Content deleted Content added
more references |
fix cite error |
||
Line 19:
== Phosphorylation ==
Phosphorylation of chaperone proteins can affect their activity. [[Hsp70|HSP70]], a major chaperone protein, was identified in 2012 as a hotspot of phospho-regulation. <ref>{{Cite journal|last=Beltrao|first=Pedro|last2=Albanèse|first2=Véronique|last3=Kenner|first3=Lillian R.|last4=Swaney|first4=Danielle L.|last5=Burlingame|first5=Alma|last6=Villén|first6=Judit|last7=Lim|first7=Wendell A.|last8=Fraser|first8=James S.|last9=Frydman|first9=Judith|last10=Krogan|first10=Nevan J.|date=2012-07-20|title=Systematic Functional Prioritization of Protein Posttranslational Modifications|url=https://www.cell.com/cell/abstract/S0092-8674(12)00706-4|journal=Cell|language=English|volume=150|issue=2|pages=413–425|doi=10.1016/j.cell.2012.05.036|issn=0092-8674|pmid=22817900}}</ref> Subsequently, phosphorylation of chaperone protein HSP70 by a cyclin dependent kinase was shown to be delay [[cell cycle]] progression in yeast and mammals by altering [[Cyclin D1]] stability (a key regulator of the cell cycle). <ref>{{Cite journal|last=Truman|first=Andrew
|