Membrane topology of the 12- and the 25-kDa subunits of the mammalian signal peptidase complex (Q24311608)

Signal peptidase complex subunit 1 homolog (S. cerevisiae)

GOA release 2020-03-11

1 reference

Journal of Biological Chemistry

GOA release 2020-03-11

author name string

K U Kalies

series ordinal

1

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E Hartmann

series ordinal

2

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language of work or name

English

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publication date

16 February 1996

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published in

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volume

271

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issue

7

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page(s)

3925-9

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cites work

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Purification of microsomal signal peptidase as a complex

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Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex

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Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane

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The signal sequence receptor has a second subunit and is part of a translocation complex in the endoplasmic reticulum as probed by bifunctional reagents

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A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation

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Predicting the orientation of eukaryotic membrane-spanning proteins

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A tetrameric complex of membrane proteins in the endoplasmic reticulum

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Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases

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A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane

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7 January 2021

A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae

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Signal Sequence Processing in Rough Microsomes

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Mammalian Signal Peptidase: Partial Purification and General Characterization of the Signal Peptidase from Microsomal Membranes of Porcine Pancreas1

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Identifiers

DOI

10.1074/JBC.271.7.3925

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Fatcat ID

release_dpw3mtbv5va6dd2hkvdmjvtomm

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PubMed publication ID

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https://api.fatcat.wiki/v0/release/dpw3mtbv5va6dd2hkvdmjvtomm

30 July 2022