Fibrinogen is a ligand for the Staphylococcus aureus microbial surface components recognizing adhesive matrix molecules (MSCRAMM) bone sialoprotein-binding protein (Bbp). - Test2 - elhamkhani - TriplyDB

Fibrinogen is a ligand for the Staphylococcus aureus microbial surface components recognizing adhesive matrix molecules (MSCRAMM) bone sialoprotein-binding protein (Bbp).

Fibrinogen is a ligand for the Staphylococcus aureus microbial surface components recognizing adhesive matrix molecules (MSCRAMM) bone sialoprotein-binding protein (Bbp).

http://www.wikidata.org/entity/Q35313875

about

Targeting Staphylococcus aureus Toxins: A Potential form of Anti-Virulence Therapy Staphylococcus aureus vs. Osteoblast: Relationship and Consequences in Osteomyelitis Multi-disciplinary antimicrobial strategies for improving orthopaedic implants to prevent prosthetic joint infections in hip and knee A recombinant clumping factor A-containing vaccine induces functional antibodies to Staphylococcus aureus that are not observed after natural exposure Leptospira Immunoglobulin-Like Protein B Interacts with the 20th Exon of Human Tropoelastin Contributing to Leptospiral Adhesion to Human Lung Cells.Molecular Characterization of the Multiple Interactions of SpsD, a Surface Protein from Staphylococcus pseudintermedius, with Host Extracellular Matrix Proteins.Identification of the immunodominant regions of Staphylococcus aureus fibronectin-binding protein A.Novel mycobacteria antigen 85 complex binding motif on fibronectin.Leptospira Immunoglobulin-Like Protein B (LigB) Binds to Both the C-Terminal 23 Amino Acids of Fibrinogen αC Domain and Factor XIII: Insight into the Mechanism of LigB-Mediated Blockage of Fibrinogen α Chain Cross-Linking.Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen α.Molecular Characterization of a Prevalent Ribocluster of Methicillin-Sensitive Staphylococcus aureus from Orthopedic Implant Infections. Correspondence with MLST CC30 Elastin, a novel extracellular matrix protein adhering to mycobacterial antigen 85 complex Serine-Aspartate Repeat Protein D Increases Staphylococcus aureus Virulence and Survival in Blood Repeating structures of the major staphylococcal autolysin are essential for the interaction with human thrombospondin 1 and vitronectin.Scenery of Staphylococcus implant infections in orthopedics.Adhesion, invasion and evasion: the many functions of the surface proteins of Staphylococcus aureus.Cutaneous Immune Defenses Against Staphylococcus aureus Infections.Fibrinogen Is at the Interface of Host Defense and Pathogen Virulence in Staphylococcus aureus Infection.Staphylococcus aureus Aggregation and Coagulation Mechanisms, and Their Function in Host-Pathogen Interactions.The Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) Genes among Clinical Isolates of Staphylococcus aureus from Hospitalized Children.Staphylococcus aureus biofilm: a complex developmental organism.(+)-Dehydroabietic acid, an abietane-type diterpene, inhibits Staphylococcus aureus biofilms in vitro.Adaptive Upregulation of Clumping Factor A (ClfA) by Staphylococcus aureus in the Obese, Type 2 Diabetic Host Mediates Increased Virulence.A rapid method for selecting suitable animal species for studying pathogen interactions with plasma protein ligands in vivo.Molecular Interactions of Human Plasminogen with Fibronectin-binding Protein B (FnBPB), a Fibrinogen/Fibronectin-binding Protein from Staphylococcus aureus.Cell Wall-Anchored Surface Proteins of Staphylococcus aureus: Many Proteins, Multiple Functions.Clonal distribution of bone sialoprotein-binding protein gene among Staphylococcus aureus isolates associated with bloodstream infections.Complement regulator C4BP binds to Staphylococcus aureus surface proteins SdrE and Bbp inhibiting bacterial opsonization and killing.Staphylococcal Osteomyelitis: Disease Progression, Treatment Challenges, and Future Directions.Elevated serum levels of bone sialoprotein during ICU treatment predict long-term mortality in critically ill patients.

P2860

Q26752975-5CD3F294-164B-43E2-949E-B67681A1AD42 Q26774480-C9B90B48-FC80-410D-B858-AC462BAE636B Q26785872-0D398D6B-2DB6-487B-A3BA-C1316E6F38AE Q28714292-2910F2C6-B190-4F90-BEA6-07E8A340F3BE Q30848041-58E24F66-E946-4779-9652-0F062E45BFF0 Q34785604-5CAE04A7-14F7-46BC-80C2-0AFAC82543D1 Q35149380-167CD50F-DEB0-4540-9169-F64E0A6B503D Q35693993-48E06921-D3A3-4EC2-9603-4DB8EC0F41F2 Q36131278-ED60DB29-A9BC-47F0-ABE5-DF71922CF3D4 Q36137700-B6352F9D-9B0A-4A42-AB2F-89AA724671B4 Q36582469-38CF1A90-2BEE-4AC0-865D-A9EA8F3EE380 Q36596170-2DB831FA-F9CC-41C0-8901-BCB4E8C679FC Q37546975-5047C919-601B-49B8-80BE-5CA377749F54 Q37583476-F7A4E32D-50E1-4172-92B5-F773D8B14ECA Q37955951-93D2E126-78A5-414F-B975-9BAFC28BFCBB Q38171226-D3D8AAB1-0C96-4C05-B891-55F3FB6A8216 Q38524810-BB8C042E-18D7-40AA-A13E-0C58DBB2949E Q38801276-A2B4F4E5-002D-48E5-8C70-91553B541B87 Q38938178-2273A544-F575-4F73-826F-BF45D97198C9 Q38965976-62237727-32BF-4955-BE03-5976BE1CE7A3 Q39112028-40DC5C83-4516-4850-9CFB-9D00CFD24568 Q39143591-70F24194-C286-4F79-8B0F-100AC12FBC16 Q40287232-9BDC8823-AF76-45C3-9F81-87C47D0C4D37 Q40342144-D6A9DA10-105F-408F-B987-A0B6219B3E45 Q40622301-408F55C4-AC4D-4444-86B8-594A0EA9CDC4 Q40871551-11C0E897-058D-4448-8794-5ED28AA70B67 Q41899848-0F3D59C0-FF02-49E3-830E-957B6D7B0C46 Q41902927-F6EEBDD7-14E9-4538-85E5-3A0781645787 Q53708430-70A72920-CF28-48A5-8108-5F875ED1E4D5 Q55513504-09A5999B-F9BA-4F21-96D9-C7F5F3054114

