Mutational analyses of the recombinant globular regions of human C1q A, B, and C chains suggest an essential role for arginine and histidine residues in the C1q-IgG interaction.
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Engineered Fc variant antibodies with enhanced ability to recruit complement and mediate effector functionsInhibition of the classical pathway of complement by meningococcal capsular polysaccharidesA C1q domain containing protein from scallop Chlamys farreri serving as pattern recognition receptor with heat-aggregated IgG binding activityComplement System Part I - Molecular Mechanisms of Activation and Regulation.Structural insights into the C1q domain of Caprin-2 in canonical Wnt signaling.Structural and functional anatomy of the globular domain of complement protein C1q.The C1q family of proteins: insights into the emerging non-traditional functionsStructural and Functional Characterization of a Single-Chain Form of the Recognition Domain of Complement Protein C1q.Identification of the gC1qR sites for the HIV-1 viral envelope protein gp41 and the HCV core protein: Implications in viral-specific pathogenesis and therapy.Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: mutational studies using recombinant globular head modules of human C1q A, B, and C chainsAnalysis of the Interaction between Globular Head Modules of Human C1q and Its Candidate Receptor gC1qR.Complement Protein C1q Interacts with DC-SIGN via Its Globular Domain and Thus May Interfere with HIV-1 Transmission.Complement activation and disease: protective effects of hyperbilirubinaemia.Complement and non-complement activating functions of C1q: a prototypical innate immune molecule.C1q: A fresh look upon an old molecule.Interactions of complement proteins C1q and factor H with lipid A and Escherichia coli: further evidence that factor H regulates the classical complement pathwayComplement C1q-target proteins recognition is inhibited by electric moment effectors.Is the A-Chain the Engine That Drives the Diversity of C1q Functions? Revisiting Its Unique Structure.Importance of carbohydrate in the interaction of Tamm-Horsfall protein with complement 1q and inhibition of classical complement activation.
P2860
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P2860
Mutational analyses of the recombinant globular regions of human C1q A, B, and C chains suggest an essential role for arginine and histidine residues in the C1q-IgG interaction.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Mutational analyses of the rec ...... es in the C1q-IgG interaction.
@en
Mutational analyses of the rec ...... es in the C1q-IgG interaction.
@nl
type
label
Mutational analyses of the rec ...... es in the C1q-IgG interaction.
@en
Mutational analyses of the rec ...... es in the C1q-IgG interaction.
@nl
prefLabel
Mutational analyses of the rec ...... es in the C1q-IgG interaction.
@en
Mutational analyses of the rec ...... es in the C1q-IgG interaction.
@nl
P2093
P50
P1476
Mutational analyses of the rec ...... ues in the C1q-IgG interaction
@en
P2093
Aleksandra Zlatarova
Boris P Atanasov
Ivanka G Tsacheva
Kenneth B M Reid
Magdalena I Tchorbadjieva
Mihaela G Gadjeva
Mihaela S Kojouharova
Robert B Sim
P304
P356
10.4049/JIMMUNOL.172.7.4351
P407
P577
2004-04-01T00:00:00Z