Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Manuel M, Müller"'
Publikováno v:
Chemical Science. 14:3881-3892
Structure-activity studies with site-specifically modified apoptin in living cells demonstrate that this protein's toxicity is mediated by phosphorylation and downstream interactions with the cytoskeleton.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cbaddb769178eb38fcb80d9a8ff64206
https://doi.org/10.1039/d2sc04481a
https://doi.org/10.1039/d2sc04481a
Autor:
Qi Lin, Hao Lan, Chunmiao Ma, Ryan T. Stendall, Kenneth Shankland, Rebecca A. Musgrave, Peter N. Horton, Carsten Baldauf, Hans-Jörg Hofmann, Craig P. Butts, Manuel M. Müller, Alexander John Andre Cobb
Publikováno v:
Angewandte Chemie International Edition.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c5a833bc885a695fe2558e779796031
https://doi.org/10.1002/anie.202305326
https://doi.org/10.1002/anie.202305326
Autor:
Linjiao Zhou, Matthew T. Holt, Nami Ohashi, Aishan Zhao, Manuel M. Müller, Boyuan Wang, Tom W. Muir
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
The ubiquitylation of histone H2B on lysine 120 is an important modification with roles in a diverse range of nuclear processes. Here, the authors use 'designer' chromatin to show that H2B-ub orients hDot1L into the correct position for activation.
Externí odkaz:
https://doaj.org/article/c8971f0fedfb44acb73222b3980cc7bc
Autor:
Rhys C. Griffiths, Frances R. Smith, Diyuan Li, Jasmine Wyatt, David M. Rogers, Jed E. Long, Lola M. L. Cusin, Patrick J. Tighe, Robert Layfield, Jonathan D. Hirst, Manuel M. Müller, Nicholas J. Mitchell
Publikováno v:
Chemistry – A European Journal. 29
The site-selective modification of peptides and proteins facilitates the preparation of targeted therapeutic agents and tools to interrogate fundamental biochemistry. Among the numerous bioconjugation techniques developed to install groups of interes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80caa832813ad59d1a50ddd17c603d4f
https://doi.org/10.1002/chem.202202503
https://doi.org/10.1002/chem.202202503
Apoptin is a small viral protein capable of inducing cell death selectively in cancer cells. Despite its potential as an anticancer agent, relatively little is known about its mechanism of toxicity and cancer-selectivity. Previous experiments suggest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9eefc33e9006808c9bee1bdb09bbc793
https://doi.org/10.1101/2022.11.23.517692
https://doi.org/10.1101/2022.11.23.517692
Publikováno v:
Chemical Science
The tumor suppressor protein p53 is a master regulator of cell fate. The activity of p53 is controlled by a plethora of posttranslational modifications (PTMs). However, despite extensive research, the mechanisms of this regulation are still poorly un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d1510c38eac7475504190b99da98ed1
https://doi.org/10.1039/d1sc00396h
https://doi.org/10.1039/d1sc00396h
Autor:
Manuel M Müller, Jane R Allison, Narupat Hongdilokkul, Laurent Gaillon, Peter Kast, Wilfred F van Gunsteren, Philippe Marlière, Donald Hilvert
Publikováno v:
PLoS Genetics, Vol 9, Iss 1, p e1003187 (2013)
The contemporary proteinogenic repertoire contains 20 amino acids with diverse functional groups and side chain geometries. Primordial proteins, in contrast, were presumably constructed from a subset of these building blocks. Subsequent expansion of
Externí odkaz:
https://doaj.org/article/0f687fdbf2764a9ca772733f50d682da
Publikováno v:
Biochemistry. 59(39)
Proteins are subject to spontaneous rearrangements of their backbones. Most prominently, asparagine and aspartate residues isomerize to their β-linked isomer, isoaspartate (isoAsp), on time scales ranging from days to centuries. Such modifications a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::011b3a68fb11c897c4fb0e3c730496e0
https://pubmed.ncbi.nlm.nih.gov/32930597
https://pubmed.ncbi.nlm.nih.gov/32930597
Autor:
Manuel M. Müller
Publikováno v:
Biophysical Journal. 121:1a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c679233e755f9dd7e943ac0a001bb732
https://doi.org/10.1016/j.bpj.2021.11.2701
https://doi.org/10.1016/j.bpj.2021.11.2701
Publikováno v:
J Am Chem Soc
Polycomb Repressive Complex 2 (PRC2) catalyzes mono-, di-, and trimethylation of lysine 27 on histone H3 (H3K27me1-3) to control expression of genes important for differentiation and maintenance of cell identity. PRC2 activity is regulated by a numbe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38cb7c5069b682f97596f197c89211da
https://pubmed.ncbi.nlm.nih.gov/31479253
https://pubmed.ncbi.nlm.nih.gov/31479253