Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry (Q34581109)

3 August 2017

title

Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry (English)

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3 August 2017

10

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author name string

Zhuoru Wu

1

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3 August 2017

Nieng Yan

2

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3 August 2017

Liang Feng

3

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3 August 2017

Adam Oberstein

4

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3 August 2017

Hanchi Yan

5

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3 August 2017

Rosanna P Baker

6

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3 August 2017

Lichuan Gu

7

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3 August 2017

Philip D Jeffrey

8

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3 August 2017

Sinisa Urban

9

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3 August 2017

publication date

10 November 2006

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Nature Structural & Molecular Biology

3 August 2017

published in

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3 August 2017

volume

13

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3 August 2017

issue

12

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3 August 2017

page(s)

1084-1091

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Regulated intramembrane proteolysis: from the endoplasmic reticulum to the nucleus

3 August 2017

cites work

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A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands

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Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila

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Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling

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Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane

31 March 2020

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Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.

31 March 2020

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Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity

31 March 2020

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Crystal structure of a rhomboid family intramembrane protease.

31 March 2020

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The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers

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Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain

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PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2

31 March 2020

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NSMB1179

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3 August 2017

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