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The crystal structure of caspase-6, a selective effector of axonal degeneration

The crystal structure of caspase-6, a selective effector of axonal degeneration

http://www.wikidata.org/entity/Q27657093

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Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation Substrate-Induced Conformational Changes Occur in All Cleaved Forms of Caspase-6 Zinc-mediated Allosteric Inhibition of Caspase-6 Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation Inhibitory Mechanism of Caspase-6 Phosphorylation Revealed by Crystal Structures, Molecular Dynamics Simulations, and Biochemical Assays Phosphorylation regulates assembly of the caspase-6 substrate-binding groove.PROSPER: an integrated feature-based tool for predicting protease substrate cleavage sites.Pharmacological inhibition of caspase-2 protects axotomised retinal ganglion cells from apoptosis in adult rats A multipronged approach for compiling a global map of allosteric regulation in the apoptotic caspases.Effector caspases and leukemia Sox11 Reduces Caspase-6 Cleavage and Activity.Small Molecule Active Site Directed Tools for Studying Human Caspases An optimized activity-based probe for the study of caspase-6 activation.Targeting caspase-6 and caspase-8 to promote neuronal survival following ischemic stroke.Substrate and inhibitor-induced dimerization and cooperativity in caspase-1 but not caspase-3.A tunable, modular approach to fluorescent protease-activated reporters.What can we learn about stroke from retinal ischemia models?Caspase-6 Undergoes a Distinct Helix-Strand Interconversion upon Substrate Binding.Peptide inhibitors: Four of a kind beats a pair.Promoting crystallization of antibody-antigen complexes via microseed matrix screening.Caspase-6 latent state stability relies on helical propensity.Palmitoylation of caspase-6 by HIP14 regulates its activation.The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays.Multiple proteolytic events in caspase-6 self-activation impact conformations of discrete structural regions.Efficient expression and purification of recombinant human μ-calpain using an Escherichia coli expression system.Rare human Caspase-6-R65W and Caspase-6-G66R variants identify a novel regulatory region of Caspase-6 activity.

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The crystal structure of caspase-6, a selective effector of axonal degeneration

http://www.wikidata.org/entity/Q27657093

description

2009 nî lūn-bûn

@nan

2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

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2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

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2009年論文

@zh-tw

2009年论文

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name

The crystal structure of caspase-6, a selective effector of axonal degeneration

@ast

The crystal structure of caspase-6, a selective effector of axonal degeneration

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The crystal structure of caspase-6, a selective effector of axonal degeneration

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type

label

The crystal structure of caspase-6, a selective effector of axonal degeneration

@ast

The crystal structure of caspase-6, a selective effector of axonal degeneration

@en

The crystal structure of caspase-6, a selective effector of axonal degeneration

@nl

prefLabel

The crystal structure of caspase-6, a selective effector of axonal degeneration

@ast

The crystal structure of caspase-6, a selective effector of axonal degeneration

@en

The crystal structure of caspase-6, a selective effector of axonal degeneration

@nl

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The crystal structure of caspase-6, a selective effector of axonal degeneration

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Allan D'arcy

http://www.w3.org/2001/XMLSchema#string

Arnaud Decock

http://www.w3.org/2001/XMLSchema#string

Christophe Briand

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Gabriele Meder

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Martin Renatus

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Renato Baumgartner

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Richard Morse

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Ulrich Hassiepen

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P2860

APP binds DR6 to trigger axon pruning and neuron death via distinct caspases

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Structure and mechanism of interleukin-1 beta converting enzyme

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Use of non-crystallographic symmetry in protein structure refinement

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The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32

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429-39

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10.1042/BJ20090540

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3

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423

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2009-10-12T00:00:00Z

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19694615

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crystal structure