Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Martin L. Rennie"'
Autor:
Jimi M. Alex, Martin L. Rennie, Sylvain Engilberge, Gábor Lehoczki, Hajdu Dorottya, Ádám Fizil, Gyula Batta, Peter B. Crowley
Publikováno v:
IUCrJ, Vol 6, Iss 2, Pp 238-247 (2019)
Synthetic macrocycles such as calixarenes and cucurbiturils are increasingly applied as mediators of protein assembly and crystallization. The macrocycle can facilitate assembly by providing a surface on which two or more proteins bind simultaneously
Externí odkaz:
https://doaj.org/article/43b1441bed51482d8aeaf431095ccb11
Autor:
Kiefer O. Ramberg, Francesca Guagnini, Sylvain Engilberge, Javier Pérez, Małgorzata A. Wrońska, Martin L. Rennie, Peter B. Crowley
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
One approach to protein assembly involves water‐soluble supramolecular receptors that act like glues. Bionanoarchitectures directed by these scaffolds are often system‐specific, with few studies investigating their customization. Herein, the modu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3abebabfb3cba9d0a597e40ff6bb207
http://europepmc.org/articles/PMC8596587
http://europepmc.org/articles/PMC8596587
Autor:
Kimon Lemonidis, Martin L Rennie, Connor Arkinson, Viduth K Chaugule, Mairi Clarke, James Streetley, Helen Walden
Publikováno v:
The EMBO journalReferences.
Di-monoubiquitination of the FANCI-FANCD2 (ID2) complex is a central and crucial step for the repair of DNA interstrand crosslinks via the Fanconi anaemia pathway. While FANCD2 ubiquitination precedes FANCI ubiquitination, FANCD2 is also deubiquitina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8fbe554624ddf4b4284dae74c0deab7
https://pubmed.ncbi.nlm.nih.gov/36385258
https://pubmed.ncbi.nlm.nih.gov/36385258
Publikováno v:
The FEBS Journal
Fanconi anemia (FA) is a rare genetic disorder caused by mutations in any of the currently 22 known FA genes. The products of these genes, along with other FA-associated proteins, participate in a biochemical pathway, known as the FA pathway. This pa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b6b96f5c67b9328414ec8ddf7835af3
https://eprints.gla.ac.uk/244287/1/244287.pdf
https://eprints.gla.ac.uk/244287/1/244287.pdf
Publikováno v:
Supramolecular Chemistry. 33:122-128
Water soluble calixarenes are versatile mediators of protein assembly, including the fabrication of crystalline frameworks. Here, we report the X-ray crystal structure of cytochrome c (cytc) co-cry...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2dd8f7f21b52e5855b237866a201b862
https://doi.org/10.1080/10610278.2021.1935946
https://doi.org/10.1080/10610278.2021.1935946
Autor:
Kimon Lemonidis, Martin L. Rennie, Connor Arkinson, Viduth K. Chaugule, Mairi Clarke, James Streetley, Helen Walden
The Fanconi Anaemia pathway operates for the repair of interstrand crosslinks and the maintenance of genomic stability upon replication stalling. Di-monoubiquitination of the FANCI-FANCD2 (ID2) complex is a central and crucial step in this pathway. E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::adc5a0cfec14cce559513ad83a144b9f
https://doi.org/10.1101/2022.04.07.487446
https://doi.org/10.1101/2022.04.07.487446
Publikováno v:
FEBS Letters. 593:2112-2117
Supramolecular receptors such as water-soluble calixarenes are in development as 'molecular glues' for protein assembly. Here, we obtained cocrystals of sulfonato-calix[6]arene (sclx6 ) and yeast cytochrome c (cytc) in the presence of imidazole. A cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::990df2aee85679d51d1b079b02caf5fe
https://doi.org/10.1002/1873-3468.13512
https://doi.org/10.1002/1873-3468.13512
Autor:
Martin L. Rennie, Peter B. Crowley
Publikováno v:
ChemPhysChem. 20:1011-1017
Ligand-mediated regulation of protein assembly occurs frequently in different cellular contexts. Auto-regulated assembly, where a ligand acts as its own competitive inhibitor, provides a mechanism for exquisite control of assembly. Unlike simple prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::591c15b59a28360b6635d584f4306e4c
https://doi.org/10.1002/cphc.201900153
https://doi.org/10.1002/cphc.201900153
Publikováno v:
Nature Structural & Molecular Biology
Ubiquitin-specific protease 1 (USP1) acts together with the cofactor UAF1 during DNA repair processes to specifically remove monoubiquitin signals. One substrate of the USP1−UAF1 complex is the monoubiquitinated FANCI−FANCD2 heterodimer, which is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bb505210e22e29c8460c158007acc39