Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Michael D. Crabtree"'
Autor:
Michael D. Crabtree, Jack Holland, Arvind S. Pillai, Purnima S. Kompella, Leon Babl, Noah N. Turner, James T. Eaton, Georg K.A. Hochberg, Dirk G.A.L. Aarts, Christina Redfield, Andrew J. Baldwin, Timothy J. Nott
Publikováno v:
Cell Reports, Vol 42, Iss 11, Pp 113375- (2023)
Summary: Membraneless organelles, or biomolecular condensates, enable cells to compartmentalize material and processes into unique biochemical environments. While specific, attractive molecular interactions are known to stabilize biomolecular condens
Externí odkaz:
https://doaj.org/article/cff76a2fea4944b2b0c67269ba00369a
Autor:
Fabian Paul, Christoph Wehmeyer, Esam T. Abualrous, Hao Wu, Michael D. Crabtree, Johannes Schöneberg, Jane Clarke, Christian Freund, Thomas R. Weikl, Frank Noé
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Binding and unbinding kinetics are important determinants of protein-protein or small molecule protein functional interactions that can guide drug development. Here the authors exploit the multi-ensemble Markov model framework to develop a computatio
Externí odkaz:
https://doaj.org/article/895ac415114440f59bd90dfcfa45a3b0
Autor:
Fabian Paul, Christoph Wehmeyer, Esam T. Abualrous, Hao Wu, Michael D. Crabtree, Johannes Schöneberg, Jane Clarke, Christian Freund, Thomas R. Weikl, Frank Noé
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-1 (2018)
In the original version of this Article, the Acknowledgement section omitted financial support from the Deutsche Forschungsgemeinschaft grant SFB 958/A4. This error has now been corrected in both the PDF and HTML versions of the Article.
Externí odkaz:
https://doaj.org/article/d0b83249de724e78b176d0adab53f744
Autor:
Leon Babl, Andrew Baldwin, Jack Holland, Michael D. Crabtree, Timothy J. Nott, Purnima Kompella, Noah Turner
Liquid-like membraneless organelles form via multiple, weak interactions between biomolecules. The resulting condensed states constitute novel solvent environments inside eukaryotic cells that partition biomolecules and may favour particular biochemi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::62b92b1467bceb4c80427c23412b41c5
https://doi.org/10.1101/2020.10.29.357863
https://doi.org/10.1101/2020.10.29.357863
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2141
Intracellular compartmentalization through liquid-liquid phase separation is an emerging organizing principle of cell biology. These compartments, such as the nucleolus and stress granules, are collectively known as membraneless organelles or biomole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5648e03274913415b1acec08a6089f05
https://pubmed.ncbi.nlm.nih.gov/32696385
https://pubmed.ncbi.nlm.nih.gov/32696385
Publikováno v:
Methods in Molecular Biology ISBN: 9781071605233
Intracellular compartmentalization through liquid-liquid phase separation is an emerging organizing principle of cell biology. These compartments, such as the nucleolus and stress granules, are collectively known as membraneless organelles or biomole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4270763c13e53dafd26b6988c7368fb2
https://doi.org/10.1007/978-1-0716-0524-0_36
https://doi.org/10.1007/978-1-0716-0524-0_36
Autor:
Arthur Christopoulos, Colin Molloy, Michael D. Crabtree, Simon M. Brooke, Christoffer Bundgaard, Adrian J. Mogg, Patrick M. Sexton, Helen E. Sanger, Karen J. Thompson, Sophie J. Bradley, Christian C. Felder, Andrew B. Tobin, Christopher J. Langmead, Lisa M. Broad, Louis Dwomoh
Publikováno v:
Molecular Pharmacology. 93:645-656
The realization of the therapeutic potential of targeting the M1 muscarinic acetylcholine receptor (mAChR) for the treatment of cognitive decline in Alzheimer’s disease has prompted the discovery of M1 mAChR ligands showing efficacy in alleviating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e4008c1543e1e5e40a2a7a21ba0475a
https://doi.org/10.1124/mol.118.111872
https://doi.org/10.1124/mol.118.111872
Autor:
Michael D, Crabtree, Sarah L, Shammas
Publikováno v:
Methods in enzymology. 611
Intrinsically disordered proteins are abundant in signaling processes such as transcription. Suitable binding and unbinding rates of proteins with their partners are critical for allowing them to perform their biological roles. Understanding how thes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::89be907b8281a3702efe2a5b6af3ae8f
https://pubmed.ncbi.nlm.nih.gov/30471695
https://pubmed.ncbi.nlm.nih.gov/30471695
Autor:
Christian Freund, Michael D. Crabtree, Frank Noé, Hao Wu, Christoph Wehmeyer, Esam T. Abualrous, Thomas R. Weikl, Jane Clarke, Johannes Schöneberg, Fabian Paul
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-1 (2018)
Nature Communications
Nature Communications
Understanding and control of structures and rates involved in protein ligand binding are essential for drug design. Unfortunately, atomistic molecular dynamics (MD) simulations cannot directly sample the excessively long residence and rearrangement t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::633879189dfd6804a6cab79c7afd22af
https://doi.org/10.1038/s41467-018-03452-0
https://doi.org/10.1038/s41467-018-03452-0
Autor:
Sophie J, Bradley, Colin, Molloy, Christoffer, Bundgaard, Adrian J, Mogg, Karen J, Thompson, Louis, Dwomoh, Helen E, Sanger, Michael D, Crabtree, Simon M, Brooke, Patrick M, Sexton, Christian C, Felder, Arthur, Christopoulos, Lisa M, Broad, Andrew B, Tobin, Christopher J, Langmead
Publikováno v:
Molecular Pharmacology
The realization of the therapeutic potential of targeting the M1 muscarinic acetylcholine receptor (mAChR) for the treatment of cognitive decline in Alzheimer’s disease has prompted the discovery of M1 mAChR ligands showing efficacy in alleviating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::53c63447ffaed7a256dbd47cdf0c741d
https://pubmed.ncbi.nlm.nih.gov/29695609
https://pubmed.ncbi.nlm.nih.gov/29695609