Structure of C3b in complex with CRIg gives insights into regulation of complement activation
about
Molecular basis for genetic resistance of Anopheles gambiae to Plasmodium: structural analysis of TEP1 susceptible and resistant allelesSubstrate recognition by complement convertases revealed in the C5-cobra venom factor complexA heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiaeStructures of C3b in complex with factors B and D give insight into complement convertase formationStructural basis for engagement by complement factor H of C3b on a self surfaceStructure of complement fragment C3b-factor H and implications for host protection by complement regulatorsStructure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variationsHuman alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3Compstatin: a complement inhibitor on its way to clinical applicationStructural basis for conserved complement factor-like function in the antimalarial protein TEP1.Factor B structure provides insights into activation of the central protease of the complement systemThe Structure of OMCI, a Novel Lipocalin Inhibitor of the Complement SystemA novel inhibitor of the alternative pathway of complement reverses inflammation and bone destruction in experimental arthritisInsights into complement convertase formation based on the structure of the factor B-cobra venom factor complexStructure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibitionStructural and Functional Analysis of a C3b-specific Antibody That Selectively Inhibits the Alternative Pathway of ComplementThe Crystal Structure of Cobra Venom Factor, a Cofactor for C3- and C5-Convertase CVFBbStructural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitorStructural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureusMolecular Basis for Complement Recognition and Inhibition Determined by Crystallographic Studies of the Staphylococcal Complement Inhibitor (SCIN) Bound to C3c and C3bA structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3dA Structurally Dynamic N-terminal Helix Is a Key Functional Determinant in Staphylococcal Complement Inhibitor (SCIN) ProteinsDiversity in the C3b Convertase Contact Residues and Tertiary Structures of the Staphylococcal Complement Inhibitor (SCIN) Protein FamilyInhibiting Alternative Pathway Complement Activation by Targeting the Factor D ExositeCrystal Structure of C5b-6 Suggests Structural Basis for Priming Assembly of the Membrane Attack ComplexStructural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3Structure of a bacterial α2-macroglobulin reveals mimicry of eukaryotic innate immunityInfections of People with Complement Deficiencies and Patients Who Have Undergone SplenectomyDynamic structural changes during complement C3 activation analyzed by hydrogen/deuterium exchange mass spectrometryComplex interactions with several arms of the complement system dictate innate and humoral immunity to adenoviral vectors.Improving therapeutic efficacy of a complement receptor by structure-based affinity maturation.Proteolysis of complement factors iC3b and C5 by the serine protease prostate-specific antigen in prostatic fluid and seminal plasmaDevelopment of Sjogren's syndrome in nonobese diabetic-derived autoimmune-prone C57BL/6.NOD-Aec1Aec2 mice is dependent on complement component-3.Commandeering a biological pathway using aptamer-derived molecular adaptorsConvertase inhibitory properties of Staphylococcal extracellular complement-binding protein.Complement control protein factor H: the good, the bad, and the inadequate.Functional basis for complement evasion by staphylococcal superantigen-like 7.Human C3 mutation reveals a mechanism of dense deposit disease pathogenesis and provides insights into complement activation and regulation.Allosteric inhibition of complement function by a staphylococcal immune evasion protein.The efficacy of pneumococcal capsular polysaccharide-specific antibodies to serotype 3 Streptococcus pneumoniae requires macrophages.
