Prodynorphin processing by proprotein convertase 2. Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity (Q34451599)

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English	Prodynorphin processing by proprotein convertase 2. Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 August 2017

Prodynorphin processing by proprotein convertase 2. Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity (English)

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Europe PubMed Central

PubMed publication ID

2 August 2017

author name string

R Day

1

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Europe PubMed Central

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2 August 2017

C Lazure

2

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Europe PubMed Central

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2 August 2017

A Basak

3

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Europe PubMed Central

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2 August 2017

A Boudreault

4

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Europe PubMed Central

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2 August 2017

P Limperis

5

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Europe PubMed Central

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2 August 2017

W Dong

6

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Europe PubMed Central

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2 August 2017

I Lindberg

7

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Europe PubMed Central

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2 August 2017

language of work or name

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publication date

1 January 1998

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Europe PubMed Central

PubMed publication ID

2 August 2017

number of pages

8

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Journal of Biological Chemistry

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2 August 2017

273

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2 August 2017

2

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2 August 2017

829-836

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Europe PubMed Central

PubMed publication ID

2 August 2017

Sequence and expression of the rat prodynorphin gene

1 reference

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21 January 2018

The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions

1 reference

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21 January 2018

cDNA and Gene Structure for a Human Subtilisin-Like Protease with Cleavage Specificity for Paired Basic Amino Acid Residues

1 reference

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21 January 2018

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

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21 January 2018

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.

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Identification of a Second Human Subtilisin-Like Protease Gene in thefes/fpsRegion of Chromosome 15

1 reference

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21 January 2018

cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells.

1 reference

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21 January 2018

Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: its striking structural similarity to PACE4

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Bacteriophage lambda N protein alone can induce transcription antitermination in vitro

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PC8 [corrected], a new member of the convertase family

1 reference

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21 January 2018

Region specific expression of furin mRNA in the rat brain

1 reference

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21 January 2018

Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms. Cleavage at a single arginine residue

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Proinsulin processing by the subtilisin-related proprotein convertases furin, PC2, and PC3

1 reference

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Carboxypeptidase E

1 reference

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21 January 2018

Cloning and Sequence Analysis of cDNA Encoding Rat Carboxypeptidase D

1 reference

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21 January 2018

The posttranslational processing of prodynorphin in the rat anterior pituitary.

1 reference

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21 January 2018

Sertoli cells are the primary site of prodynorphin gene expression in rat testis: regulation of mRNA and secreted peptide levels by cyclic adenosine 3' ,5'-monophosphate analogs in cultured cells

1 reference

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21 January 2018

Atypical prodynorphin gene expression in corticosteroid-producing cells of the rat adrenal gland

1 reference

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21 January 2018

Pro-dynorphin is endogenous to the anterior pituitary and is co-localized with LH and FSH in the gonadotrophs

1 reference

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21 January 2018

7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity

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21 January 2018

Enzymatic characterization of immunopurified prohormone convertase 2: potent inhibition by a 7B2 peptide fragment

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21 January 2018

Consensus sequence for processing of peptide precursors at monobasic sites

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Characterization of a metalloprotease from ovine chromaffin granules which cleaves a proenkephalin fragment (BAM12P) at a single arginine residue

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Subcellular Localization, Partial Purification, and Characterization of a Dynorphin Processing Endopeptidase from Bovine Pituitary

1 reference

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21 January 2018

Regulation of striatonigral prodynorphin peptides by dopaminergic agents

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Prohormone-converting enzymes: regulation and evaluation of function using antisense RNA.

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21 January 2018

Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2.

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Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity

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21 January 2018

Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases.

1 reference

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Carboxypeptidase E activity is deficient in mice with the fat mutation. Effect on peptide processing

1 reference

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Testicular expression of PC4 in the rat: molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase

1 reference

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Distribution and regulation of the prohormone convertases PC1 and PC2 in the rat pituitary

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21 January 2018

Approaches in the study of the posttranslational processing of opioid peptide peptide precursors: Focus on prodynorphin

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Mouse insulinoma beta TC3 cells express prodynorphin messenger ribonucleic acid and derived peptides: a unique cellular model for the study of prodynorphin biosynthesis and processing

1 reference

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Purification and enzymatic characterization of recombinant prohormone convertase 2: stabilization of activity by 21 kDa 7B2

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Peptidyl substrates containing unnatural amino acid at the P'1 position are potent inhibitors of prohormone convertases

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21 January 2018

Identifiers

10.1074/JBC.273.2.829

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

ResearchGate publication ID

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