Zobrazeno 1 - 10
of 84
pro vyhledávání: '"Andreas T Matouschek"'
Publikováno v:
Curr Opin Struct Biol
The majority of regulated protein degradation in eukaryotes is accomplished by the 26S proteasome, the large proteolytic complex responsible for removing regulatory proteins and damaged proteins. Proteins are targeted to the proteasome by ubiquitinat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7369daafc44d18168fd43e046c87fcc8
https://doi.org/10.1016/j.sbi.2020.10.010
https://doi.org/10.1016/j.sbi.2020.10.010
Publikováno v:
J Proteome Res
Multiple ion fragmentation methods involving collision-induced dissociation (CID), higher-energy collisional dissociation (HCD) with regular and very high energy settings, and electron-transfer dissociation (ETD) with supplementary HCD (EThcD) were i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8771ebc3dd72d4c78eb8521e8ecf5ba2
https://doi.org/10.1021/acs.jproteome.0c00111
https://doi.org/10.1021/acs.jproteome.0c00111
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
Nature Communications
Nature Communications
Retinoblastoma protein (Rb) is a tumor suppressor that binds and represses E2F transcription factors. In cervical cancer cells, human papilloma virus (HPV) protein E7 binds to Rb, releasing it from E2F to promote cell cycle progression, and inducing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74cafdc292f9ac3f7a590f36ab3c7bcd
http://link.springer.com/article/10.1038/s41467-020-16003-3
http://link.springer.com/article/10.1038/s41467-020-16003-3
Autor:
Andreas T Matouschek, Suzanne Elsasser, Daniel Finley, Kirby Martinez-Fonts, Takuya Tomita, Yuan Shi, Caroline Davis, Andrew R. Nager
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
Nature Communications
Nature Communications
Proteins are targeted to the proteasome by the attachment of ubiquitin chains, which are markedly varied in structure. Three proteasome subunits–Rpn10, Rpn13, and Rpn1–can recognize ubiquitin chains. Here we report that proteins with single chain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::248616188a4662f4c4eef2bfc93b7bc7
https://doaj.org/article/b6829197ab4442dc88d9ed892b9626e3
https://doaj.org/article/b6829197ab4442dc88d9ed892b9626e3
Autor:
J. P. Renn, Andres F. Oberhauser, John F. Marko, H. Bai, Sucharita Bhattacharyya, Dmitrii E. Makarov, Chengzhi He, Hongbin Li, Andreas T Matouschek
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019)
Scientific Reports
Scientific Reports
We investigated the mechanical unfolding of single spectrin molecules over a broad range of loading rates and thus unfolding forces by combining magnetic tweezers with atomic force microscopy. We find that the mean unfolding force increases logarithm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4525504c6b7a2a000a14756e1ea8f04f
http://link.springer.com/article/10.1038/s41598-019-46525-w
http://link.springer.com/article/10.1038/s41598-019-46525-w
Autor:
Kyle M. Miller, Marcus Buschbeck, Fade Gong, Frank Medina, Andreas T Matouschek, Jullian Perren, Ramhari Kumbhar, David Corujo
The histone demethylase KDM5A removes histone H3 lysine 4 methylation, which is involved in transcription and DNA damage responses (DDR). While DDR functions of KDM5A have been identified, how KDM5A recognizes DNA lesion sites within chromatin is unk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::181a56ebaa4e6fa032de78ad1fde548a
https://doi.org/10.1101/2020.07.27.223131
https://doi.org/10.1101/2020.07.27.223131
Autor:
Andreas T Matouschek, Houqing Yu, Adrian H. Elcock, Christopher M. Yellman, Amit Kumar Singh Gautam
The proteasome establishes protein homeostasis by selectively degrading cellular proteins. There are two main prerequisites for a protein to be selected for proteasomal degradation: a ubiquitin tag covalently attached to the protein and a disordered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b80f059fa4f46e8a93cc6ece3e4e27d7
https://doi.org/10.21203/rs.3.rs-38559/v1
https://doi.org/10.21203/rs.3.rs-38559/v1
Publikováno v:
Nature Chemical Biology. 15:210-212
A new method introduces ubiquitin or ubiquitin-like proteins at specific sites in any protein without the requirement of the cellular ubiquitylation machinery. This will help decipher the code by which these modifications control cellular processes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eabf0fbe17602d4819a607e3ef62021
https://doi.org/10.1038/s41589-019-0230-9
https://doi.org/10.1038/s41589-019-0230-9