Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection. - Wikidata - awgldk - TriplyDB

Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection.

Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection.

http://www.wikidata.org/entity/Q33943822

about

Complex networks govern coiled-coil oligomerization--predicting and profiling by means of a machine learning approach Direct inactivation of human immunodeficiency virus type 1 by a novel small-molecule entry inhibitor, DCM205 Synthetic Peptides as Protein Mimics Complexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41 Design of an engineered N-terminal HIV-1 gp41 trimer with enhanced stability and potency Molecular basis of coiled-coil oligomerization-state specificity Structural Basis for the Oligomerization-State Switch from a Dimer to a Trimer of an Engineered Cortexillin-1 Coiled-Coil Variant Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action Antibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics.Evaluation of "credit card" libraries for inhibition of HIV-1 gp41 fusogenic core formation Affinity maturation and characterization of a human monoclonal antibody against HIV-1 gp41 Vaccination with peptide mimetics of the gp41 prehairpin fusion intermediate yields neutralizing antisera against HIV-1 isolates.A low-molecular-weight entry inhibitor of both CCR5- and CXCR4-tropic strains of human immunodeficiency virus type 1 targets a novel site on gp41 Binding of HIV-1 gp41-directed neutralizing and non-neutralizing fragment antibody binding domain (Fab) and single chain variable fragment (ScFv) antibodies to the ectodomain of gp41 in the pre-hairpin and six-helix bundle conformations Novel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicides Mechanism of resistance to S138A substituted enfuvirtide and its application to peptide design Investigation of the network of preferred interactions in an artificial coiled-coil association using the peptide array technique.Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.Covalent fusion inhibitors targeting HIV-1 gp41 deep pocket.Small molecule mimetics of an HIV-1 gp41 fusion intermediate as vaccine leads.The conserved residue Arg46 in the N-terminal heptad repeat domain of HIV-1 gp41 is critical for viral fusion and entry Single-chain protein mimetics of the N-terminal heptad-repeat region of gp41 with potential as anti-HIV-1 drugs.Biochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor design Artificial 64-Residue HIV-1 Enhancer-Binding Peptide Is a Potent Inhibitor of Viral Replication in HIV-1-Infected Cells Membrane-Active Sequences within gp41 Membrane Proximal External Region (MPER) Modulate MPER-Containing Peptidyl Fusion Inhibitor Activity and the Biosynthesis of HIV-1 Structural Proteins Potent anti-HIV-1 activity of N-HR-derived peptides including a deep pocket-forming region without antagonistic effects on T-20 Polyvalent side chain peptide-synthetic polymer conjugates as HIV-1 entry inhibitors Progress in identifying peptides and small-molecule inhibitors targeted to gp41 of HIV-1.Cell surface assembly of HIV gp41 six-helix bundles for facile, quantitative measurements of hetero-oligomeric interactions.Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency.Site-specific Isopeptide Bridge Tethering of Chimeric gp41 N-terminal Heptad Repeat Helical Trimers for the Treatment of HIV-1 Infection.Peptides in the treatment of AIDS.Insights into the mechanism of HIV-1 envelope induced membrane fusion as revealed by its inhibitory peptides.Escape from human immunodeficiency virus type 1 (HIV-1) entry inhibitors.Site-Specific Polymer Attachment to HR2 Peptide Fusion Inhibitors against HIV-1 Decreases Binding Association Rates and Dissociation Rates Rather Than Binding Affinity.A synthetic C34 trimer of HIV-1 gp41 shows significant increase in inhibition potency.Conserved salt bridge between the N- and C-terminal heptad repeat regions of the human immunodeficiency virus type 1 gp41 core structure is critical for virus entry and inhibition.A multi-functional peptide as an HIV-1 entry inhibitor based on self-concentration, recognition, and covalent attachment.

P2860

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P2860

Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection.

http://www.wikidata.org/entity/Q33943822

description

2005 nî lūn-bûn

@nan

2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի օգոստոսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Covalent stabilization of coil ...... inhibitors of viral infection.

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Covalent stabilization of coil ...... inhibitors of viral infection.

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type

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Covalent stabilization of coil ...... inhibitors of viral infection.

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Covalent stabilization of coil ...... inhibitors of viral infection.

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Covalent stabilization of coil ...... inhibitors of viral infection.

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Covalent stabilization of coil ...... inhibitors of viral infection.

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Proceedings of the National Academy of Sciences of the United States of America

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Covalent stabilization of coil ...... inhibitors of viral infection.

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P2093

Anthony V Carella

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Antonello Pessi

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Elisabetta Bianchi

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Marco Finotto

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Michael D Miller

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Paolo Ingallinella

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Renee Hrin

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Romas Geleziunas

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William A Schleif

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Xiaoli S Hou

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P2860

Identification of a major co-receptor for primary isolates of HIV-1

Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41

Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket

Core structure of gp41 from the HIV envelope glycoprotein

Atomic structure of the ectodomain from HIV-1 gp41

Atomic structure of a thermostable subdomain of HIV-1 gp41

Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues

The structural biology of type I viral membrane fusion

A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition

Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor

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12903-12908

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102

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