A Fragment-Based Ligand Screen Against Part of a Large Protein Machine: The ND1 Domains of the AAA+ ATPase p97/VCP. (Q35563032)

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1 March 2020

title

A Fragment-Based Ligand Screen Against Part of a Large Protein Machine: The ND1 Domains of the AAA+ ATPase p97/VCP (English)

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1 March 2020

5

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author name string

Michael S Chimenti

1

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1 March 2020

Stacie L Bulfer

2

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1 March 2020

R Jeffrey Neitz

3

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1 March 2020

Adam R Renslo

4

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1 March 2020

Thomas L James

6

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1 March 2020

Michelle R Arkin

7

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1 March 2020

Mark J S Kelly

8

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1 March 2020

publication date

17 February 2015

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Journal of Biomolecular Screening

1 March 2020

published in

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1 March 2020

volume

20

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issue

6

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1 March 2020

page(s)

788-800

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Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system

1 March 2020

cites work

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Recent advances in p97/VCP/Cdc48 cellular functions

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Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy

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ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity

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Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase

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Specific inhibition of p97/VCP ATPase and kinetic analysis demonstrate interaction between D1 and D2 ATPase domains

21 January 2018

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Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

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Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase

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Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways

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The role of the N-domain in the ATPase activity of the mammalian AAA ATPase p97/VCP.

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ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain

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Interprotomer motion-transmission mechanism for the hexameric AAA ATPase p97.

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Dynamic flexibility of the ATPase p97 is important for its interprotomer motion transmission

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From experimental design to validated hits a comprehensive walk-through of fragment lead identification using surface plasmon resonance

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Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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