ArticleMolecular biology of the cell1999
The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- Characterizing the Murine Leukemia Virus Envelope Glycoprotein Membrane-Spanning Domain for Its Roles in Interface Alignment and Fusogenicity.Journal of virology · 2015Article
- Trimeric transmembrane domain interactions in paramyxovirus fusion proteins: roles in protein folding, stability, and function.The Journal of biological chemistry · 2013Article
- Analysis of jaagsiekte sheep retrovirus (JSRV) envelope protein domains in transformation.Virus genes · 2012Article
- The paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Journal of virology · 2012Article
- The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Journal of virology · 2011Article
- Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Cell entry of enveloped viruses.Advances in genetics · 2011Review
- The Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: analysis of transmembrane domain length and sequence requirements.Journal of virology · 2009Article
- The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design.Microbiology and molecular biology reviews : MMBR · 2008Review
- Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus.Biophysical journal · 2005Article
- Role of the specific amino acid sequence of the membrane-spanning domain of human immunodeficiency virus type 1 in membrane fusion.Journal of virology · 2005Article
- The many mechanisms of viral membrane fusion proteins.Current topics in microbiology and immunology · 2005Review
- De novo design of conformationally flexible transmembrane peptides driving membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein.Journal of virology · 2004Article
- The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement.The Journal of membrane biology · 2004Review
- Characterization of a cytolytic strain of equine infectious anemia virus.Journal of virology · 2003Article
- Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide.Journal of virology · 2003Article
- The transmembrane domain and cytoplasmic tail of herpes simplex virus type 1 glycoprotein H play a role in membrane fusion.Journal of virology · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The role of glycoprotein membrane-spanning domains in the process of membrane fusion is poorly understood. It has been demonstrated that replacing all or part of the membrane-spanning domain of a viral fusion protein with sequences that encode signals for glycosylphosphatidylinositol linkage attachment abrogates membrane fusion activity. It has been suggested, however, that the actual amino acid sequence of the membrane-spanning domain is not critical for the activity of viral fusion proteins. We have examined the function of Moloney murine leukemia virus envelope proteins with substitutions in the membrane-spanning domain. Envelope proteins bearing substitutions for proline 617 are processed and incorporated into virus particles normally and bind to the viral receptor. However, they possess greatly reduced or undetectable capacities for the promotion of membrane fusion and infectious virus particle formation. Our results imply a direct role for the residues in the membrane-spanning domain of the murine leukemia virus envelope protein in membrane fusion and its regulation. They also support the thesis that membrane-spanning domains possess a sequence-dependent function in other protein-mediated membrane fusion events.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.