Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Jinzen Ikebe"'
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
Abstract Enzymes with low regioselectivity of substrate reaction sites may produce multiple products from a single substrate. When a target product is produced industrially using these enzymes, the production of non-target products (byproducts) cause
Externí odkaz:
https://doaj.org/article/3b5e11fddab54ea69e607d30ff4b5269
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-2 (2022)
Externí odkaz:
https://doaj.org/article/4b25d5fe51374b538cfec12090e2b51a
Autor:
Jovylyn Gatchalian, Xiaodong Wang, Jinzen Ikebe, Khan L. Cox, Adam H. Tencer, Yi Zhang, Nathaniel L. Burge, Luo Di, Matthew D. Gibson, Catherine A. Musselman, Michael G. Poirier, Hidetoshi Kono, Jeffrey J. Hayes, Tatiana G. Kutateladze
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
The chromatin remodeller CHD4 contains two PHD finger reader domains that have been shown to bivalently recognize H3 histone tails. Here, the authors describe a mechanism by which the PHD fingers bind to the intact nucleosome core particle, revealing
Externí odkaz:
https://doaj.org/article/80503b36d74a4bc3b72aa20bc28f7b84
Autor:
Adam H. Tencer, Khan L. Cox, Luo Di, Joseph B. Bridgers, Jie Lyu, Xiaodong Wang, Jennifer K. Sims, Tyler M. Weaver, Hillary F. Allen, Yi Zhang, Jovylyn Gatchalian, Michael A. Darcy, Matthew D. Gibson, Jinzen Ikebe, Wei Li, Paul A. Wade, Jeffrey J. Hayes, Brian D. Strahl, Hidetoshi Kono, Michael G. Poirier, Catherine A. Musselman, Tatiana G. Kutateladze
Publikováno v:
Cell Reports, Vol 21, Iss 2, Pp 455-466 (2017)
Summary: Chromatin remodeling is required for genome function and is facilitated by ATP-dependent complexes, such as nucleosome remodeling and deacetylase (NuRD). Among its core components is the chromodomain helicase DNA binding protein 3 (CHD3) who
Externí odkaz:
https://doaj.org/article/7ca566c3011e443687e83fac93b1d9f8
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 3, p e1004788 (2016)
Acetylation of lysine residues in histone tails is associated with gene transcription. Because histone tails are structurally flexible and intrinsically disordered, it is difficult to experimentally determine the tail conformations and the impact of
Externí odkaz:
https://doaj.org/article/c6a8a2a083e346d0b7e95d881cb045bd
Publikováno v:
Biomolecules, Vol 2, Iss 1, Pp 104-121 (2012)
The phosphorylated kinase-inducible activation domain (pKID) adopts a helix–loop–helix structure upon binding to its partner KIX, although it is unstructured in the unbound state. The N-terminal and C-terminal regions of pKID, which adopt helices
Externí odkaz:
https://doaj.org/article/a18eabe4fb324136bfe5e014625fa10c
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
Scientific Reports
Scientific Reports
Enzymes with low regioselectivity of substrate reaction sites may produce multiple products from a single substrate. When a target product is produced industrially using these enzymes, the production of non-target products (byproducts) causes adverse
Autor:
Jinzen, Ikebe, Hidetoshi, Kono
Publikováno v:
平成29年度 HPCI 利用研究成果集.
We tried to predict docking structures of a complex system of an intrinsically disordered protein (IDP) with high structural flexibility and the receptor protein using Adaptive Lambda Square Dynamics (ALSD) method, which is a molecular dynamics (MD)
Autor:
Jie Lyu, Khan L. Cox, Joseph B. Bridgers, Michael A. Darcy, Jeffrey J. Hayes, Hidetoshi Kono, Hillary F. Allen, Adam H. Tencer, Wei Li, Jennifer K. Sims, Tyler M. Weaver, Xiaodong Wang, Paul A. Wade, Yi Zhang, Catherine A. Musselman, Tatiana G. Kutateladze, Jovylyn Gatchalian, Jinzen Ikebe, Matthew D. Gibson, Brian D. Strahl, Luo Di, Michael G. Poirier
Publikováno v:
Cell Reports, Vol 21, Iss 2, Pp 455-466 (2017)
Summary: Chromatin remodeling is required for genome function and is facilitated by ATP-dependent complexes, such as nucleosome remodeling and deacetylase (NuRD). Among its core components is the chromodomain helicase DNA binding protein 3 (CHD3) who
Publikováno v:
Seibutsu Butsuri. 57:095-097