(Q24305015)

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Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins

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2 January 2020

Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins (English)

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2 January 2020

Signal peptide peptidase like 2B

1 reference

GOA release 2020-03-11

Signal peptide peptidase like 2A

1 reference

GOA release 2020-03-11

Signal peptide peptidase like 2C

1 reference

GOA release 2020-03-11

Signal peptide peptidase like 3

1 reference

GOA release 2020-03-11

Histocompatibility minor 13

1 reference

GOA release 2020-03-11

Marius K Lemberg

2

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2 January 2020

4

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2 January 2020

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Elena Friedmann

1

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2 January 2020

Andreas Weihofen

3

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2 January 2020

Uwe Dengler

5

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2 January 2020

Giorgio Rovelli

6

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2 January 2020

Bruno Martoglio

7

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2 January 2020

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21 September 2004

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2 January 2020

Journal of Biological Chemistry

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2 January 2020

279

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2 January 2020

50790-50798

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2 January 2020

49

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2 January 2020

Notch signaling: from the outside in

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Analysis of polypeptides by sodium dodecyl sulfate-polyacrylamide gel electrophoresis alongside in vitro-generated reference peptides

1 reference

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Consensus predictions of membrane protein topology

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Reliability of transmembrane predictions in whole-genome data

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On the mechanism of SPP-catalysed intramembrane proteolysis; conformational control of peptide bond hydrolysis in the plane of the membrane

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The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor

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Protein topology of presenilin 1

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Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex

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Signal sequences: more than just greasy peptides

1 reference

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Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs

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Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis

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Novel class of polytopic proteins with domains associated with putative protease activity

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Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity

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The role of presenilin cofactors in the gamma-secretase complex

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Membrane-protein biosynthesis at the endoplasmic reticulum

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Large-scale analysis of the human and mouse transcriptomes

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Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilins

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Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3

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Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins

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Membrane topology of Alzheimer's disease-related presenilin 1. Evidence for the existence of a molecular species with a seven membrane-spanning and one membrane-embedded structure

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Targeting presenilin-type aspartic protease signal peptide peptidase with gamma-secretase inhibitors

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Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor

1 reference

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Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets

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Identification of a novel family of presenilin homologues

1 reference

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Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs

1 reference

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7 January 2021

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1 reference

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7 January 2021

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Intramembrane proteolysis: theme and variations.

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Identifiers

10.1074/JBC.M407898200

1 reference

Europe PubMed Central

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1 reference

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