P2860

Fibrinogen is a ligand for the Staphylococcus aureus microbial surface components recognizing adhesive matrix molecules (MSCRAMM) bone sialoprotein-binding protein (Bbp).

http://www.wikidata.org/entity/Q35313875

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Fibrinogen is a ligand for the ...... protein-binding protein (Bbp).

@ast

Fibrinogen is a ligand for the ...... protein-binding protein (Bbp).

@en

type

label

Fibrinogen is a ligand for the ...... protein-binding protein (Bbp).

@ast

Fibrinogen is a ligand for the ...... protein-binding protein (Bbp).

@en

prefLabel

Fibrinogen is a ligand for the ...... protein-binding protein (Bbp).

@ast

Fibrinogen is a ligand for the ...... protein-binding protein (Bbp).

@en

P1433

Q35313875-43769060-2D8C-4AA4-9A63-29B9551C349B

P1476

Q35313875-39C47201-F7E7-4F1A-898C-E4D904DABE5F

P2093

Q35313875-7630EDD2-61D9-4B5D-9855-657C0444D2B8

Q35313875-87225712-6D78-4AA5-B584-6812E2CD016C

Q35313875-A74F7DAC-314B-4EB5-8321-AA7A2BCCCB5A

Q35313875-CBB58907-22AB-4020-9BC2-0B45503A66D6

Q35313875-EFF60F32-BE2D-4211-B421-BF3EF668DB2A

P2860

Q35313875-0378732C-6C0A-40EE-905A-77C88F5663B9

Q35313875-0401E297-9CEA-4B6C-8B0E-ADE4B1CECD95

Q35313875-07C39B5A-5387-4C65-A0A9-EBD08A22FE04

Q35313875-19B70883-6C00-4E1E-9597-C0DF43190A7D

Q35313875-22FA6BBE-6E1D-447C-9209-B1E33293F727

Q35313875-280262E5-4CC1-4215-AA2A-BE181E25CEC4

Q35313875-2DE8DD25-9EB5-40DB-B2C0-81A6B55E41DF

Q35313875-3A032EC5-AA14-41BE-8F8A-89C31808B89F

Q35313875-498DD954-A047-4FCA-B39B-AD01A6E5F270

Q35313875-4AC6E9CD-07A4-480D-9270-C97589CCB9C5

P304

Q35313875-25AEF73D-658D-4A50-9AAA-2A6E2AEA384B

P31

Q35313875-1D6474C3-0F54-40CC-95EB-B3E5957E3DB2

P356

Q35313875-1AFFA9B4-5E44-4BEE-BB92-A9368E13E802

P407

Q35313875-9BB567BC-F7EE-46C2-AE89-F1BA2D128ACE

P433

Q35313875-CFFF61C6-F755-4F09-802D-A24A90806282

P478

Q35313875-267764A9-F675-4F5B-BE52-71830C32B773

P50

Q35313875-19D2607F-0BFD-4404-ACB0-1D8BC7D9CE0E

Q35313875-5BFF4BB8-6B17-46E8-B4AE-ECE5E4F44B8F

P577

Q35313875-7ABB494A-8CDA-4459-8755-1FFE27E48865

P698

Q35313875-96E99CDF-1FF6-434C-A476-5A3E9EB0D5A9

P932

Q35313875-E455C7DD-72EC-4F11-A1EB-DEF2509CB092

P356

JBC.M110.214981

P1433

Journal of Biological Chemistry

P1476

Fibrinogen is a ligand for the ...... protein-binding protein (Bbp).

@en

P2093

Emanuel Smeds

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

Jenny K Horndahl

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

Magnus Hook

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

Timothy J Foster

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

Vannakambadi K Ganesh

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

P2860

Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance

A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen

Evidence for the "dock, lock, and latch" ligand binding mechanism of the staphylococcal microbial surface component recognizing adhesive matrix molecules (MSCRAMM) SdrG

A Structural Model of the Staphylococcus aureus ClfA–Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics

Crystal structure of human fibrinogen

Clustal W and Clustal X version 2.0

Staphylococcus aureus infections

Staphylococcus aureus clumping factor A binds to complement regulator factor I and increases factor I cleavage of C3b

The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen

P304

29797-29805

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

P31

scholarly article

P356

10.1074/JBC.M110.214981

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

P407

P433

34

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

P478

286

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

P50

Vanessa V. Sarathy

P577

2011-06-03T00:00:00Z

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

P698

21642438

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

P932

3191021

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