Disease-Associated Mutations in CEP120 Destabilize the Protein and Impair Ciliogenesis

Autor: Joseph, Nimesh, Al-Jassar, Caezar, Johnson, Christopher M, Andreeva, Antonina, Barnabas, Deepak D, Freund, Stefan MV, Gergely, Fanni, Van Breugel, Mark

Publikováno v: Cell Reports, Vol 23, Iss 9, Pp 2805-2818 (2018)
Cell Reports
'Cell Reports ', vol: 23, pages: 2805-2818 (2018)

Summary Ciliopathies are a group of genetic disorders caused by a failure to form functional cilia. Due to a lack of structural information, it is currently poorly understood how ciliopathic mutations affect protein functionality to give rise to the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cef7f5e2063c29ec65cb6ad9b2636859
https://www.repository.cam.ac.uk/handle/1810/278907

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis.

Autor: Wauer, Tobias, Swatek, Kirby N, Wagstaff, Jane L, Gladkova, Christina, Pruneda, Jonathan N, Michel, Martin A, Gersch, Malte, Johnson, Christopher M, Freund, Stefan MV, Komander, David

Publikováno v: EMBO Journal; Feb2015, Vol. 34 Issue 3, p307-325, 19p

FtsA forms actin-like protofilaments.

Autor: Szwedziak, Piotr, Wang, Qing, Freund, Stefan MV, Löwe, Jan

Publikováno v: EMBO Journal; 5/16/2012, Vol. 31 Issue 10, p2249-2260, 12p, 1 Color Photograph, 4 Diagrams, 1 Chart, 1 Graph

Controlled Ligand Exchange Between Ruthenium Organometallic Cofactor Precursors and a Naïve Protein Scaffold Generates Artificial Metalloenzymes Catalysing Transfer Hydrogenation

Autor: Biggs, George S, Klein, Oskar James, Maslen, Sarah L, Skehel, J Mark, Rutherford, Trevor J, Freund, Stefan MV, Hollfelder, Florian, Boss, Sally R, Barker, Paul D

Many natural metalloenzymes assemble from proteins and biosynthesised complexes, generating potent catalysts by changing metal coordination. Here we adopt the same strategy to generate artificial metalloenzymes (ArMs) using ligand exchange to unmask

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::feec7a2ad7063d6e84a910fa33b51ce6

Mechanism of completion of peptidyltransferase centre assembly in eukaryotes.

Autor: Kargas V; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Castro-Hartmann P; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Escudero-Urquijo N; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Dent K; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Hilcenko C; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Sailer C; Department of Biology, University of Konstanz, Konstanz, Germany., Zisser G; Institute of Molecular Biosciences, University of Graz, Graz, Austria., Marques-Carvalho MJ; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Pellegrino S; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Wawiórka L; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom.; Department of Molecular Biology, Maria Curie-Skłodowska University, Lublin, Poland., Freund SM; MRC Laboratory of Molecular Biology, Cambridge, United Kingdom., Wagstaff JL; MRC Laboratory of Molecular Biology, Cambridge, United Kingdom., Andreeva A; MRC Laboratory of Molecular Biology, Cambridge, United Kingdom., Faille A; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom., Chen E; Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom., Stengel F; Department of Biology, University of Konstanz, Konstanz, Germany., Bergler H; Institute of Molecular Biosciences, University of Graz, Graz, Austria., Warren AJ; Cambridge Institute for Medical Research, Cambridge, United Kingdom.; Department of Haematology, University of Cambridge, Cambridge, United Kingdom.; Wellcome Trust-Medical Research Council Stem Cell Institute, University of Cambridge, Cambridge, United Kingdom.

Publikováno v: ELife [Elife] 2019 May 22; Vol. 8. Date of Electronic Publication: 2019 May 22.