Matches in SemOpenAlex for { <https://semopenalex.org/work/W154608328> ?p ?o ?g. }
- W154608328 endingPage "75" @default.
- W154608328 startingPage "47" @default.
- W154608328 abstract "The small (76 amino acids) and highly conserved ubiquitin protein plays key roles in the physiology of eukaryotic cells. Protein ubiquitylation has emerged as one of the most important intracellular signaling mechanisms, and in 2004 the Nobel Prize was awarded to Aaron Ciechanower, Avram Hersko, and Irwin Rose for their pioneering studies of the enzymology of ubiquitin attachment. One of the most common features of protein ubiquitylation is the attachment of polyubiquitin chains (four or more ubiquitin moieties attached to each other), which is a widely used mechanism to target proteins for degradation via the 26S proteosome. However, it is noteworthy that the first ubiquitylated protein to be identified was histone H2A, to which a single ubiquitin moiety is most commonly attached. Following this discovery, other histones (H2B, H3, H1, H2A.Z, macroH2A), as well as many nonhistone proteins, have been found to be monoubiquitylated. The role of monoubiquitylation is still elusive because a single ubiquitin moiety is not sufficient to target proteins for turnover, and has been hypothesized to control the assembly or disassembly of multiprotein complexes by providing a protein-binding site. Indeed, a number of ubiquitin-binding domains have now been identified in both polyubiquitylated and monoubiquitylated proteins. Despite the early discovery of ubiquitylated histones, it has only been in the last five or so years that we have begun to understand how histone ubiquitylation is regulated and what roles it plays in the cell. This review will discuss current research on the factors that regulate the attachment and removal of ubiquitin from histones, describe the relationship of histone ubiquitylation to histone methylation, and focus on the roles of ubiquitylated histones in gene expression." @default.
- W154608328 created "2016-06-24" @default.
- W154608328 creator A5005136064 @default.
- W154608328 creator A5012946900 @default.
- W154608328 creator A5024150433 @default.
- W154608328 date "2006-02-10" @default.
- W154608328 modified "2023-10-07" @default.
- W154608328 title "Histone Ubiquitylation and the Regulation of Transcription" @default.
- W154608328 cites W1483766000 @default.
- W154608328 cites W1488978880 @default.
- W154608328 cites W1495218540 @default.
- W154608328 cites W1497941038 @default.
- W154608328 cites W1536662766 @default.
- W154608328 cites W1554656840 @default.
- W154608328 cites W1557500293 @default.
- W154608328 cites W1561767449 @default.
- W154608328 cites W1586131224 @default.
- W154608328 cites W1628512331 @default.
- W154608328 cites W1832030339 @default.
- W154608328 cites W1862466440 @default.
- W154608328 cites W1914441096 @default.
- W154608328 cites W1954801073 @default.
- W154608328 cites W1956603911 @default.
- W154608328 cites W1963545795 @default.
- W154608328 cites W1963996414 @default.
- W154608328 cites W1964096828 @default.
- W154608328 cites W1967364632 @default.
- W154608328 cites W1969958451 @default.
- W154608328 cites W1974016204 @default.
- W154608328 cites W1974768373 @default.
- W154608328 cites W1974875206 @default.
- W154608328 cites W1975102664 @default.
- W154608328 cites W1976172452 @default.
- W154608328 cites W1977188840 @default.
- W154608328 cites W1977208266 @default.
- W154608328 cites W1977374512 @default.
- W154608328 cites W19784639 @default.
- W154608328 cites W1978535727 @default.
- W154608328 cites W1979274256 @default.
- W154608328 cites W1979976015 @default.
- W154608328 cites W1980300257 @default.
- W154608328 cites W1982172694 @default.
- W154608328 cites W1982262507 @default.
- W154608328 cites W1982315838 @default.
- W154608328 cites W1983970621 @default.
- W154608328 cites W1984098022 @default.
- W154608328 cites W1984786295 @default.
- W154608328 cites W1989789417 @default.
- W154608328 cites W1990536596 @default.
- W154608328 cites W1992108755 @default.
- W154608328 cites W1992868975 @default.
- W154608328 cites W1993181132 @default.
- W154608328 cites W1994301929 @default.
- W154608328 cites W1997029250 @default.
- W154608328 cites W1999022187 @default.
- W154608328 cites W1999310200 @default.
- W154608328 cites W1999406663 @default.
- W154608328 cites W2001553480 @default.
- W154608328 cites W2001928543 @default.
- W154608328 cites W2002085309 @default.
- W154608328 cites W2002103750 @default.
- W154608328 cites W2003391080 @default.
- W154608328 cites W2005722151 @default.
- W154608328 cites W2008461545 @default.
- W154608328 cites W2008922065 @default.
- W154608328 cites W2012326746 @default.
- W154608328 cites W2013289317 @default.
- W154608328 cites W2015132841 @default.
- W154608328 cites W2015255326 @default.
- W154608328 cites W2015997780 @default.
- W154608328 cites W2016546870 @default.
- W154608328 cites W2017048095 @default.
- W154608328 cites W2021483806 @default.
- W154608328 cites W2022376508 @default.
- W154608328 cites W2022936129 @default.
- W154608328 cites W2028003321 @default.
- W154608328 cites W2036479240 @default.
- W154608328 cites W2036644816 @default.
- W154608328 cites W2038451572 @default.
- W154608328 cites W2039190089 @default.
- W154608328 cites W2039778682 @default.
- W154608328 cites W2039940539 @default.
- W154608328 cites W2040073289 @default.
- W154608328 cites W2042960789 @default.
- W154608328 cites W2045829055 @default.
- W154608328 cites W2045887257 @default.
- W154608328 cites W2047143392 @default.
- W154608328 cites W2047801109 @default.
- W154608328 cites W2048815297 @default.
- W154608328 cites W2049780043 @default.
- W154608328 cites W2049868369 @default.
- W154608328 cites W2051337966 @default.
- W154608328 cites W2054918042 @default.
- W154608328 cites W2056018903 @default.
- W154608328 cites W2057623594 @default.
- W154608328 cites W2057724970 @default.
- W154608328 cites W2059180978 @default.
- W154608328 cites W2059698383 @default.