Results 41 to 50 of about 3,038,180 (280)

Three-helix bundle structures

open access: yes, 2020
Relevant data in "Enumeration and comprehensive in-silico modeling of three-helix bundle structures composed of typical αα-hairpins" : https://doi.org/10.1186/s12859-021-04380-5 This repository contains following materials.
Sakuma Koya
core   +1 more source

Structure‐forward targeting of claudins with synthetic binders

open access: yesFEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source

The Six-Helix Bundle of Human Immunodeficiency Virus Env Controls Pore Formation and Enlargement and Is Initiated at Residues Proximal to the Hairpin Turn [PDF]

open access: yesJournal of Virology, 2009
ABSTRACT Residues that create the grooves of the human immunodeficiency virus type 1 (HIV-1) Env triple-stranded coiled coil (HR1) and the residues that pack into the grooves (HR2) to complete the formation of the six-helix bundle (6HB) were mutated.
Ruben M, Markosyan   +2 more
openaire   +2 more sources

Efficient trapping of HIV-1 envelope protein by hetero-oligomerization with an N-helix chimera

open access: yesRetrovirology, 2005
Background The N-heptad repeat region of the HIV-1 Transmembrane Envelope protein is a trimerization domain that forms part of a "six helix bundle" crucial to Envelope-mediated membrane fusion.
Silver Jonathan, Ou Wu
doaj   +1 more source

New Design of Helix Bundle Peptide−Polymer Conjugates

open access: yes, 2016
We present a new design of peptide−polymer conjugates where a polymer chain is covalently linked to the side chain of a helix bundle-forming peptide. The effect of conjugated polymer chains on the peptide structure was examined using a de novo designed ...
William F. DeGrado (276486)   +3 more
core   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

open access: yesFEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang   +2 more
wiley   +1 more source

Anti-HIV-1 activity of cellulose acetate phthalate: Synergy with soluble CD4 and induction of "dead-end" gp41 six-helix bundles [PDF]

open access: yesBMC Infectious Diseases, 2002
Cellulose acetate phthalate (CAP), a promising candidate microbicide for prevention of sexual transmission of the human immunodeficiency virus type 1 (HIV-1) and other sexually transmitted disease (STD) pathogens, was shown to inactivate HIV-1 and to block the coreceptor binding site on the virus envelope glycoprotein gp120.
Li Yun-Yao   +4 more
openaire   +3 more sources

Template-assembled peptide models of the N-peptide helix bundle from HIV-1 Gp41

open access: yes, 2007
The HIV-1 pandemic is one of the most serious health problems facing the world today. Infection of target cells by HIV-1 is initiated by fusion of viral and cell membranes, which is mediated by the viral glycoproteins, gp120 and gp41.
Xu, Weiming
core   +1 more source

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

open access: yesFEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav   +2 more
wiley   +1 more source

The Cytoplasmic Tail Slows the Folding of Human Immunodeficiency Virus Type 1 Env from a Late Prebundle Configuration into the Six-Helix Bundle [PDF]

open access: yesJournal of Virology, 2005
ABSTRACT Effects of the cytoplasmic tail (CT) of human immunodeficiency virus type 1 Env on the process of membrane fusion were investigated. Full-length Env (wild type [WT]) and Env with its CT truncated (ΔCT) were expressed on cell surfaces, these cells were fused to target cells, and the inhibition of fusion by peptides that prevent Env ...
Levon G, Abrahamyan   +5 more
openaire   +2 more sources

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