Zobrazeno 1 - 10
of 129
pro vyhledávání: '"Richard W, Baker"'
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-1 (2023)
Externí odkaz:
https://doaj.org/article/c6f33251197e47a780a4655907d13cbd
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Abstract The Cullin 5 (CUL5) Ring E3 ligase uses adaptors Elongins B and C (ELOB/C) to bind different SOCS-box-containing substrate receptors, determining the substrate specificity of the ligase. The 18-member ankyrin and SOCS box (ASB) family is the
Externí odkaz:
https://doaj.org/article/0bbb6cb9e2c74688aa91f0f7c786a41f
Publikováno v:
G3: Genes, Genomes, Genetics, Vol 8, Iss 5, Pp 1593-1601 (2018)
The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (RNAPII) is required to regulate transcription and to integrate it with other essential cellular processes. In the budding yeast Saccharomyces cerevisiae, the CTD of Rpb1p consis
Externí odkaz:
https://doaj.org/article/b2a2bf2ac827474ba03bda12b327e052
Autor:
Edward A Partlow, Richard W Baker, Gwendolyn M Beacham, Joshua S Chappie, Andres E Leschziner, Gunther Hollopeter
Publikováno v:
eLife, Vol 8 (2019)
Endocytosis of transmembrane proteins is orchestrated by the AP2 clathrin adaptor complex. AP2 dwells in a closed, inactive state in the cytosol, but adopts an open, active conformation on the plasma membrane. Membrane-activated complexes are also ph
Externí odkaz:
https://doaj.org/article/094aeadc1c9548f2b101e3cf7d38a0e8
Autor:
Junyi Jiao, Mengze He, Sarah A Port, Richard W Baker, Yonggang Xu, Hong Qu, Yujian Xiong, Yukun Wang, Huaizhou Jin, Travis J Eisemann, Frederick M Hughson, Yongli Zhang
Publikováno v:
eLife, Vol 7 (2018)
Sec1/Munc18-family (SM) proteins are required for SNARE-mediated membrane fusion, but their mechanism(s) of action remain controversial. Using single-molecule force spectroscopy, we found that the SM protein Munc18-1 catalyzes step-wise zippering of
Externí odkaz:
https://doaj.org/article/2f2f2bb0b4e54e3b99b0352811480cc3
Autor:
Thomas M. Bartlett, Tyler A. Sisley, Aaron Mychack, Suzanne Walker, Richard W. Baker, David Z. Rudner, Thomas G. Bernhardt
SUMMARYStaphylococcus aureusis a gram-positive pathogen responsible for life-threatening infections that are difficult to treat due to antibiotic resistance. The identification of new vulnerabilities in essential processes like cell envelope biogenes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c213763732d24522d879ba010f6a370
https://doi.org/10.1101/2023.04.24.538170
https://doi.org/10.1101/2023.04.24.538170
Lipid nanodiscs as a template for high-resolution cryo-EM structures of peripheral membrane proteins
Peripheral membrane proteins are ubiquitous throughout cell biology and are required for a variety of cellular processes such as signal transduction, membrane trafficking, and autophagy. Transient binding to the membrane has a profound impact on prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9abd5159f51005f55e622eb13b969aa
https://doi.org/10.1101/2023.03.07.531120
https://doi.org/10.1101/2023.03.07.531120
Autor:
Takako Niikura, Tsutomu Arakawa, Richard W. Baker, Yoshiko Kita, J.M. Reimer, Andres E. Leschziner, Masao Tokunaga
Publikováno v:
The Protein Journal. 40:867-875
Difference circular dichroism (CD) spectroscopy was used here to characterize changes in structure of flexible peptides upon altering their environments. Environmental changes were introduced by binding to a large target structure, temperature shift
Autor:
Roberto Dominguez, T. Arakawa, Peter J. Carman, J.M. Reimer, Andres E. Leschziner, Richard W. Baker
Publikováno v:
Nature structural & molecular biology
Chromatin remodelers regulate the position and composition of nucleosomes throughout the genome, producing different remodeling outcomes despite a shared underlying mechanism based on a conserved RecA DNA translocase. How this functional diversity is
Autor:
Tsutomu, Arakawa, Masao, Tokunaga, Yoshiko, Kita, Takako, Niikura, Richard W, Baker, Janice M, Reimer, Andres E, Leschziner
Publikováno v:
The protein journal. 40(6)
Difference circular dichroism (CD) spectroscopy was used here to characterize changes in structure of flexible peptides upon altering their environments. Environmental changes were introduced by binding to a large target structure, temperature shift