64-BE26-0FBC452781B0

Q27638985-0C4366F4-FCB8-4DE2-A836-E5DD05AFC236

Q27638985-1505CD6F-2311-457E-8A9D-E4072BD92C66

Q27638985-1C541478-98A4-4748-84B8-CB79C66136DE

Q27638985-25AE1608-D982-4436-A1B6-3B4C1CCC4722

Q27638985-2A1F8E9F-24C3-4089-895C-516025AC8320

Q27638985-305456E4-CA83-4574-B365-3704838928B4

Q27638985-321EA2E8-C4AD-4368-B55B-D4951D615B24

Q27638985-36E755EE-256E-4F04-A53D-6FA7822F227A

Q27638985-39E090B7-23B7-4BB5-BC9F-7C0730DBFB4E

P304

Q27638985-90E30481-D8E1-4C22-9F44-D3CD5A08AC07

P31

Q27638985-E230B1C1-B256-4441-B171-979304653BC1

P3181

Q27638985-E43D9BC6-49BA-4475-98CA-C275917CB3F3

P356

Q27638985-871D9A3E-443E-44C4-8EA2-8C287C5E1179

P407

Q27638985-EA4BD16A-BF16-48C2-921F-5E3A8AFDAF1B

P433

Q27638985-AA2DAABD-4179-46F0-AE44-C8CA908E8CF4

P478

Q27638985-3E4A4E57-96D1-48AA-AFF7-1A71521E30E3

P50

Q27638985-3202026C-777B-459E-93B6-3F5ADB9A2801

Q27638985-3E2BF671-F73B-4EC3-8EF6-9CB1D7E8D0C5

P577

Q27638985-A2F5D3C3-0D2E-4BAB-9F26-88366CA9C4A5

P5875

Q27638985-5A8451A1-20C6-446B-8BFC-C11C79536C13

P698

Q27638985-6CF4A59F-58E6-4A86-83F4-8C02C204F078

P921

Q27638985-06810BFE-4E6E-4768-872D-352C496E4D74

P3181

P356

J.1365-2958.2002.02915.X

P1433

Molecular Microbiology

P1476

Structural basis of tropism of ...... during urinary tract infection

@en

P2093

Anthony DeFusco

http://www.w3.org/2001/XMLSchema#string

C Gale Auguste

http://www.w3.org/2001/XMLSchema#string

Charlotte Widberg

http://www.w3.org/2001/XMLSchema#string

Chia-Suei Hung

http://www.w3.org/2001/XMLSchema#string

Danielle Hung

http://www.w3.org/2001/XMLSchema#string

Jerome Pinkner

http://www.w3.org/2001/XMLSchema#string

Julie Bouckaert

http://www.w3.org/2001/XMLSchema#string

Robert Strouse

http://www.w3.org/2001/XMLSchema#string

Solomon Langermann

http://www.w3.org/2001/XMLSchema#string

P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Structural basis of chaperone function and pilus biogenesis

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination

Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector

Functional flexibility of the FimH adhesin: insights from a random mutant library

Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis.

P304

903-15

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2733549

http://www.w3.org/2001/XMLSchema#string

P356

10.1046/J.1365-2958.2002.02915.X

http://www.w3.org/2001/XMLSchema#string

P407

P433

4

http://www.w3.org/2001/XMLSchema#string

P478

44

http://www.w3.org/2001/XMLSchema#string

P50

Gabriel Waksman

Scott J. Hultgren

P577

2002-05-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11360042

http://www.w3.org/2001/XMLSchema#string

P698

12010488

http://www.w3.org/2001/XMLSchema#string

P921

Escherichia coli