P2860
Q21558783-65AFF8D6-AD00-499F-A677-FCA536D23F77Q24336071-211795BD-4557-4E23-AB4E-530AD38566BBQ24597714-8E98854D-05A7-4662-AA04-AD71DC9A1165Q24601226-D6625DAE-E6A5-4FAA-AE43-C17B85892CF5Q24604385-D48C3E17-7FF1-469A-855C-634566ED136AQ24646723-AD0913A9-BBE4-4E22-86DD-220AD33D3890Q24648540-AF4D7C4B-A6CA-419C-BC1F-DF85035C4168Q24654232-FCFFCB17-2148-4024-9B95-12F904C4C29CQ24658454-5364434C-2F82-4163-BB89-4A6DC5852758Q24681538-BDAF2D59-5702-40C9-9DC3-0FF93DDA8917Q27643861-A879A906-7D02-4701-999E-35796CF805FCQ27644514-A67937F1-5825-43F9-82AF-878911E30F2FQ27645256-D4756091-AAFA-406E-8DA4-977F5F55FFFFQ27646432-6CF8608C-FB2F-488F-A465-24DBB0E1130DQ27647015-C9F7E8CC-DA31-44BA-8CB2-47B3BCE1B68EQ27653668-D6596D8D-F86A-4F1E-B103-A1ACBF787259Q27654785-C57AF1FB-A033-4F38-AD67-B709353828BFQ27655786-6072C255-4CE9-4CC3-ABCA-FBCCF319640DQ27659556-54830447-1C6D-45E4-8C74-A6C4B0AC0FA3Q27663585-227BAFAC-A1D9-4697-A2E9-CB803F48A885Q27665619-3AD2900B-88DF-453A-A1D8-80CC10A54C9FQ27675451-F5673E4F-E2D6-4DF0-8D63-37A147BFBD18Q27675598-0E2DEB4F-DE38-4CCA-ACBD-688A8147B90DQ27677455-07756B6A-01B8-4282-B2EB-29690BD2920CQ27678501-EE3D7CF6-20F4-48E4-8592-85A78BD43569Q27680051-04935379-E276-4CC3-BD65-D42C30B6226EQ27695619-A2A1C83F-072F-4E97-91B0-9462E8679EDFQ28972389-92260330-D669-4113-A6F8-04998B56D558Q33331674-69806DDC-CABF-4333-9904-D61A44191289Q33380283-8348FB31-3CD2-4071-800C-8E0E758D3A48Q33510862-C751EACF-94AB-486F-AD85-1775E1603E49Q33684468-547C1CBA-43B3-4BE2-B895-82E639FB5591Q33771577-B3CA4674-41C4-4419-840A-BD10110DA74BQ33783191-AB2D267C-F9D3-4735-B2DC-B68A16F98C3FQ33832527-8AC2C92F-9DCE-4007-BF40-478882A37A7FQ34067107-3A791C7C-1E77-47C1-93C3-0E2FCDA6E6ABQ34137944-6022E8DE-C755-46FD-AAA0-A9149782FDCBQ34162206-B434EEFA-0E97-4E6B-ADAD-EDCB0D0CA7C9Q34200056-0AE8CD46-F5C4-430D-B8CF-F5E97A2738A1Q34238386-754E2517-53E9-4BE4-A5FC-D583F51ED6AA
P2860
Structure of C3b in complex with CRIg gives insights into regulation of complement activation
description
2006 nî lūn-bûn
@nan
2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Structure of C3b in complex wi ...... ation of complement activation
@ast
Structure of C3b in complex wi ...... ation of complement activation
@en
Structure of C3b in complex wi ...... ation of complement activation
@nl
type
label
Structure of C3b in complex wi ...... ation of complement activation
@ast
Structure of C3b in complex wi ...... ation of complement activation
@en
Structure of C3b in complex wi ...... ation of complement activation
@nl
prefLabel
Structure of C3b in complex wi ...... ation of complement activation
@ast
Structure of C3b in complex wi ...... ation of complement activation
@en
Structure of C3b in complex wi ...... ation of complement activation
@nl
P2093
P3181
P356
P1433
P1476
Structure of C3b in complex wi ...... ation of complement activation
@en
P2093
Christian Wiesmann
JianPing Yin
Karim Y Helmy
Kenneth J Katschke
Laura DeForge
Lizette Embuscado
Philip E Hass
Scott A McCallum
Wayne J Fairbrother
P2888
P304
P3181
P356
10.1038/NATURE05263
P407
P577
2006-11-09T00:00:00Z
P6179
1043041201