Results 131 to 140 of about 13,547 (178)
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Two Interaction Modes of the gp41-Derived Peptides with gp41 and Their Correlation with Antimembrane Fusion Activity

Biochemical and Biophysical Research Communications, 1999
Peptides derived from gp41 effectively block the gp41-mediated cell fusion or HIV infection. A 36-mer (naDP178), 51-mer (C51) and 27-mer peptide (C27) from the membrane proximal region of gp41 have been examined their interaction modes with the coiled-coil motif of gp41 presented in thioredoxin (Trx-N) or the bacterially expressed ectodomain of gp41 ...
Moo-Jin Suh, Yeon Gyu Yu, Eun-Rhan Woo
exaly   +3 more sources

HIV-1 gp41 binding proteins and antibodies to gp41 could inhibit enhancement of human raji cell mhc class I and II expression by gp41

Molecular Immunology, 1994
Based on our findings, that HIV-1 soluble gp41 could bind to several proteins on the human, T, B and monocyte cells independently of CD4, we examined the effect of HIV-1 soluble gp41 (sgp41;Env amino acids 539-684) on surface expression of MHC I and II, ICAM-1 and CD21 molecules on human Raji cells.
Hermann Katinger   +2 more
exaly   +3 more sources

Development of HIV-1 Fusion Inhibitors Targeting gp41

Current Medicinal Chemistry, 2014
The HIV-1 envelope protein glycoprotein 41 (gp41) is crucial in the HIV-1 infection process, therefore gp41 has emerged as an attractive target for drug design against AIDS. During the past few decades, tremendous efforts have been made on developing inhibitors that can prevent the HIV-1 entry process via suppressing functional gp41.
Fangwei Shao
exaly   +5 more sources

On the Interaction Between gp41 and Membranes: The Immunodominant Loop Stabilizes gp41 Helical Hairpin Conformation

Journal of Molecular Biology, 2003
gp41 is the protein responsible for the process of membrane fusion that allows primate lentiviruses (HIV and SIV) to enter into their host cells. gp41 ectodomain contains an N-terminal and a C-terminal heptad repeat region (NHR and CHR) connected by an immunodominant loop.
Sergio G, Peisajovich   +4 more
openaire   +2 more sources

HIV‐1 gp41 and gp160 are hyperthermostable proteins in a mesophilic environment

European Journal of Biochemistry, 2004
HIV gp41(24–157) unfolds cooperatively over the pH range of 1.0–4.0 with Tm values of > 100 °C. At pH 2.8, protein unfolding was 80% reversible and the ΔHvH/ΔHcal ratio of 3.7 is indicative of gp41 being trimeric. No evidence for a monomer–trimer equilibrium in the concentration range of 0.3–36 µm was obtained by DSC and tryptophan fluorescence ...
Krell, Tino   +10 more
openaire   +3 more sources

Alanine Scanning Mutagenesis of HIV-1 gp41 Heptad Repeat 1: Insight into the gp120−gp41 Interaction

Biochemistry, 2010
On the basis of mutagenesis, biochemical, and structural studies, heptad repeat 1 of HIV gp41 (HR1) has been shown to play numerous critical roles in HIV entry, including interacting with gp120 in prefusion states and interacting with gp41 heptad repeat 2 (HR2) in the fusion state.
Jayita, Sen   +5 more
openaire   +2 more sources

Antigenic variation of the dominant gp41 epitope in Africa

AIDS, 1993
To determine the value of (combinations of) synthetic peptides representing immunodominant sites on HIV-1/HIV-2 transmembrane proteins for the detection and discrimination between HIV-1 and HIV-2 infection in various populations.Two 24-mer synthetic peptides derived from immunodominant sites on the HIV-1 and HIV-2 transmembrane proteins were used ...
Lange, J. M.   +9 more
openaire   +2 more sources

Helical Interactions in the HIV-1 gp41 Core Reveal Structural Basis for the Inhibitory Activity of gp41 Peptides,

Biochemistry, 2000
The HIV-1 gp41 envelope protein mediates membrane fusion that leads to virus entry into the cell. The core structure of fusion-active gp41 is a six-helix bundle in which an N-terminal three-stranded coiled coil is surrounded by a sheath of antiparallel C-terminal helices.
W, Shu   +5 more
openaire   +2 more sources

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