(Q48492994)

English

Processing of adrenocorticotropin by two proteases in bovine intermediate lobe secretory vesicle membranes. A distinct acidic, tetrabasic residue-specific calcium-activated serine protease and a PC2-like enzyme

scientific article published on April 15, 1992

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Europe PubMed Central

PubMed publication ID

12 February 2018

http://europepmc.org/abstract/MED/1313803

Processing of adrenocorticotropin by two proteases in bovine intermediate lobe secretory vesicle membranes. A distinct acidic, tetrabasic residue-specific calcium-activated serine protease and a PC2-like enzyme (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:1313803

12 September 2022

post-translational protein modification

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12 September 2022

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10.1016/S0021-9258(18)42539-2

https://api.crossref.org/works/10.1016/S0021-9258(18)42539-2

3 December 2023

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10.1016/S0021-9258(18)42539-2

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3 December 2023

Fernando E. Estivariz

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Estivariz FE

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12 February 2018

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T. C. Friedman

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:1313803

12 September 2022

T. Chikuma

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:1313803

12 September 2022

Y. P. Loh

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12 September 2022

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1 April 1992

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12 February 2018

http://europepmc.org/abstract/MED/1313803

15 April 1992

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1313803

12 September 2022

full work available at URL

http://intl.jbc.org/cgi/content/abstract/267/11/7456

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:1313803

12 September 2022

https://doi.org/10.1016/s0021-9258(18)42539-2

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:1313803

3 December 2023

https://api.elsevier.com/content/article/PII:S0021925818425392?httpAccept=text/xml

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10.1016/S0021-9258(18)42539-2

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3 December 2023

https://api.elsevier.com/content/article/PII:S0021925818425392?httpAccept=text/plain

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3 December 2023

Journal of Biological Chemistry

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Europe PubMed Central

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12 February 2018

http://europepmc.org/abstract/MED/1313803

267

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Europe PubMed Central

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12 February 2018

http://europepmc.org/abstract/MED/1313803

11

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Europe PubMed Central

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12 February 2018

http://europepmc.org/abstract/MED/1313803

7456-7463

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Europe PubMed Central

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12 February 2018

http://europepmc.org/abstract/MED/1313803

Post-translational proteolysis in polypeptide hormone biosynthesis

1

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Proteolytic events in the post-translational processing of polypeptide hormone precursors

2

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Proteolysis in Neuropeptide Processing and Other Neural Functions

3

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Endopeptidases and prohormone processing

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Nucleotide sequence of the human parathyroid hormone gene

7

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Structure and Biosynthesis of Pro-Adrenocorticotropin/Endorphin and Related Peptides*

8

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Structure and bioactivity of the amino-terminal fragment of pro-opiomelanocortin

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Influence of ascorbic acid on in vivo amidation of alpha-melanocyte stimulating hormone in guinea pig pituitary

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Preparation of Iodine-131 Labelled Human Growth Hormone of High Specific Activity

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Adrenal regeneration in the rat is mediated by mitogenic N-terminal pro-opiomelanocortin peptides generated by changes in precursor processing in the anterior pituitary

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Isolation of ACTH1-39,ACTH1-38 and CLIP from the calf anterior pituitary

19

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cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases

22

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Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans

23

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Isolation of two complementary deoxyribonucleic acid clones from a rat insulinoma cell line based on similarities to Kex2 and furin sequences and the specific localization of each transcript to endocrine and neuroendocrine tissues in rats

24

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Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, Furin, and Kex2: distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2.

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Prenatal processing of pro-opiomelanocortin in the brain and pituitary of mouse embryos

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Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary

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The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing

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Effect of calcium ions on the processing of pro-opiomelanocortin by bovine intermediate lobe pro-opiomelanocortin-converting enzyme

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Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2 -dependent serine protease

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Enzymes required for yeast prohormone processing

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Kex2-like endoproteases PC2 and PC3 accurately cleave a model prohormone in mammalian cells: evidence for a common core of neuroendocrine processing enzymes

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Structural homology between the human fur gene product and the subtilisin-like protease encoded by yeast KEX2

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Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein

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Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo

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Coordinate regulation of mRNA levels of pro-opiomelanocortin and the candidate processing enzymes PC2 and PC3, but not furin, in rat pituitary intermediate lobe

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PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues

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Characterization of PC2, a mammalian Kex2 homologue, following expression of the cDNA in microinjected Xenopus oocytes

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Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor

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Immunocytochemical evidence for intragranular processing of pro-opiomelanocortin in the melanotropic cells of the rabbit

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Variants of alpha-melanocyte stimulating hormone in rat brain and pituitary evidence that acetylated alpha-MSH exists only in the intermediate lobe of pituitary.

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Europe PubMed Central

PubMed publication ID

12 February 2018

http://europepmc.org/abstract/MED/1313803

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