Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown. - Wikidata - wikimedia - TriplyDB

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

http://www.wikidata.org/entity/Q37206086

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SBDPs and Tau proteins for diagnosis and hypothermia therapy in neonatal hypoxic ischemic encephalopathy.An Efficient and Economical Assay to Screen for Triclosan Binding to FabI.

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Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

http://www.wikidata.org/entity/Q37206086

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 12 August 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

@en

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

@nl

type

label

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

@en

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

@nl

prefLabel

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

@en

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

@nl

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J.BRAINRES.2013.08.010

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Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.

@en

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L W-M Fung

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Marta A Witek

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P2860

Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin

Sequence logos: a new way to display consensus sequences

Spectrin-based skeleton as an actor in cell signaling

Global mapping of the topography and magnitude of proteolytic events in apoptosis

Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini

Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex

Crystal structure of a Src-homology 3 (SH3) domain

Crystal Structure of the Nonerythroid -Spectrin Tetramerization Site Reveals Differences between Erythroid and Nonerythroid Spectrin Tetramer Formation

Predicting coiled coils from protein sequences

Caspases: structure-guided design of drugs to control cell death

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1-15

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scholarly article

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10.1016/J.BRAINRES.2013.08.010

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2013-08-12T00:00:00Z

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