Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Caroline A, Ewens"'
Publikováno v:
The Journal of Biological Chemistry
Background: p97/VCP disease-linked mutations increase ATPase activity and destabilize the N-D1 domain interaction. Results: Increased N-domain flexibility in p97/VCP increases ATPase activity, whereas locking down the N-domain decreases it. Conclusio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c239f8caa3ff4c1d4257e235962428e3
http://europepmc.org/articles/PMC3318706
http://europepmc.org/articles/PMC3318706
Autor:
Patrik Kloppsteck, Xiaodong ZhangX. Zhang, Caroline A. Ewens, Andreas Förster, Paul S. Freemont
Publikováno v:
Biochemistry and Cell Biology. 88:41-48
p97, also known as VCP (valosin-containing protein), is a hexameric AAA+ ATPase that participates in a variety of cellular processes. It is believed that p97 mediates these processes through the binding of various adaptor proteins. Many factors gover
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::591167c67e0425404ccaf4c023557a1c
https://doi.org/10.1139/o09-128
https://doi.org/10.1139/o09-128
Publikováno v:
Structure (London, England : 1993). 24(5)
Rvb1 and Rvb2 are essential AAA+ proteins that interact together during the assembly and activity of diverse macromolecules including chromatin remodelers INO80 and SWR-C, and ribonucleoprotein complexes including telomerase and snoRNPs. ATP hydrolys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::321e2b6686288d7ce25c7d52a6583684
https://pubmed.ncbi.nlm.nih.gov/27112599
https://pubmed.ncbi.nlm.nih.gov/27112599
Autor:
Ima-Obong Ebong, Paul S. Freemont, Patrik Kloppsteck, Caroline A. Ewens, Ciaran Mckeown, Carol V. Robinson, Silvia Panico, Xiaodong Zhang
Publikováno v:
The Journal of Biological Chemistry
Background: p97 function is facilitated by a huge array of varied adaptor proteins, including FAF1. Results: FAF1 binds over the AAA rings of p97 alone and in a trimer-hexamer arrangement. Conclusion: p97 and FAF1 bind with a similar affinity and in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00e5a1d9ade7fb653d61a5712bca54ce
http://hdl.handle.net/11588/584902
http://hdl.handle.net/11588/584902
Publikováno v:
Biochimica et biophysica acta. 1823(1)
The AAA protein p97 is a central component in the ubiquitin–proteasome system, in which it is thought to act as a molecular chaperone, guiding protein substrates to the 26S proteasome for degradation. This function is dependent on association with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::124f5c4df2655a5f78e49d165ce923dd
https://pubmed.ncbi.nlm.nih.gov/21963883
https://pubmed.ncbi.nlm.nih.gov/21963883
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 88(1)
p97, also known as VCP (valosin-containing protein), is a hexameric AAA+ ATPase that participates in a variety of cellular processes. It is believed that p97 mediates these processes through the binding of various adaptor proteins. Many factors gover
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::588fec23182d2055665ab2c0c8b2d04f
https://pubmed.ncbi.nlm.nih.gov/20130678
https://pubmed.ncbi.nlm.nih.gov/20130678