ArticleOncogene2001
Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein.
Article in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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Who cites it
20 citing papers in PubMed.
- Dimeric Transmembrane Orientations of APP/C99 Regulate γ-Secretase Processing Line Impacting Signaling and Oligomerization.iScience · 2020Article
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Hydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor.Biophysical journal · 2015Article
- Mapping the homodimer interface of an optimized, artificial, transmembrane protein activator of the human erythropoietin receptor.PloS one · 2014Article
- Viral miniproteins.Annual review of microbiology · 2014Review
- The E5 proteins.Virology · 2013Review
- Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Papillomavirus E5: the smallest oncoprotein with many functions.Molecular cancer · 2011Review
- Orientation-specific signalling by thrombopoietin receptor dimers.The EMBO journal · 2011Article
- Structural role of the conserved cysteines in the dimerization of the viral transmembrane oncoprotein E5.Biophysical journal · 2010Article
- Artificial transmembrane oncoproteins smaller than the bovine papillomavirus E5 protein redefine sequence requirements for activation of the platelet-derived growth factor beta receptor.Journal of virology · 2009Article
- The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango.Virology · 2009Review
- In vitro dimerization of the bovine papillomavirus E5 protein transmembrane domain.Biochemistry · 2008Article
- Protein-protein interactions in the membrane: sequence, structural, and biological motifs.Structure (London, England : 1993) · 2008Review
- Packing contacts can mediate highly specific interactions between artificial transmembrane proteins and the PDGFbeta receptor.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Modulation of cell function by small transmembrane proteins modeled on the bovine papillomavirus E5 protein.Oncogene · 2005Review
- PKA/PrKX activity is a modulator of AAV/adenovirus interaction.The EMBO journal · 2003Article
- Functional replacement of the carboxy-terminal two-thirds of the influenza A virus NS1 protein with short heterologous dimerization domains.Journal of virology · 2002Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
We have developed a genetic method to determine the active orientation of dimeric transmembrane protein helices. The bovine papillomavirus E5 protein, a 44-amino acid homodimeric protein that appears to traverse membranes as a left-handed coiled-coil, transforms fibroblasts by binding and activating the platelet-derived growth factor (PDGF) beta receptor. A heterologous dimerization domain was used to force E5 monomers to adopt all seven possible symmetric coiled-coil registries relative to one another within the dimer. Focus formation assays demonstrated that dimerization of the E5 protein is required for transformation and identified a single preferred orientation of the monomers. The essential glutamine residue at position 17 resided in the dimer interface in this active orientation. The active chimera formed complexes with the PDGF beta receptor and induced receptor tyrosine phosphorylation. We also identified E5-like structures that underwent non-productive interactions with the receptor.
Indexed as
Identifiers
11439346What OpenQuestion holds
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.