Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Chris H. Hill"'
Autor:
Chris H. Hill, Lukas Pekarek, Sawsan Napthine, Anuja Kibe, Andrew E. Firth, Stephen C. Graham, Neva Caliskan, Ian Brierley
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Many RNA viruses employ programmed –1 ribosomal frameshifting (PRF) to expand their coding capacity and optimize production of viral proteins. Here, the authors report structural and biophysical analysis of protein 2A from a cardiovirus, with insig
Externí odkaz:
https://doaj.org/article/4b234d9264ef4780bb30f06b7dbc26de
Autor:
Chris H. Hill, Georgia M. Cook, Samantha J. Spratley, Stuart Fawke, Stephen C. Graham, Janet E. Deane
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Lysosomal degradation of sphingolipids requires lipid-binding saposin proteins and hydrolytic enzymes. Here the authors present the crystal structure of the hydrolase β-galactocerebrosidase in complex with saposin SapA and give insights into the gly
Externí odkaz:
https://doaj.org/article/2892fdb00d5d43eb9babf8bf3fb7a3dc
Publikováno v:
Viruses, Vol 13, Iss 7, p 1230 (2021)
The product of the interferon-stimulated gene C19orf66, Shiftless (SHFL), restricts human immunodeficiency virus replication through downregulation of the efficiency of the viral gag/pol frameshifting signal. In this study, we demonstrate that bacter
Externí odkaz:
https://doaj.org/article/af04608523794b58871706c821d41b33
Autor:
Mykhaylo Demydchuk, Chris H. Hill, Aiwu Zhou, Gábor Bunkóczi, Penelope E. Stein, Denis Marchesan, Janet E. Deane, Randy J. Read
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
Hunter syndrome is a lysosomal storage disease caused by mutations in the enzyme iduronate-2-sulfatase (IDS). Here, the authors present the IDS crystal structure and give mechanistic insights into mutations that cause Hunter syndrome.
Externí odkaz:
https://doaj.org/article/73c38b90598b4907b8cedce5ff4f26cb
Autor:
Benjamin G Butt, Danielle J Owen, Cy M Jeffries, Lyudmila Ivanova, Chris H Hill, Jack W Houghton, Md Firoz Ahmed, Robin Antrobus, Dmitri I Svergun, John J Welch, Colin M Crump, Stephen C Graham
Publikováno v:
eLife, Vol 9 (2020)
Herpesviruses acquire their membrane envelopes in the cytoplasm of infected cells via a molecular mechanism that remains unclear. Herpes simplex virus (HSV)−1 proteins pUL7 and pUL51 form a complex required for efficient virus envelopment. We show
Externí odkaz:
https://doaj.org/article/cfd82648c6a14487a1d5e6ed851657bb
Autor:
Karla Helena-Bueno, Chinenye L. Ekemezie, Charlotte R. Brown, Arnaud Baslé, James N. Blaza, Chris H. Hill, Sergey V. Melnikov
During starvation and stress, virtually all organisms arrest protein synthesis to conserve energy. Inactive ribosomes are converted into a dormant state, in which they are protected from damage by hibernation factor proteins. In bacteria, two major f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::76956aa9af2776805a7123a319d10d27
https://doi.org/10.1101/2022.11.24.517861
https://doi.org/10.1101/2022.11.24.517861
Autor:
Neva Caliskan, Chris H. Hill
Publikováno v:
Bioscience Reports
Cardioviruses are single-stranded RNA viruses of the family Picornaviridae. In addition to being the first example of internal ribosome entry site (IRES) utilization, cardioviruses also employ a series of alternative translation strategies, such as S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a59d5d81946dc7384c5aa32e24565992
https://eprints.whiterose.ac.uk/185954/1/bsr_2021_0406c.pdf
https://eprints.whiterose.ac.uk/185954/1/bsr_2021_0406c.pdf
Autor:
Sawsan Napthine, Neva Caliskan, Anuja Kibe, Stephen C. Graham, Katherine A. Brown, Chris H. Hill, Andrew E. Firth, Georgia M. Cook, Ian Brierley
Publikováno v:
Nucleic Acids Research
bioRxiv
bioRxiv
The 2A protein of Theiler’s murine encephalomyelitis virus (TMEV) acts as a switch to stimulate programmed −1 ribosomal frameshifting (PRF) during infection. Here we present the X-ray crystal structure of TMEV 2A and define how it recognises the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5db27ac53bdb989daee537874cf6b0c8
https://eprints.whiterose.ac.uk/180488/1/gkab969.pdf
https://eprints.whiterose.ac.uk/180488/1/gkab969.pdf
Publikováno v:
Viruses, Vol 13, Iss 1230, p 1230 (2021)
Viruses
Volume 13
Issue 7
Viruses
Volume 13
Issue 7
The product of the interferon-stimulated gene C19orf66, Shiftless (SHFL), restricts human immunodeficiency virus replication through downregulation of the efficiency of the viral gag/pol frameshifting signal. In this study, we demonstrate that bacter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::135d722fb0d3d079afc2fb933b06fb10
https://www.repository.cam.ac.uk/handle/1810/324638
https://www.repository.cam.ac.uk/handle/1810/324638
Autor:
Shabih Shakeel, Christopher J. Russo, Gianluca Degliesposti, Pablo Alcón, Eeson Rajendra, J.M. Skehel, Ketan J. Patel, Sarah L. Maslen, Carol V. Robinson, Chris H. Hill, Dror S. Chorev, Francis J. O’Reilly, Juri Rappsilber, Shaoda He, Sjors H.W. Scheres, Lori A. Passmore
Publikováno v:
Shakeel, S, Rajendral, E, Alcón, P, O’Reilly, F J, Chorev, D S, Maslen, S, Degliesposti, G, Russo, C J, He, S, Hill, C H, Skehel, J M, Scheres, S H W, Patel, K J, Rappsilber, J, Robinson, C V & Passmore, L A 2019, ' Structure of the fanconi anaemia monoubiquitin ligase complex ', Nature, vol. 575, pp. 234-237 . https://doi.org/10.1038/s41586-019-1703-4
Nature
Nature
The Fanconi anaemia (FA) pathway repairs DNA damage caused by endogenous and chemotherapy-induced DNA crosslinks, and responds to replication stress1,2. Genetic inactivation of this pathway by mutation of genes encoding FA complementation group (FANC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46bffaa0a6d75638ea3668a8eca98bf3
https://doi.org/10.1038/s41586-019-1703-4
https://doi.org/10.1038/s41586-019-1703-4