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1 of maturation into phagolysosomes, acquired cellubrevin.
2 y of the syb mutations, as can rat VAMP2 and cellubrevin.
3 endosomes, BAP31 did not cofractionate with cellubrevin.
5 of the cytoplasmic domains of VAMP2 or VAMP3/cellubrevin also resulted in an inhibition of insulin-st
8 y colocalized with transferrin receptors and cellubrevin and morphologically resembled the recycling
10 -deficient neurons but that deletion of both cellubrevin and synaptobrevin does not cause a more seve
11 eimide attachment protein receptors (SNAREs) cellubrevin and vesicle-associated membrane protein-2 (V
12 ed with recycling endosomes, such as rab 11, cellubrevin, and endobrevin, but relatively poor in earl
14 ment (ERC), which is marked by Rab11a, VAMP3/cellubrevin, and VAMP8/endobrevin and holds large reserv
15 lysin O-permeabilized platelets to antihuman cellubrevin antibody inhibited Ca(++)-induced alpha-gran
17 e to the wild-type TR, and sphingomyelin and cellubrevin, both of which label all compartments of the
18 ytoplasmic tail of BAP31 prevented export of cellubrevin, but not of the transferrin receptor from th
19 unocytochemistry, BAP31 did not overlap with cellubrevin, but rather colocalized with resident protei
20 nstrate that syntaxin 4, VAMP2, and/or VAMP3/cellubrevin can function as target membrane and vesicle
21 onally involved in receptor recycling [Rab4, cellubrevin (Cbvn)] relative to the distribution of a re
24 rified with BAP31 on immobilized recombinant cellubrevin, demonstrating that the interaction is speci
26 internalized FITC-F(ab) to measure the pH of cellubrevin-enriched recycling endosomes (pHCb) and FITC
27 ociated membrane protein (VAMP) 1, 2, or rat cellubrevin failed to detect these v-SNAREs in human pla
29 y internalized by COS cells transfected with cellubrevin-Ig, which at steady state accumulated in a p
30 demonstrated that approximately 80% of human cellubrevin in resting platelets was localized to platel
31 oxin D, which selectively cleaves VAMP-2 and cellubrevin, inhibited the ability of insulin to stimula
34 rescent protein, that CFTR affects the pH of cellubrevin-labeled endosomal organelles resulting in hy
35 show that the ubiquitously expressed v-SNARE cellubrevin localizes to the basolateral membrane and to
36 n 93% identity with human VAMP 1, 2, and rat cellubrevin over the conserved core region, but has a un
37 hree mammalian isoforms, VAMP-1, VAMP-2, and cellubrevin, play a role in protein transport to the pla
39 how that the closely related R-SNARE protein cellubrevin rescues synaptic transmission in synaptobrev
43 th rosiglitazone (30 micromol/kg) normalized cellubrevin, VAMP-2, and syntaxin 4 protein to levels ap
45 us, and null platelets confirmed the lack of cellubrevin/VAMP-3 in nulls and showed that most element
48 mbrane Protein (VAMPs: synaptobrevin/VAMP-2, cellubrevin/VAMP-3, TI-VAMP/VAMP-7, and endobrevin/VAMP-
49 Although several SNAREs, including VAMP3/cellubrevin, VAMP8/endobrevin, syntaxin 13, and syntaxin
50 attachment protein receptor (v-SNARE) called cellubrevin/vesicle-associated membrane protein-3 (VAMP-
51 , one in which the vesicle transport protein cellubrevin was appended with a luminal IgG epitope to a
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