Involvement of a polyproline helix-like structure in the interaction of 7B2 with prohormone convertase 2. (Q30176819)

9 June 2017

title

Involvement of a polyproline helix-like structure in the interaction of 7B2 with prohormone convertase 2. (English)

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9 June 2017

X Zhu

1

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9 June 2017

N S Lamango

series ordinal

2

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9 June 2017

I Lindberg

series ordinal

3

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9 June 2017

language of work or name

English

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publication date

1 September 1996

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Journal of Biological Chemistry

9 June 2017

number of pages

6

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based on heuristic

inferred from page(s)

published in

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9 June 2017

volume

271

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9 June 2017

issue

38

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9 June 2017

page(s)

23582-23587

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Left-handed polyproline II helices commonly occur in globular proteins.

9 June 2017

cites work

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SH3 domains direct cellular localization of signaling molecules

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7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway

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Isolation and NH2-terminal sequence of a novel porcine anterior pituitary polypeptide. Homology to proinsulin, secretin and Rous sarcoma virus transforming protein TVFV60.

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SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

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Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition

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Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains

21 January 2018

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

21 January 2018

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The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2

21 January 2018

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Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase

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Role of the cytokines in the neuroendocrine-immune system axis

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Proprotein and prohormone convertases of the subtilisin family Recent developments and future perspectives

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Cloning and Characterization of the Rat Complementary Deoxyribonucleic Acid and Gene Encoding the Neuroendocrine Peptide 7B2*

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

21 January 2018

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Internal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: a potential mechanism for its inactivation

21 January 2018

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The neuroendocrine chaperone 7B2 can enhance in vitro POMC cleavage by prohormone convertase PC2

21 January 2018

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

21 January 2018

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Identification of the region within the neuroendocrine polypeptide 7B2 responsible for the inhibition of prohormone convertase PC2

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.38.23582

1 reference

9 June 2017

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