J
James C. Morrell
Researcher at Johns Hopkins University
Publications - 32
Citations - 3326
James C. Morrell is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Peroxisome & Peroxisomal targeting signal. The author has an hindex of 22, co-authored 32 publications receiving 3142 citations. Previous affiliations of James C. Morrell include Johns Hopkins University School of Medicine.
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Journal ArticleDOI
Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes.
TL;DR: The hypothesis that HIV and other retroviruses are generated by a normal, nonviral pathway of exosome biogenesis is supported.
Journal ArticleDOI
Expression of PEX11β Mediates Peroxisome Proliferation in the Absence of Extracellular Stimuli
Michael Schrader,Bernadette E. Reuber,James C. Morrell,Gerardo Jimenez-Sanchez,Cassandra Obie,Tina A. Stroh,David Valle,Trina A. Schroer,Stephen Jay Gould +8 more
TL;DR: Overexpression of the human PEX11β gene alone was sufficient to induce peroxisome proliferation, demonstrating that proliferation can occur in the absence of extracellular stimuli and may be mediated by a single gene.
Journal ArticleDOI
Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor.
Stephen Jay Gould,Jennifer E. Kalish,James C. Morrell,Jonas Carl-Otto Bjorkman,Aaron J. Urquhart,Denis I. Crane +5 more
TL;DR: It is concluded that Pex13p functions as a docking factor for the predominantly cytoplasmic PTS1 receptor and eliminates import of peroxisomal matrix proteins that contain either the type-1 or type-2 peroxISomal targeting signal but does not affect targeting and insertion of integral perox isomal membrane proteins.
Journal ArticleDOI
PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
TL;DR: These results show that PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs, and the existence of two PMP import mechanisms and two classes of mPTSs.
Journal ArticleDOI
PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins
TL;DR: It is shown that PEX3 is required for P EX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is necessary for recruitment of the PEX21 docking domain to peroxIsomes, and transient inhibition of P EX3 abrogates class I PMP import but has no effect on class II PMP Import or peroxISomal matrix protein import.