The crystal structure of the proprotein processing proteinase furin explains its stringent specificity (Q27641411)

5

object named as

Robert Huber

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author name string

Stefan Henrich

1

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Angus Cameron

2

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Gleb P Bourenkov

3

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Reiner Kiefersauer

4

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Iris Lindberg

6

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Manuel E Than

Nature structural biology

8

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language of work or name

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July 2003

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published in

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volume

10

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page(s)

520-6

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issue

7

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cites work

Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins

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The proprotein convertases

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Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides

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Furin at the cutting edge: from protein traffic to embryogenesis and disease

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Precursor processing by kex2/furin proteases

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Intracellular targeting and structural conservation of a prohormone-processing endoprotease.

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Subtilases: the superfamily of subtilisin-like serine proteases

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Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage

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The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation

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Processing of the Ebola virus glycoprotein by the proprotein convertase furin

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Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160

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Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus

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Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases.

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Mutational analysis of predicted interactions between the catalytic and P domains of prohormone convertase 3 (PC3/PC1)

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The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry

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The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking

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Regulatory roles of the P domain of the subtilisin-like prohormone convertases

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pH-induced conformational transitions of a molten-globule-like state of the inhibitory prodomain of furin: implications for zymogen activation.

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The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'

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Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor

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Inhibitory potency and specificity of subtilase-like pro-protein convertase (SPC) prodomains

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Polyarginines are potent furin inhibitors

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The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo

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A novel free-mounting system for protein crystals: transformation and improvement of diffraction power by accurately controlled humidity changes

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Processing of X-ray diffraction data collected in oscillation mode

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Further additions to MolScript version 1.4, including reading and contouring of electron-density maps

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Identifiers

DOI

10.1038/NSB941

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

3330286

1022392550

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3330286

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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