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Literature DB >> 25083864

Chance, destiny, and the inner workings of ClpXP.

Abstract

AAA+ proteases are responsible for protein degradation in all branches of life. Using single-molecule and ensemble assays, Cordova et al. investigate how the bacterial protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic model that recapitulates the interplay between stochastic and deterministic behaviors of ClpXP.

Entities: Chemical Disease Gene

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Year: 2014 PMID： 25083864 PMCID： PMC4945115 DOI： 10.1016/j.cell.2014.07.009

Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582

9 in total

Review 1. A rotary molecular motor that can work at near 100% efficiency.

Authors: K Kinosita; R Yasuda; H Noji; K Adachi
Journal: Philos Trans R Soc Lond B Biol Sci Date: 2000-04-29 Impact factor: 6.237

2. Mechanism of DNA translocation in a replicative hexameric helicase.

Authors: Eric J Enemark; Leemor Joshua-Tor
Journal: Nature Date: 2006-07-20 Impact factor: 49.962

3. Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.

Authors: Andreas Martin; Tania A Baker; Robert T Sauer
Journal: Nature Date: 2005-10-20 Impact factor: 49.962

4. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.

Authors: Jon A Kenniston; Tania A Baker; Julio M Fernandez; Robert T Sauer
Journal: Cell Date: 2003-08-22 Impact factor: 41.582

1 in total

1. Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.

Authors: Julia R Kardon; Yvette Y Yien; Nicholas C Huston; Diana S Branco; Gordon J Hildick-Smith; Kyu Y Rhee; Barry H Paw; Tania A Baker
Journal: Cell Date: 2015-05-07 Impact factor: 41.582

1 in total

Chance, destiny, and the inner workings of ClpXP.

Review 1. A rotary molecular motor that can work at near 100% efficiency.

2. Mechanism of DNA translocation in a replicative hexameric helicase.

3. Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.

4. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.

5. Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine.

Review 6. Marching to the beat of the ring: polypeptide translocation by AAA+ proteases.

7. ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle.

8. An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases.

9. The ClpXP protease unfolds substrates using a constant rate of pulling but different gears.

1. Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.