Search Results - "Hanson, Phyllis I."
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Multivesicular Body Morphogenesis
Published in Annual review of cell and developmental biology (01-01-2012)“…Multivesicular bodies (MVBs) are unique organelles in the endocytic pathway that contain vesicles in their lumen. Sorting and incorporation of material into…”
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Triggered recruitment of ESCRT machinery promotes endolysosomal repair
Published in Science (American Association for the Advancement of Science) (06-04-2018)“…Endolysosomes can be damaged by diverse materials. Terminally damaged compartments are degraded by lysophagy, but pathways that repair salvageable organelles…”
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3
Membrane budding and scission by the ESCRT machinery: it's all in the neck
Published in Nature reviews. Molecular cell biology (01-08-2010)“…Key Points Endosomal sorting complexes required for transport (ESCRTs) are required for the lysosomal degradation of plasma membrane proteins, budding of most…”
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4
A cell-based assay for CD63-containing extracellular vesicles
Published in PloS one (24-07-2019)“…Extracellular vesicles (EVs) are thought to be important in cell-cell communication and have elicited extraordinary interest as potential biomarkers of…”
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5
Effects of Inhibiting VPS4 Support a General Role for ESCRTs in Extracellular Vesicle Biogenesis
Published in Biophysical journal (19-09-2017)“…Extracellular vesicles (EVs) are proposed to play important roles in intercellular communication. Two classes of EVs can be distinguished based on their…”
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6
Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
Published in The Journal of cell biology (28-01-2008)“…Endosomal sorting complex required for transport III (ESCRT-III) proteins function in multivesicular body biogenesis and viral budding. They are recruited from…”
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7
Structure and membrane remodeling activity of ESCRT-III helical polymers
Published in Science (American Association for the Advancement of Science) (18-12-2015)“…The endosomal sorting complexes required for transport (ESCRT) proteins mediate fundamental membrane remodeling events that require stabilizing negative…”
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8
Mycobacterium tuberculosis Type VII Secretion System Effectors Differentially Impact the ESCRT Endomembrane Damage Response
Published in mBio (27-11-2018)“…Intracellular pathogens have varied strategies to breach the endolysosomal barrier so that they can deliver effectors to the host cytosol, access nutrients,…”
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Redefining the Breast Cancer Exosome Proteome by Tandem Mass Tag Quantitative Proteomics and Multivariate Cluster Analysis
Published in Analytical chemistry (Washington) (20-10-2015)“…Exosomes are microvesicles of endocytic origin constitutively released by multiple cell types into the extracellular environment. With evidence that exosomes…”
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Structure/Function Analysis of Four Core ESCRT‐III Proteins Reveals Common Regulatory Role for Extreme C‐Terminal Domain
Published in Traffic (Copenhagen, Denmark) (01-08-2007)“…Endosomal sorting complex required for transport‐III (ESCRT‐III) is a large complex built from related ESCRT‐III proteins involved in multivesicular body…”
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Structure of cellular ESCRT-III spirals and their relationship to HIV budding
Published in eLife (30-05-2014)“…The ESCRT machinery along with the AAA+ ATPase Vps4 drive membrane scission for trafficking into multivesicular bodies in the endocytic pathway and for the…”
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Activation of Human VPS4A by ESCRT-III Proteins Reveals Ability of Substrates to Relieve Enzyme Autoinhibition
Published in The Journal of biological chemistry (12-11-2010)“…VPS4 proteins are AAA+ ATPases required to form multivesicular bodies, release viral particles, and complete cytokinesis. They act by disassembling ESCRT-III…”
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13
Impaired Protein Aggregate Handling and Clearance Underlie the Pathogenesis of p97/VCP-associated Disease
Published in The Journal of biological chemistry (31-10-2008)“…Mutations in p97/VCP cause the multisystem disease inclusion body myopathy, Paget disease of the bone and frontotemporal dementia (IBMPFD). p97/VCP is a member…”
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14
Access of torsinA to the inner nuclear membrane is activity dependent and regulated in the endoplasmic reticulum
Published in Journal of cell science (01-08-2015)“…TorsinA (also known as torsin-1A) is a membrane-embedded AAA+ ATPase that has an important role in the nuclear envelope lumen. However, most torsinA is…”
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Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation
Published in Human molecular genetics (15-01-2006)“…Mutations in the AAA+ protein (ATPase associated with a variety of cellular activities) p97/VCP (valosin-containing protein) cause a dominantly inherited…”
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Ubiquitin Depletion and Dominant-Negative VPS4 Inhibit Rhabdovirus Budding without Affecting Alphavirus Budding
Published in Journal of Virology (01-12-2007)“…Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice
Published in Human molecular genetics (15-04-2007)“…Mutations in p97/VCP cause the autosomal-dominant, inherited syndrome inclusion body myopathy (IBM) associated with Paget's disease of the bone and…”
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Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum
Published in The EMBO journal (17-08-2011)“…TorsinA is a membrane‐associated enzyme in the endoplasmic reticulum (ER) lumen that is mutated in DYT1 dystonia. How it remains in the ER has been unclear. We…”
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TorsinA in the Nuclear Envelope
Published in Proceedings of the National Academy of Sciences - PNAS (18-05-2004)“…Early-onset torsion dystonia, a CNS-based movement disorder, is usually associated with a single amino acid deletion (ΔE302/303) in the protein torsinA…”
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An essential and NSF independent role for α-SNAP in store-operated calcium entry
Published in eLife (16-07-2013)“…Store-operated calcium entry (SOCE) by calcium release activated calcium (CRAC) channels constitutes a primary route of calcium entry in most cells. Orai1…”
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