PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24705014-7	2014	Microtubule disruption with nocodazole prevented pre-internalized GLUT4myc from reaching the Stx6-positive perinuclear sub-compartment and from undergoing insulin-responsive exocytosis.	Nocodazole	28-38	solute carrier family 2 member 4	Homo sapiens	66-71	
12959978-6	2003	Using methods that measure insulin-dependent GLUT4 translocation in populations of adipocytes as opposed to individual cells, we show a statistically significant reduction in translocation (30% inhibition) in the presence of low concentrations of nocodazole (2 mum).	Nocodazole	247-257	solute carrier family 2 member 4	Homo sapiens	45-50	
16239226-2	2005	Here, we investigated the effects of microtubule-depolymerizing reagent, nocodazole and colchicine, on GLUT4 translocation in 3T3-L1 adipocytes.	Nocodazole	73-83	solute carrier family 2 member 4	Homo sapiens	103-108	
16239226-3	2005	After nocodazole treatment to disrupt microtubules, GLUT4 vesicles were dispersed from the perinuclear region in the basal state, and insulin-induced GLUT4 translocation was partially inhibited by 20-30%, consistent with other reports.	Nocodazole	6-16	solute carrier family 2 member 4	Homo sapiens	52-57	
16239226-4	2005	We found that platelet-derived growth factor (PDGF), which did not stimulate GLUT4 translocation in intact cells, was surprisingly able to enhance GLUT4 translocation to approximately 50% of the maximal insulin response, in nocodazole-treated cells with disrupted microtubules.	Nocodazole	224-234	solute carrier family 2 member 4	Homo sapiens	147-152	
16239226-5	2005	This effect of PDGF was blocked by pretreatment with wortmannin and attenuated in cells pretreated with cytochalasin D. Using confocal microscopy, we found an increased co-localization of GLUT4 and F-actin in nocodazole-treated cells upon PDGF stimulation compared with control cells.	Nocodazole	209-219	solute carrier family 2 member 4	Homo sapiens	188-193	
16239226-7	2005	In summary, our data suggest that 1) proper perinuclear localization of GLUT4 vesicles is a requirement for insulin-specific stimulation of GLUT4 translocation, and 2) nocodazole treatment disperses GLUT4 vesicles from the perinuclear region allowing them to engage insulin and PDGF-sensitive actin filaments, which can participate in GLUT4 translocation in a phosphatidylinositol 3-kinase-dependent manner.	Nocodazole	168-178	solute carrier family 2 member 4	Homo sapiens	72-77	
16239226-7	2005	In summary, our data suggest that 1) proper perinuclear localization of GLUT4 vesicles is a requirement for insulin-specific stimulation of GLUT4 translocation, and 2) nocodazole treatment disperses GLUT4 vesicles from the perinuclear region allowing them to engage insulin and PDGF-sensitive actin filaments, which can participate in GLUT4 translocation in a phosphatidylinositol 3-kinase-dependent manner.	Nocodazole	168-178	solute carrier family 2 member 4	Homo sapiens	140-145	
16239226-7	2005	In summary, our data suggest that 1) proper perinuclear localization of GLUT4 vesicles is a requirement for insulin-specific stimulation of GLUT4 translocation, and 2) nocodazole treatment disperses GLUT4 vesicles from the perinuclear region allowing them to engage insulin and PDGF-sensitive actin filaments, which can participate in GLUT4 translocation in a phosphatidylinositol 3-kinase-dependent manner.	Nocodazole	168-178	solute carrier family 2 member 4	Homo sapiens	140-145	
16239226-7	2005	In summary, our data suggest that 1) proper perinuclear localization of GLUT4 vesicles is a requirement for insulin-specific stimulation of GLUT4 translocation, and 2) nocodazole treatment disperses GLUT4 vesicles from the perinuclear region allowing them to engage insulin and PDGF-sensitive actin filaments, which can participate in GLUT4 translocation in a phosphatidylinositol 3-kinase-dependent manner.	Nocodazole	168-178	solute carrier family 2 member 4	Homo sapiens	140-145	
14595108-8	2004	Nocodazole disruption of the microtubule cytoskeleton reduces the insulin-stimulated exocytosis of GLUT4, accounting for the reduced insulin-stimulated translocation of GLUT4 to the cell surface.	Nocodazole	0-10	solute carrier family 2 member 4	Homo sapiens	99-104	
14595108-8	2004	Nocodazole disruption of the microtubule cytoskeleton reduces the insulin-stimulated exocytosis of GLUT4, accounting for the reduced insulin-stimulated translocation of GLUT4 to the cell surface.	Nocodazole	0-10	solute carrier family 2 member 4	Homo sapiens	169-174	
11278355-5	2001	Insulin-mediated GLUT4 translocation was inhibited by more than 80% in nocodazole-treated cells.	Nocodazole	71-81	solute carrier family 2 member 4	Homo sapiens	17-22	
11571289-3	2001	In the present study we show that 2 microm nocodazole completely depolymerized microtubules in 3T3-L1 adipocytes, as determined morphologically and biochemically, resulting in dispersal of the perinuclear GLUT4 compartment and the Golgi apparatus.	Nocodazole	43-53	solute carrier family 2 member 4	Homo sapiens	205-210	
11571289-6	2001	This effect was not likely the result of microtubule depolymerization because in the presence of taxol, which blocked nocodazole-induced depolymerization of microtubules as well as the dispersal of the perinuclear GLUT4 compartment, the inhibitory effect of 10-33 microm nocodazole on insulin-stimulated glucose uptake prevailed.	Nocodazole	271-281	solute carrier family 2 member 4	Homo sapiens	214-219	
11278355-7	2001	An intact microtubule network is specifically required for insulin-mediated GLUT4 translocation since nocodazole treatment did not affect insulin-mediated GLUT1 translocation or adipsin secretion.	Nocodazole	102-112	solute carrier family 2 member 4	Homo sapiens	76-81