Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Xiangyan Xue"'
Autor:
Shihao Zhang, Xilan Yu, Yuan Zhang, Xiangyan Xue, Qi Yu, Zitong Zha, Madelaine Gogol, Jerry L. Workman, Shanshan Li
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Pyruvate kinase phosphorylates histone H3T11 (H3pT11) and represses gene expression by forming a large complex SESAME (Serine-responsive SAM-containing Metabolic Enzyme). Here the authors show that SESAME-catalyzed H3pT11 regulates telomere silencing
Externí odkaz:
https://doaj.org/article/9e1bd0d0532546299ffe3623112e7b14
Autor:
Qi Yu, Chong Tong, Mingdan Luo, Xiangyan Xue, Qianyun Mei, Lixin Ma, Xiaolan Yu, Wuxiang Mao, Lingbao Kong, Xilan Yu, Shanshan Li
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0175576 (2017)
Cancer cells prefer aerobic glycolysis, but little is known about the underlying mechanism. Recent studies showed that the rate-limiting glycolytic enzymes, pyruvate kinase M2 (PKM2) directly phosphorylates H3 at threonine 11 (H3T11) to regulate gene
Externí odkaz:
https://doaj.org/article/aa8f484596c240c2aaaeb28cfc6fb975
Autor:
Yuan Zhang, Shihao Zhang, Xiangyan Xue, Zitong Zha, Jerry L. Workman, Madelaine Gogol, Xilan Yu, Qi Yu, Shanshan Li
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Telomeres are organized into a heterochromatin structure and maintenance of silent heterochromatin is required for chromosome stability. How telomere heterochromatin is dynamically regulated in response to stimuli remains unknown. Pyruvate kinase Pyk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b8b620267deb77e3041641d788b10a
https://pubmed.ncbi.nlm.nih.gov/33500413
https://pubmed.ncbi.nlm.nih.gov/33500413
Autor:
Xiangyan Xue, Chong Tong, Qianyun Mei, Mingdan Luo, Xiaolan Yu, Qi Yu, Xilan Yu, Lingbao Kong, Shanshan Li, Lixin Ma, Wuxiang Mao
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 4, p e0175576 (2017)
PLoS ONE, Vol 12, Iss 4, p e0175576 (2017)
Cancer cells prefer aerobic glycolysis, but little is known about the underlying mechanism. Recent studies showed that the rate-limiting glycolytic enzymes, pyruvate kinase M2 (PKM2) directly phosphorylates H3 at threonine 11 (H3T11) to regulate gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29b6606740037db40b5b53556e8dcb5a
https://pubmed.ncbi.nlm.nih.gov/28426732
https://pubmed.ncbi.nlm.nih.gov/28426732