Control of protein life-span by N-terminal methionine excision - Wikidata - awgldk - TriplyDB

Control of protein life-span by N-terminal methionine excision

Control of protein life-span by N-terminal methionine excision

http://www.wikidata.org/entity/Q34446156

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Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics N-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule Pathway N-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects Structure and Activity of Human Mitochondrial Peptide Deformylase, a Novel Cancer Target Structure and function of a cyanophage-encoded peptide deformylase Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart Sorting signals, N-terminal modifications and abundance of the chloroplast proteome Ycf93 (Orf105), a small apicoplast-encoded membrane protein in the relict plastid of the malaria parasite Plasmodium falciparum that is conserved in Apicomplexa Generation of Artificial N-end Rule Substrate Proteins In Vivo and In Vitro.Solvent-assisted slow conversion of a dithiazole derivative produces a competitive inhibitor of peptide deformylase.Baking a mass-spectrometry data PIE with McMC and simulated annealing: predicting protein post-translational modifications from integrated top-down and bottom-up data.Comparative metagenomics of microbial traits within oceanic viral communities Inhibition of human peptide deformylase disrupts mitochondrial function In-depth analysis of exoproteomes from marine bacteria by shotgun liquid chromatography-tandem mass spectrometry: the Ruegeria pomeroyi DSS-3 case-study.Identification of protein stability determinants in chloroplasts The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms.Impact of the N-terminal amino acid on targeted protein degradation.A new strategy to produce a defensin: stable production of mutated NP-1 in nitrate reductase-deficient Chlorella ellipsoidea.Methionine aminopeptidases from Mycobacterium tuberculosis as novel antimycobacterial targets Genome-wide identification and in silico analysis of poplar peptide deformylases.A proteogenomic survey of the Medicago truncatula genome Molecular identification and functional characterization of the first Nα-acetyltransferase in plastids by global acetylome profiling.N-terminal protein processing: a comparative proteogenomic analysis.A unique peptide deformylase platform to rationally design and challenge novel active compounds.The N-terminal methionine of cellular proteins as a degradation signal Chloroplasts as expression platforms for plant-produced vaccines.Targeted large-scale analysis of protein acetylation.Modulating protein activity and cellular function by methionine residue oxidation.Understanding chloroplast biogenesis using second-site suppressors of immutans and var2.Formyl-methionine as a degradation signal at the N-termini of bacterial proteins.Three consecutive arginines are important for the mycobacterial peptide deformylase enzyme activity Proteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state and upon deformylation inhibition.From start to finish: amino-terminal protein modifications as degradation signals in plants.The Arabidopsis Chloroplast Stromal N-Terminome: Complexities of Amino-Terminal Protein Maturation and Stability.Two N-terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in Arabidopsis.Effect of salt stress on genes encoding translation-associated proteins in Arabidopsis thaliana.Common therapeutic target for both cancer and obesity.Type 3 peptide deformylases are required for oxidative phosphorylation in Trypanosoma brucei.

P2860

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P2860

Control of protein life-span by N-terminal methionine excision

http://www.wikidata.org/entity/Q34446156

description

2003 nî lūn-bûn

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2003 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2003 թվականի հունվարին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

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name

Control of protein life-span by N-terminal methionine excision

@ast

Control of protein life-span by N-terminal methionine excision

@en

Control of protein life-span by N-terminal methionine excision

@nl

type

label

Control of protein life-span by N-terminal methionine excision

@ast

Control of protein life-span by N-terminal methionine excision

@en

Control of protein life-span by N-terminal methionine excision

@nl

prefLabel

Control of protein life-span by N-terminal methionine excision

@ast

Control of protein life-span by N-terminal methionine excision

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Control of protein life-span by N-terminal methionine excision

@nl

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P1433

The EMBO Journal

P1476

Control of protein life-span by N-terminal methionine excision

@en

P2093

Olivier Vallon

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

P2860

Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi

Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms

The N-end rule: functions, mysteries, uses

Chloroplast ribosomes and protein synthesis

Methionine aminopeptidase gene of Escherichia coli is essential for cell growth

The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2

Structure of human methionine aminopeptidase-2 complexed with fumagillin

Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.

Characterization of an eukaryotic peptide deformylase from Plasmodium falciparum

A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II

P304

13-23

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scholarly article

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10.1093/EMBOJ/CDG007

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1

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22

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Thierry Meinnel

Carmela Giglione

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2003-01-01T00:00:00Z

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10970028

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12505980

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140049

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