Results 21 to 30 of about 24,285 (259)

Elucidating the Basis for Permissivity of the MT-4 T-Cell Line to Replication of an HIV-1 Mutant Lacking the gp41 Cytoplasmic Tail

Journal of Virology, 2020
The HIV-1 Env cytoplasmic tail (CT) is required for efficient Env incorporation into nascent particles and viral transmission in primary CD4+ T cells. The MT-4 T-cell line has been reported to support multiple rounds of infection of HIV-1 encoding a gp41
M. Fernandez, H. K. Hoffman, Nairi Pezeshkian, P. Tedbury, S. V. van Engelenburg, E. Freed   +5 more
semanticscholar   +1 more source

HIV Transmembrane Glycoprotein Conserved Domains and Genetic Markers Across HIV-1 and HIV-2 Variants

Frontiers in Microbiology, 2022
HIV envelope transmembrane glycoproteins gp41 (HIV-1) and gp36 (HIV-2) present high variability and play a key role in the HIV-host cell membrane's fusion, as a target for human broadly neutralizing antibodies (bnAbs) and drugs.
Ana Valadés-Alcaraz, Roberto Reinosa, África Holguín   +2 more
doaj   +1 more source

Sensitive detection systems for infectious agents in xenotransplantation*

Xenotransplantation, EarlyView., 2020
Abstract Xenotransplantation of pig cells, tissues, or organs may be associated with transmission of porcine microorganisms, first of all of viruses, to the transplant recipient, potentially inducing a disease (zoonosis). I would like to define detection systems as the complex of sample generation, sample preparation, sample origin, time of sampling ...
Joachim Denner
wiley   +1 more source

A gp41 MPER-specific llama VHH requires a hydrophobic CDR3 for neutralization but not for antigen recognition [PDF]

, 2013
The membrane proximal external region (MPER) of the HIV-1 glycoprotein gp41 is targeted by the broadly neutralizing antibodies 2F5 and 4E10. To date, no immunization regimen in animals or humans has produced HIV-1 neutralizing MPER-specific antibodies ...
Ramos, Alejandra, Alexandre M. J. J. Bonvin (18079), David Lutje Hulsik, Verrips, C. Theo, Ying-ying Liu, Liu, Ying-ying, Battella, Simone, Jean-Pierre Simorre, C. Theo Verrips (200972), Miriam Hock, Miriam Hock (386536), Lucy Rutten (386540), Nika M. Strokappe (386532), Davis, David, Hinz, Andreas, Alejandra Ramos, Mohamed El Khattabi (386534), Bonvin, Alexandre M. J. J., Michael S Seaman, Rutten, Lucy, Alexandre M J J Bonvin, Simone Battella, Marlén M. I. Aasa-Chapman (208291), Pascal Poignard (244468), Sabin, Charles, Pascal Poignard, Seaman, Michael S., Anna Forsman Quigley, Pauline Macheboeuf, Seaman, Michael, Andreas Hinz (237046), Forsman Quigley, Anna, Anna Forsman Quigley (177474), Strokappe, Nika M, C Theo Verrips, Simorre, Jean-Pierre, Mohamed El Khattabi, Hulsik, David Lutje, Andreas Hinz, Winfried Weissenhorn (214542), McCoy, Laura E., Langedijk, Johannes P M, Johannes P. M. Langedijk (254439), Pauline Macheboeuf (386537), Charles Sabin, Marlén M I Aasa-Chapman, David Davis (190113), Robin A. Weiss (254468), Johannes P M Langedijk, Favier, Adrien, Lucy Rutten, Laura E. McCoy (386535), Adrien Favier (386539), Hock, Miriam, Alejandra Ramos (386538), Weiss, Robin A., Nika M Strokappe, David Lutje Hulsik (177480), Winfried Weissenhorn, Macheboeuf, Pauline, Lutje Hulsik, David, David Davis, Robin A Weiss, Aasa-Chapman, Marlén M. I., Strokappe, Nika M., Ying-ying Liu (386531), Weissenhorn, Winfried, Adrien Favier, Weiss, Robin A, Simone Battella (386533), Langedijk, Johannes P. M., Bonvin, Alexandre M J J, Michael S. Seaman (155998), Jean-Pierre Simorre (177519), El Khattabi, Mohamed, Seaman, Michael S, Aasa-Chapman, Marlén M I, Laura E McCoy, Poignard, Pascal, Verrips, C Theo, Charles Sabin (75940), Weissenhorn W, Poignard P, Hock M, McCoy LE, Simorre JP, Rutten L., Aasa-Chapman Marlén M. I., Hock Miriam, Davis David, Rutten Lucy, Macheboeuf P, El Khattabi M, Battella Simone, Hinz A, Forsman Quigley A, Weiss Robin A., Langedijk JP, Lutje Hulsik D, Liu YY, Aasa Chapman MM, Ramos Alejandra, Simorre Jean-Pierre, Verrips C. Theo, Ramos A, Liu Ying-ying, Sabin C, Favier A, Macheboeuf Pauline, Weiss RA, Weissenhorn Winfried, Poignard Pascal, Davis D, Langedijk Johannes P. M., Hinz Andreas, Bonvin Alexandre M. J. J., Seaman Michael S., El Khattabi Mohamed, Bonvin AM, Strokappe NM, Sabin Charles, Strokappe Nika M., Seaman MS, Lutje Hulsik David, McCoy Laura E., Verrips CT, Forsman Quigley Anna, Favier Adrien, Mccoy, Laura E   +128 more
core   +2 more sources

