Highly conserved histidine plays a dual catalytic role in protein splicing: a pKa shift mechanism - Wikidata - wikimedia - TriplyDB

Highly conserved histidine plays a dual catalytic role in protein splicing: a pKa shift mechanism

Highly conserved histidine plays a dual catalytic role in protein splicing: a pKa shift mechanism

http://www.wikidata.org/entity/Q37331606

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p K a Coupling at the Intein Active Site: Implications for the Coordination Mechanism of Protein Splicing with a Conserved Aspartate Structural and Mutational Studies of a Hyperthermophilic Intein from DNA Polymerase II of Pyrococcus abyssi A conserved threonine spring-loads precursor for intein splicing Conserved residues that modulate protein trans-splicing of Npu DnaE split intein Design of a Split Intein with Exceptional Protein Splicing Activity Spontaneous proton transfer to a conserved intein residue determines on-pathway protein splicing.A mechanistic study of the spontaneous hydrolysis of glycylserine as the simplest model for protein self-cleavage.Protein splicing: how inteins escape from precursor proteins.Backbone dynamics and global effects of an activating mutation in minimized Mtu RecA inteins.Recent progress in intein research: from mechanism to directed evolution and applications.Cisplatin inhibits protein splicing, suggesting inteins as therapeutic targets in mycobacteria.Dynamics differentiate between active and inactive inteins.Electronic structure of neighboring extein residue modulates intein C-terminal cleavage activity 1H, 13C, and 15N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.SufB intein of Mycobacterium tuberculosis as a sensor for oxidative and nitrosative stresses.Mutual synergistic protein folding in split intein.¹H, ¹³C and ¹⁵N NMR assignments of a Drosophila Hedgehog autoprocessing domain Exploring chemoselective S-to-N acyl transfer reactions in synthesis and chemical biology.Self-cleavage of the Pseudomonas aeruginosa Cell-surface Signaling Anti-sigma Factor FoxR Occurs through an N-O Acyl Rearrangement Intrinsic energy landscapes of amino acid side-chains.Chemical bypass of intein-catalyzed N-S acyl shift in protein splicing.Intein lacking conserved C-terminal motif G retains controllable N-cleavage activity.Mechanism of C-terminal intein cleavage in protein splicing from QM/MM molecular dynamics simulations.Spontaneous C-cleavage of a mini-intein without its conserved N-terminal motif A.

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Highly conserved histidine plays a dual catalytic role in protein splicing: a pKa shift mechanism

http://www.wikidata.org/entity/Q37331606

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on August 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

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name

Highly conserved histidine pla ...... plicing: a pKa shift mechanism

@en

Highly conserved histidine pla ...... licing: a pKa shift mechanism.

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type

label

Highly conserved histidine pla ...... plicing: a pKa shift mechanism

@en

Highly conserved histidine pla ...... licing: a pKa shift mechanism.

@nl

prefLabel

Highly conserved histidine pla ...... plicing: a pKa shift mechanism

@en

Highly conserved histidine pla ...... licing: a pKa shift mechanism.

@nl

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Journal of the American Chemical Society

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Highly conserved histidine pla ...... plicing: a pKa shift mechanism

@en

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Brian Pereira

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Chunyu Wang

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Georges Belfort

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Philip T Shemella

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Saroj K Nayak

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

Scott A McCallum

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

Yangzhong Liu

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

Zhenming Du

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

P2860

InBase: the Intein Database

Structural insights into the protein splicing mechanism of PI-SceI

Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides

Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing

Protein splicing of yeast VMA1-derived endonuclease via thiazolidine intermediates

Crystallographic and Mutational Studies of Mycobacterium tuberculosis recA Mini-inteins Suggest a Pivotal Role for a Highly Conserved Aspartate Residue

NMR structure of a KlbA intein precursor fromMethanococcus jannaschii

Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification

Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity

Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing

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11581-11589

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scholarly article

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10.1021/JA904318W

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32

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131

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Marlene Belfort

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2009-08-01T00:00:00Z

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26693617

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19630416

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2737186

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