Crystal structure of a rhomboid family intramembrane protease. (Q54453416)

30 May 2018

title

Crystal structure of a rhomboid family intramembrane protease. (English)

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30 May 2018

author name string

Yongcheng Wang

series ordinal

1

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30 May 2018

Yingjiu Zhang

series ordinal

2

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30 May 2018

Ya Ha

series ordinal

3

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30 May 2018

language of work or name

English

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publication date

11 October 2006

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30 May 2018

published in

Nature

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30 May 2018

volume

444

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issue

7116

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30 May 2018

page(s)

179-180

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30 May 2018

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

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A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma

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

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

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Global topology analysis of the Escherichia coli inner membrane proteome

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

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Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.

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The GxxxG motif: a framework for transmembrane helix-helix association

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Crystal structure of a catalytic antibody with a serine protease active site

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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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Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease

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inferred from DOI database lookup

7 January 2021

based on heuristic

Membrane topology of the C. elegans SEL-12 presenilin

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NATURE05255

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30 May 2018

Dimensions Publication ID

1018025907

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30 May 2018