A PREDICTED 3-DIMENSIONAL STRUCTURE OF CD4 AND THE LOCATION OF THE HIV GP120 BINDING REGION

A PREDICTED 3-DIMENSIONAL STRUCTURE OF CD4 AND THE LOCATION OF THE HIV GP120 BINDING REGION

Chi tiết về thư mục
Những tác giả chính:	Mcgregor, M, Bates, P, Islam, S, Sternberg, M, Sattentau, Q
Định dạng:	Conference item
Được phát hành:	1990

Những quyển sách tương tự

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Interactions of HIV gp120 with the CD4 molecule on lymphocytes and in the nervous system.
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Enhancement of soluble CD4-mediated HIV neutralization and gp 120 binding by CD4 autoantibodies and monoclonal antibodies.
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Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120.
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A predicted three-dimensional structure for the human immunodeficiency virus binding domains of CD4 antigen.
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Dissociation of gp120 from HIV-1 virions induced by soluble CD4.
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Conformational transitions in CD4 due to complexation with HIV envelope glycoprotein gp120.
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Detecting SIV gp120 and its interaction with soluble CD4 by ELISA.
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HIV gp120: double lock strategy foils host defences.
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Conservation of HIV-1 gp120 neutralizing epitopes after formalin inactivation.
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A region in domain 1 of CD4 distinct from the primary gp120 binding site is involved in HIV infection and virus-mediated fusion.
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Towards a structure of the HIV-1 envelope glycoprotein gp120: an immunochemical approach.
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Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans.
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Crystal structures of HIV-1 gp120 envelope glycoprotein in complex with NBD analogues that target the CD4-binding site.
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The role of CD4 in HIV binding and entry.
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Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer.
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