Induction of HIV neutralizing antibodies against the MPER of the HIV envelope protein by HA/gp41 chimeric protein-based DNA and VLP vaccines. [PDF]

PLoS ONE, 2011
Several conserved neutralizing epitopes have been identified in the HIV Env protein and among these, the MPER of gp41 has received great attention and is widely recognized as a promising target. However, little success has been achieved in eliciting MPER-
Ling Ye, Zhiyuan Wen, Ke Dong, Xi Wang, Zhigao Bu, Huizhong Zhang, Richard W Compans, Chinglai Yang   +7 more
doaj   +1 more source

Characterization of HIV-1 envelope gp41 genetic diversity and functional domains following perinatal transmission

Retrovirology, 2006
Background HIV-1 envelope gp41 is a transmembrane protein that promotes fusion of the virus with the plasma membrane of the host cells required for virus entry. In addition, gp41 is an important target for the immune response and development of antiviral
Davis Tiffany, Sundaravaradan Vasudha, Mehta Roshni, Ramakrishnan Rajesh, Ahmad Nafees   +4 more
doaj   +1 more source

Oligomerization of the hydrophobic heptad repeat of gp41 [PDF]

Journal of Virology, 1995
The transmembrane protein of human immunodeficiency virus type 1 (HIV-1) contains a leucine zipper-like (hydrophobic heptad) repeat which has been predicted to form an amphipathic alpha helix. To evaluate the potential of the hydrophobic heptad repeat to induce protein oligomerization, this region of gp41 has been cloned into the bacterial expression ...
H B, Bernstein, S P, Tucker, S R, Kar, S A, McPherson, D T, McPherson, J W, Dubay, J, Lebowitz, R W, Compans, E, Hunter   +8 more
openaire   +2 more sources

DNA unwinding by ring-shaped T4 helicase gp41 is hindered by tension on the occluded strand. [PDF]

PLoS ONE, 2013
The replicative helicase for bacteriophage T4 is gp41, which is a ring-shaped hexameric motor protein that achieves unwinding of dsDNA by translocating along one strand of ssDNA while forcing the opposite strand to the outside of the ring.
Noah Ribeck, Omar A Saleh
doaj   +1 more source

Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions.

PLoS Pathogens, 2010
The HIV-1 envelope glycoprotein (Env) composed of the receptor binding domain gp120 and the fusion protein subunit gp41 catalyzes virus entry and is a major target for therapeutic intervention and for neutralizing antibodies.
Victor Buzon, Ganesh Natrajan, David Schibli, Felix Campelo, Michael M Kozlov, Winfried Weissenhorn   +5 more
doaj   +1 more source

A Protein Editing Method to Modify Proteins in Live Mammalian Cells. [PDF]

Curr Protoc
Abstract Protein editing, as mediated by protein trans‐splicing, offers the ability to manipulate, label, and modify proteins in vitro and in live mammalian cells. This ability to observe and control proteins with this high resolution is a burgeoning area of interest within the chemical biology field.
Beyer JN, Toy K, Burslem GM.
europepmc   +2 more sources