Results 1 to 10 of about 14,104 (164)

A novel RAB5 binding site in human VPS34-CII that is likely the primordial site in eukaryotic evolution [PDF]

open access: yeseLife
RAB5-GTP activation of the multiprotein VPS34 complex II (VPS34-CII) is critical for endosomal sorting and maturation, phagocytosis, and receptor downregulation.
Saule Spokaite   +4 more
doaj   +2 more sources

Structure-based discovery of neoandrographolide as a novel inhibitor of Rab5 to suppress cancer growth

open access: yesComputational and Structural Biotechnology Journal, 2020
Rab5 is a small GTPase that plays a crucial role in oncogenic signal transduction, which was considered as an attractive target for cancer therapy. Rapid GDP/GTP exchange in the packet of Rab5 sustains its high activity for promoting cancer progression ...
Yang Wang, Qing-Yu He
exaly   +3 more sources

Subcellular localization of SUN2 is regulated by lamin A and Rab5. [PDF]

open access: yesPLoS ONE, 2011
SUN2 is an inner nuclear membrane protein with a conserved Sad1/UNC-84 homology SUN-domain at the C-terminus. Intriguingly, SUN2 has also been reported to interact with Rab5, which localizes in early endosomes.
Ying Liang   +3 more
doaj   +6 more sources

Development of mRNA–lipid nanoparticle intrabodies against rickettsial infection [PDF]

open access: yesJournal of Biomedical Science
Background Rickettsiosis is among the deadliest vector-borne infectious diseases worldwide, in part because rickettsiae replicate within human cells, where antibodies and most drugs cannot effectively reach this obligatory intracellular pathogen ...
Qi Yan   +7 more
doaj   +2 more sources

Interactions of rab5 with cytosolic proteins. [PDF]

open access: yesJournal of Biological Chemistry, 1992
Rab proteins, one of the subfamilies of ras-like small GTP-binding proteins, are attached to cellular compartments or transport vesicles and may determine the specificity of fusion between these compartments and vesicles. It has been proposed that they alternate between a membrane-bound and a cytosolic state during their functional cycle.
Kurzchalia, Teymuras V.   +7 more
openaire   +3 more sources

Delayed onset of positive feedback activation of Rab5 by Rabex-5 and Rabaptin-5 in endocytosis. [PDF]

open access: yesPLoS ONE, 2010
Rabex-5 is a guanine nucleotide exchange factor (GEF) that specifically activates Rab5, i.e., converting Rab5-GDP to Rab5-GTP, through two distinct pathways to promote endosome fusion and endocytosis.
Huaiping Zhu, Hong Qian, Guangpu Li
doaj   +1 more source

Coordination of the Rab5 Cycle on Macropinosomes [PDF]

open access: yesTraffic, 2011
The GTPase Rab5a regulates the homotypic and heterotypic fusion of membranous organelles during the early stages of endocytosis. Many of the molecules which regulate the Rab5a cycle of association with membranes, activation, deactivation and dissociation are known.
Feliciano, William David   +3 more
openaire   +3 more sources

Assessing Rab5 Activation in Health and Disease [PDF]

open access: yes, 2021
The endocytic pathway is a system of dynamically communicating vesicles, known as early endosomes, that internalize, sort, and traffic nutrients, trophic factors, and signaling molecules to sites throughout the cell. In all eukaryotic cells, early endosome functions are regulated by Rab5 activity, dependent upon its binding to GTP, whereas Rab5 bound ...
Anna, Pensalfini   +3 more
openaire   +2 more sources

Identification of the Rab5 Binding Site in p110β: Assays for PI3Kβ Binding to Rab5 [PDF]

open access: yes, 2015
Isoform-specific signaling by Class IA PI 3-kinases depends in part on the interactions between distinct catalytic subunits and upstream regulatory proteins. From among the class IA catalytic subunits (p110α, p110β, and p110δ), p110β has unique properties.
Rachel S, Salamon   +5 more
openaire   +2 more sources

rab5 GTPase Regulates Adenovirus Endocytosis [PDF]

open access: yesJournal of Virology, 1999
ABSTRACT Adenovirus interaction with αv integrins is important for virus entry. We have examined the effects of adenovirus attachment on intracellular signaling in HeLa cells, with an emphasis on pathways known to be activated following integrin interaction with other ligands. We found no evidence for [Ca 2+
T, Rauma   +4 more
openaire   +2 more sources

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