about
Transcellular neuroligin-2 interactions enhance insulin secretion and are integral to pancreatic β cell functionGene expression profiling of a mouse model of pancreatic islet dysmorphogenesisThe PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreasExpression of neurexin, neuroligin, and their cytoplasmic binding partners in the pancreatic beta-cells and the involvement of neuroligin in insulin secretionPancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and controls exocytosis.Targeted inactivation of kinesin-1 in pancreatic β-cells in vivo leads to insulin secretory deficiency.ICER induced by hyperglycemia represses the expression of genes essential for insulin exocytosis.Phosphatidylinositol 4-kinase serves as a metabolic sensor and regulates priming of secretory granules in pancreatic beta cells.Specific glucose-induced control of insulin receptor substrate-2 expression is mediated via Ca2+-dependent calcineurin/NFAT signaling in primary pancreatic islet β-cells.Pancreatic islet cell therapy for type I diabetes: understanding the effects of glucose stimulation on islets in order to produce better islets for transplantation.Differentiation of human labia minora dermis-derived fibroblasts into insulin-producing cellsInvolvement of the Rab27 binding protein Slac2c/MyRIP in insulin exocytosis.Host cell signaling and Trypanosoma cruzi invasion: do all roads lead to lysosomes?A Small Molecule Swertisin from Enicostemma littorale Differentiates NIH3T3 Cells into Islet-Like Clusters and Restores Normoglycemia upon Transplantation in Diabetic Balb/c MiceTwo-way traffic on the road to plasma membrane repairProteomics analysis of insulin secretory granules.Novel regulation by Rac1 of glucose- and forskolin-induced insulin secretion in INS-1 beta-cells.The identification of potential factors associated with the development of type 2 diabetes: a quantitative proteomics approachTime-dependent mechanisms in beta-cell glucose sensing.Gpr40 is expressed in enteroendocrine cells and mediates free fatty acid stimulation of incretin secretion.A redistribution of actin and myosin IIA accompanies Ca(2+)-dependent insulin secretion.Cyclin-dependent kinase 5 promotes insulin exocytosis.Imaging secretory vesicles by fluorescent protein insertion in propeptide rather than mature secreted peptide.Insulin secretory deficiency and glucose intolerance in Rab3A null mice.A 4D view on insulin secretory granule turnover in the β-cell.Mimicking Neuroligin-2 Functions in β-Cells by Functionalized Nanoparticles as a Novel Approach for Antidiabetic Therapy.Involvement of actin filament in the generation of Ca2+ mobilizing messengers in glucose-induced Ca2+ signaling in pancreatic β-cells.Islet heparan sulfate but not heparan sulfate proteoglycan core protein is lost during islet isolation and undergoes recovery post-islet transplantation.PI4KIIα regulates insulin secretion and glucose homeostasis via a PKD-dependent pathway.Cell-sized lipid vesicles for cell-cell synaptic therapies.Annexin I stimulates insulin secretion through regulation of cytoskeleton and PKC activity
P2860
Q24316925-C8D0CDEF-A073-4F36-96E1-9EC4C8638CADQ27301944-2E87ED3B-9C58-4472-869A-9B64CC669C17Q28505821-59FD4153-740E-4FE3-9FAB-4281AC30533EQ28572953-CC0ACFB2-FA6E-4205-93AB-1798E6C255AFQ33898882-DF708D13-D66D-4C9B-BDBD-847C15632FEBQ34448753-AA1D7B14-DFD0-43DF-A5AD-A3E4836B99F0Q34468268-7DD19C0F-20FD-4254-921A-8DF064EED275Q34982315-24F4E7D9-79FF-428D-A14B-B83ED75FAE03Q35405586-A8AAA687-210D-42FC-982F-607A76DBB4CCQ35585661-8EA9EEA0-0431-4C9C-9CDC-74E6DD00483FQ35752093-40EC2495-68A8-4954-B845-446715273F80Q36125027-609F7124-C348-48A9-8617-415DF7937FC7Q36200725-5D5A8268-DAC7-43B1-BAB5-ED3FCC78DF5EQ36804816-680248F1-684E-4CDB-86FF-AC6C7B93AB1EQ36995027-A48FD7CB-169C-48A9-8B11-B17AB0FBD132Q40167745-1CBD03D5-173A-404C-BBBE-F9A04B0A9D86Q40596974-E6FC2F6E-2B69-4D40-8FD6-7FC848C48F6DQ41356232-491FFAE2-D9ED-4EB9-8351-B3E9B23F2516Q41850024-C6D6AD28-987E-494C-A97F-EE4938FF1E9EQ41918359-0AB5F07D-C2AF-43C6-8688-69321C218877Q42501115-95A6E0E6-5CD1-4F21-AA5D-7CAD3F1423F5Q43666421-D7033834-035D-40A6-9D30-949B7208DDD3Q44016473-64477D36-51FF-4493-A0D0-117756119876Q44268165-41F76614-06EF-4561-8025-98D8F8AFA315Q47843038-FC03EE05-9227-4321-AF69-44C14EB0BEFAQ48101015-DD95CC5B-B6F8-46E2-8F32-85A39E2520DFQ52738081-3585D7BC-AEA4-44CE-A99B-46FF45C312CEQ53457111-FBD6B0A0-951B-41BE-B75F-038C6DA26EF6Q53954047-375BA0A8-589E-4301-8882-0F00846988E4Q55017639-B39184C5-2E1C-43BF-9D07-00A5A6E61ECBQ58282677-8AABD3F8-4974-4CB9-A71F-C4DA692407F4
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Beta-granule transport and exocytosis.
@ast
Beta-granule transport and exocytosis.
@en
Beta-granule transport and exocytosis.
@nl
type
label
Beta-granule transport and exocytosis.
@ast
Beta-granule transport and exocytosis.
@en
Beta-granule transport and exocytosis.
@nl
prefLabel
Beta-granule transport and exocytosis.
@ast
Beta-granule transport and exocytosis.
@en
Beta-granule transport and exocytosis.
@nl
P356
P1476
Beta-granule transport and exocytosis.
@en
P2093
P304
P356
10.1006/SCDB.2000.0174
P577
2000-08-01T00:00:00Z