The selective recruitment of mRNA to the ER and an increase in initiation are important for glucose-stimulated proinsulin synthesis in pancreatic beta-cells. (Q39498096)

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English	The selective recruitment of mRNA to the ER and an increase in initiation are important for glucose-stimulated proinsulin synthesis in pancreatic beta-cells.	scientific article

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13 January 2020

The selective recruitment of mRNA to the ER and an increase in initiation are important for glucose-stimulated proinsulin synthesis in pancreatic beta-cells (English)

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13 January 2020

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Terence P. Herbert

4

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13 January 2020

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Isabel C Greenman

1

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13 January 2020

Edith Gomez

2

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13 January 2020

Claire E J Moore

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13 January 2020

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1 October 2005

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13 January 2020

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10

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Biochemical Journal

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13 January 2020

391

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13 January 2020

Pt 2

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13 January 2020

291-300

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13 January 2020

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11 June 2022

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Polypyrimidine tract-binding protein promotes insulin secretory granule biogenesis

1 reference

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Control of insulin mRNA stability in rat pancreatic islets. Regulatory role of a 3'-untranslated region pyrimidine-rich sequence

1 reference

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The signal recognition particle

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Inhibition of protein synthesis sequentially impairs distinct steps of stimulus-secretion coupling in pancreatic beta cells

1 reference

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The fate of membrane-bound ribosomes following the termination of protein synthesis

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Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes

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Glucose-stimulated protein synthesis in pancreatic beta-cells parallels an increase in the availability of the translational ternary complex (eIF2-GTP.Met-tRNAi) and the dephosphorylation of eIF2 alpha.

1 reference

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Insulin biosynthesis and its regulation

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Insulin mediates glucose-stimulated phosphorylation of PHAS-I by pancreatic beta cells. An insulin-receptor mechanism for autoregulation of protein synthesis by translation

1 reference

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25 September 2017

Glucose stimulation of the proinsulin synthesis in isolated pancreatic islets without increasing amount of proinsulin mRNA

1 reference

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25 September 2017

Glucose-regulated translational control of proinsulin biosynthesis with that of the proinsulin endopeptidases PC2 and PC3 in the insulin-producing MIN6 cell line

1 reference

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25 September 2017

Pancreatic beta cell line MIN6 exhibits characteristics of glucose metabolism and glucose-stimulated insulin secretion similar to those of normal islets

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Insulin biosynthesis. I. On the mechanism of glucose stimulation.

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Mechanisms of leucine- and theophylline-stimulated insulin biosynthesis in isolated rat pancreatic islets

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Translational control of insulin biosynthesis. Evidence for regulation of elongation, initiation and signal-recognition-particle-mediated translational arrest by glucose.

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Regulation of the biosynthesis of insulin-secretory-granule proteins. Co-ordinate translational control is exerted on some, but not all, granule matrix constituents

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GTP-binding proteins may stimulate insulin biosynthesis in rat pancreatic islets by enhancing the signal-recognition-particle-dependent translocation of the insulin mRNA poly-/mono-some complex to the endoplasmic reticulum

1 reference

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RNA—protein interactions in the 5′ untranslated region of preproinsulin mRNA

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Analysis of the two steps in polypeptide chain initiation inhibited by pactamycin

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Cooperativity between the preproinsulin mRNA untranslated regions is necessary for glucose-stimulated translation

1 reference

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The biosynthesis of the subtilisin-related proprotein convertase PC3, but no that of the PC2 convertase, is regulated by glucose in parallel to proinsulin biosynthesis in rat pancreatic islets

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transcriptional and Translational Control of Glucose-Stimulated (Pro)insulin Biosynthesis

1 reference

https://pubmed.ncbi.nlm.nih.gov/15972000

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Translational control of proinsulin synthesis by glucose

1 reference

https://pubmed.ncbi.nlm.nih.gov/15972000

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/BJ20050468

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15972000%20AND%20SRC:MED&resulttype=core&format=json

13 January 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15972000%20AND%20SRC:MED&resulttype=core&format=json

13 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15972000%20AND%20SRC:MED&resulttype=core&format=json

13 January 2020

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