Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage.
about
Human Non-neutralizing HIV-1 Envelope Monoclonal Antibodies Limit the Number of Founder Viruses during SHIV Mucosal Infection in Rhesus MacaquesDevelopmental pathway for potent V1V2-directed HIV-neutralizing antibodiesStructural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan ShieldA gp41 MPER-specific Llama VHH Requires a Hydrophobic CDR3 for Neutralization but not for Antigen RecognitionStructural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers.A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodiesAn efficiently cleaved HIV-1 clade C Env selectively binds to neutralizing antibodiesFunctional stability of unliganded envelope glycoprotein spikes among isolates of human immunodeficiency virus type 1 (HIV-1)Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine targetEffect of trimerization motifs on quaternary structure, antigenicity, and immunogenicity of a noncleavable HIV-1 gp140 envelope glycoprotein.In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type 1Comparing antigenicity and immunogenicity of engineered gp120.A novel, live-attenuated vesicular stomatitis virus vector displaying conformationally intact, functional HIV-1 envelope trimers that elicits potent cellular and humoral responses in mice.Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimerNature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1.Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface.Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.Increased functional stability and homogeneity of viral envelope spikes through directed evolution.Chimeric HIV-1 envelope glycoproteins with potent intrinsic granulocyte-macrophage colony-stimulating factor (GM-CSF) activity.An HIV-1 envelope glycoprotein trimer with an embedded IL-21 domain activates human B cellsStable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure.HIV-1 envelope glycoprotein variable loops are indispensable for envelope structural integrity and virus entry.Structure-based vaccine design in HIV: blind men and the elephant?Binding interactions between soluble HIV envelope glycoproteins and quaternary-structure-specific monoclonal antibodies PG9 and PG16.A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene.HIV type 1 Env precursor cleavage state affects recognition by both neutralizing and nonneutralizing gp41 antibodies.Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01.Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors.Well-ordered trimeric HIV-1 subtype B and C soluble spike mimetics generated by negative selection display native-like propertiesSingle-Chain Soluble BG505.SOSIP gp140 Trimers as Structural and Antigenic Mimics of Mature Closed HIV-1 Env.The role of amino acid changes in the human immunodeficiency virus type 1 transmembrane domain in antibody binding and neutralizationIntraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimer.PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4.A New Approach to Produce HIV-1 Envelope Trimers: BOTH CLEAVAGE AND PROPER GLYCOSYLATION ARE ESSENTIAL TO GENERATE AUTHENTIC TRIMERSAntigenicity and immunogenicity of HIV-1 consensus subtype B envelope glycoproteins.Targeted Isolation of Antibodies Directed against Major Sites of SIV Env Vulnerability.Structure and Recognition of a Novel HIV-1 gp120-gp41 Interface Antibody that Caused MPER Exposure through Viral Escape.Antigenic characterization of the human immunodeficiency virus (HIV-1) envelope glycoprotein precursor incorporated into nanodiscs.HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelope glycoproteins.
P2860
Q27318508-F7DB7655-922B-4602-9A26-BAC0D35B55ADQ27644515-66DA6E81-6B74-4A08-AEFA-89D2083C46C8Q27658449-8289003A-3A1D-495B-818C-6DF4337A0A08Q27675032-87065FC8-88DF-414E-88F0-773A20B06434Q27676864-19559E67-47D7-4CAD-B6B4-E1D2FC10D3B6Q27683553-4B16CB08-1C2B-4D97-9E1E-7E5C803B2B3DQ28299280-0D5F12D9-1C14-491C-B1F8-E9953DB985D1Q28545185-5889BBA5-EAE9-4EBA-A338-EE05C184C90DQ28743199-7432D77D-990A-4429-8E8D-E5B77BA3319DQ29547347-2C417249-F640-443A-8F78-EFCEC15F48B0Q33571825-FE9BD64A-071B-4898-AF2B-B8A38AE56CD5Q33725718-642F72B2-9AF9-4B1E-931B-DB905F60F3DFQ33984309-B22B5F61-C3D7-4921-A4C2-A159FCCB8E58Q34172295-AFC3A685-0C08-49BE-99FC-47D759CE5795Q34292319-0383DB94-1D78-44E8-BEC9-B77F3D39C1AEQ34434854-73229B5E-C6FB-406B-A65D-5BB17A205E16Q34473958-1E790B1B-2E92-4331-B8C6-E1FE3A216D46Q34555891-222F05DE-07F1-4FB9-8324-9F0FCE30C998Q34611144-72C00C20-3F39-41FF-A596-E6FBCAB368F3Q34658136-6462D74A-7193-4782-BE6D-AB758B2A3340Q34796885-6D1B945C-6D51-49D9-8245-DC9E1DE79A9BQ34831341-521FDC57-076B-40A4-AB75-3008ACD7B4B9Q34924647-A9F7DAC6-3AD6-4012-985D-449B87690961Q34987048-FD7FC5C9-D4E8-4052-A17D-C6C0609F1C47Q35077716-51E78352-DD44-46CE-A69A-36864C39892BQ35110976-9F661FBB-A977-4A88-A911-196808A17185Q35173635-E6AA4107-2FCD-4DB6-8EC6-5D5ECAE2BC2AQ35192782-125495A6-A06A-45D9-8DD3-9D54122CCA1CQ35382871-BFB0F24A-5B7D-4E7E-A8B3-CDE19A40B51DQ35540033-1C3773B1-90F0-4E0D-BE31-5AF8D94E90E1Q35641498-BC633687-3097-46FF-A185-09A4BD58DD38Q35644971-20186856-A8E9-4BD7-A6C1-B023FD8FBEBDQ35647772-7BC2E69E-9B62-4C9D-B376-6444968D1F1BQ35868102-864993A3-EBC8-4265-8ED6-DCC07A4D53DAQ35925858-35EEA434-5F71-477D-B600-C20438B091FFQ35933555-9F047A44-4299-4145-BEFA-038B00B3383FQ35985519-B29DF3AC-52B6-4E13-B67D-9E7ED452219FQ36246403-94865011-A357-4AF9-B07A-A68EEA51BE11Q36267348-D7F2D478-2582-4EFD-AB30-08C53A8E4783Q36276274-940D145D-43BA-43B2-A3E7-F7833529FB19
P2860
Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Selective recognition of oligo ...... efficient precursor cleavage.
@en
type
label
Selective recognition of oligo ...... efficient precursor cleavage.
@en
prefLabel
Selective recognition of oligo ...... efficient precursor cleavage.
@en
P1433
P1476
Selective recognition of oligo ...... efficient precursor cleavage.
@en
P2093
Marie Pancera
Richard Wyatt
P304
P356
10.1016/J.VIROL.2004.10.042
P407
P577
2005-02-01T00:00:00Z