Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights. - Test2 - elhamkhani - TriplyDB

Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights.

Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights.

http://www.wikidata.org/entity/Q39757500

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Bivalent and co-operative binding of complement factor H to heparan sulfate and heparin Near-planar solution structures of mannose-binding lectin oligomers provide insight on activation of lectin pathway of complement The Fab conformations in the solution structure of human immunoglobulin G4 (IgG4) restrict access to its Fc region: implications for functional activity Atomistic modelling of scattering data in the Collaborative Computational Project for Small Angle Scattering (CCP-SAS).Allosteric inhibition of complement function by a staphylococcal immune evasion protein.A revised mechanism for the activation of complement C3 to C3b: a molecular explanation of a disease-associated polymorphism The solution structure of heparan sulfate differs from that of heparin: implications for function.The solution structures of two human IgG1 antibodies show conformational stability and accommodate their C1q and FcγR ligands.The solution structures of native and patient monomeric human IgA1 reveal asymmetric extended structures: implications for function and IgAN disease Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering.How random are intrinsically disordered proteins? A small angle scattering perspective.Non-linearity of the collagen triple helix in solution and implications for collagen function.Biological physics at large facilities: from molecule to cell Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes.Masking of the Fc region in human IgG4 by constrained X-ray scattering modelling: implications for antibody function and therapy Two distinct conformations of factor H regulate discrete complement-binding functions in the fluid phase and at cell surfaces

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Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights.

http://www.wikidata.org/entity/Q39757500

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年學術文章

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2009年學術文章

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Constrained solution scatterin ...... als novel biological insights.

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Constrained solution scatterin ...... als novel biological insights.

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type

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Constrained solution scatterin ...... als novel biological insights.

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Constrained solution scatterin ...... als novel biological insights.

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Constrained solution scatterin ...... als novel biological insights.

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Constrained solution scatterin ...... als novel biological insights.

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RSIF.2009.0164.FOCUS

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Journal of the Royal Society Interface

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Constrained solution scatterin ...... als novel biological insights.

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Alexandra Bonner

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Azubuike I Okemefuna

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Keying Li

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Ruodan Nan

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Stephen J Perkins

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P2860

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Structural basis for complement factor H linked age-related macular degeneration

The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling

Structure of complement receptor 2 in complex with its C3d ligand

Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling

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The extended multidomain solution structures of the complement protein Crry and its chimeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: implications for function and therapy

Associative and structural properties of the region of complement factor H encompassing the Tyr402His disease-related polymorphism and its interactions with heparin

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S679-96

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scholarly article

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10.1098/RSIF.2009.0164.FOCUS

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6 Suppl 5

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