Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Alexander S. Baier"'
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
The multi-subunit SWR1C remodeler deposits histone variant H2A.Z at nucleosomes flanking protein-coding genes. Here the authors use single-molecule and ensemble methodologies to identify three ATP-dependent phases in the H2A.Z deposition reaction.
Externí odkaz:
https://doaj.org/article/4f912a6a1e004577aac46127ebee3290
Publikováno v:
eLife, Vol 13 (2024)
The yeast SWR1C chromatin remodeling enzyme catalyzes the ATP-dependent exchange of nucleosomal histone H2A for the histone variant H2A.Z, a key variant involved in a multitude of nuclear functions. How the 14-subunit SWR1C engages the nucleosomal su
Externí odkaz:
https://doaj.org/article/9557f149d12e46b1a537c93f76e3ca3a
Autor:
R. Grant Rowe, Daniel S. Pearson, Longfei Wang, Areum Han, Conor McMahon, Chunxiao Yu, Alexander S. Baier, William Marion, George Q. Daley, Andrew C. Kruse, Wanying Ji, Hao Wu, Yu-Chung Huang, Piotr Sliz
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Terminal uridylyltransferases are writers of poly(U) tails in diverse RNA uridylation pathways. In the let-7 pathway, the LIN28:pre-let-7:TUTase ribonucleoprotein complex regulates the processing and maturation of the let-7 microRNA, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebf31aa13bda3988a27b49f3120b1f79
http://europepmc.org/articles/PMC7060709
http://europepmc.org/articles/PMC7060709
Autor:
Alexander S. Baier, Craig L. Peterson
Publikováno v:
Methods Enzymol
Helicase Enzymes Part B ISBN: 9780323997737
Helicase Enzymes Part B ISBN: 9780323997737
The dynamic nature of chromatin is an essential mechanism by which gene expression is regulated. Chromatin is comprised of nucleosomes, an octamer of histone proteins wrapped by DNA, and manipulation of these structures is carried out by a family of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2551d45ae0a0d636f2739122be23b7f
https://europepmc.org/articles/PMC10107425/
https://europepmc.org/articles/PMC10107425/
Autor:
Sanduo Zheng, Aashish Manglik, Aaron M. Ring, Daniel Hilger, Alexander S. Baier, Andrew C. Kruse, Janice X. Ong, Sarah C. Erlandson, Roberta Pascolutti, Marcin Wegrecki, Conor McMahon, Søren G. F. Rasmussen
Publikováno v:
Nature structural & molecular biology, vol 25, iss 3
Camelid single-domain antibody fragments (‘nanobodies’) provide the remarkable specificity of antibodies within a single 15-kDa immunoglobulin VHH domain. This unique feature has enabled applications ranging from use as biochemical tools to thera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76df3b91aeb1ef05a3b740c8c4924696
https://pubmed.ncbi.nlm.nih.gov/29556103
https://pubmed.ncbi.nlm.nih.gov/29556103
Autor:
Sarah C. Erlandson, Andrew C. Kruse, Janice X. Ong, Roberta Pascolutti, Alexander S. Baier, Aaron M. Ring, Conor McMahon, Sanduo Zheng, Aashish Manglik, Daniel Hilger
Camelid single-domain antibody fragments (“nanobodies”) provide the remarkable specificity of antibodies within a single immunoglobulin VHH domain. This unique feature enables applications ranging from their use as biochemical tools to therapeuti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9caec019e40935850fff0152c09820de
https://doi.org/10.1101/151043
https://doi.org/10.1101/151043