Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Karamanos, TK"'
Publikováno v:
Frontiers in neuroscience. 16
The early stages of protein misfolding and aggregation involve disordered and partially folded protein conformers that contain a high degree of dynamic disorder. These dynamic species may undergo large-scale intra-molecular motions of intrinsically d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35bcd3125a7b14ada5541bdab8ef5f63
https://pubmed.ncbi.nlm.nih.gov/35431773
https://pubmed.ncbi.nlm.nih.gov/35431773
Autor:
Iadanza, MG, Silvers, R, Boardman, J, Smith, HI, Karamanos, TK, Debelouchina, GT, Su, Y, Griffin, RG, Ranson, NA, Radford, SE
All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from proteins associated with different diseases remains unclear. Here, we combine cryo-EM and MAS-NMR to determine the structure of an amyloid fibril formed in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::240becc667d7351f2d79a38a698cef45
Protein aggregation is linked with the onset of several neurodegenerative disorders, including Parkinson's disease (PD), which is associated with the aggregation of α‐synuclein (αSyn). The structural mechanistic details of protein aggregation, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::08a0e7f0b926da2541528753b796a983
https://eprints.whiterose.ac.uk/127258/8/Doherty_et_al-2018-Protein_Science.pdf
https://eprints.whiterose.ac.uk/127258/8/Doherty_et_al-2018-Protein_Science.pdf
Autor:
Martin, EM, Jackson, MP, Gamerdinger, M, Gense, K, Karamanos, TK, Humes, JR, Deuerling, E, Ashcroft, AE, Radford, SE
Publikováno v:
The Journal of Biological Chemistry
As newly synthesized polypeptides emerge from the ribosome, it is crucial that they fold correctly. To prevent premature aggregation, nascent chains interact with chaperones that facilitate folding or prevent misfolding until protein synthesis is com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::29b9478a4f16529351ef5de097310b5a
Publikováno v:
Molecular Cell. 55(2):214-226
In the early stages of amyloid formation, heterogeneous populations of oligomeric species are generated, the affinity, specificity, and nature of which may promote, inhibit, or define the course of assembly. Despite the importance of the intermolecul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::4c6f025857fd65a18207c1025e09096e
The balance between protein folding and misfolding is a crucial determinant of amyloid assembly. Transient intermediates that are sparsely populated during protein folding have been identified as key players in amyloid aggregation. However, due to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::a13013529b2214acafa609da46626ee6
https://kar.kent.ac.uk/71794/1/jacs.6b02464.pdf
https://kar.kent.ac.uk/71794/1/jacs.6b02464.pdf
Autor:
Lane BJ; Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, UK., Ma Y; School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic and Health Science Centre, The University of Manchester, Manchester M13 9PT, UK., Yan N; Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, UK., Wang B; School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic and Health Science Centre, The University of Manchester, Manchester M13 9PT, UK., Ackermann K; EaStCHEM School of Chemistry, Biomedical Sciences Research Complex and Centre of Magnetic Resonance, University of St Andrews, St Andrews KY16 9ST, UK., Karamanos TK; Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK., Bode BE; EaStCHEM School of Chemistry, Biomedical Sciences Research Complex and Centre of Magnetic Resonance, University of St Andrews, St Andrews KY16 9ST, UK., Pliotas C; Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, UK; School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic and Health Science Centre, The University of Manchester, Manchester M13 9PT, UK; Manchester Institute of Biotechnology, The University of Manchester, Manchester M1 7DN, UK. Electronic address: christos.pliotas@manchester.ac.uk.
Publikováno v:
Structure (London, England : 1993) [Structure] 2024 Jun 06; Vol. 32 (6), pp. 739-750.e4. Date of Electronic Publication: 2024 Mar 22.
Autor:
Cawood EE; Astbury Centre for Structural Molecular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK a.j.wilson.1@bham.ac.uk.; School of Chemistry, University of Leeds Woodhouse Lane Leeds LS2 9JT UK., Baker E; School of Biochemistry, University of Bristol Medical Sciences Building, University Walk Bristol BS8 1TD UK d.n.woolfson@bristol.ac.uk.; BrisSynBio, University of Bristol Life Sciences Building, Tyndall Avenue Bristol BS8 1TQ UK., Edwards TA; Astbury Centre for Structural Molecular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK a.j.wilson.1@bham.ac.uk.; School of Molecular and Cellular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK.; College of Biomedical Sciences, Larkin University 18301 N Miami Ave #1 Miami FL 33169 USA., Woolfson DN; School of Chemistry, University of Leeds Woodhouse Lane Leeds LS2 9JT UK.; School of Biochemistry, University of Bristol Medical Sciences Building, University Walk Bristol BS8 1TD UK d.n.woolfson@bristol.ac.uk.; School of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK., Karamanos TK; Department of Life Sciences, Imperial College London London SW7 2BX UK t.karamanos@imperial.ac.uk., Wilson AJ; Astbury Centre for Structural Molecular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK a.j.wilson.1@bham.ac.uk.; School of Chemistry, University of Leeds Woodhouse Lane Leeds LS2 9JT UK.; School of Chemistry, University of Birmingham Edgbaston Birmingham B15 2TT UK.
Publikováno v:
Chemical science [Chem Sci] 2024 Jun 06; Vol. 15 (26), pp. 10237-10245. Date of Electronic Publication: 2024 Jun 06 (Print Publication: 2024).
Autor:
Karamanos TK; Department of Life Sciences, Faculty of Natural Sciences, Imperial College London. Electronic address: t.karamanos@imperial.ac.uk., Matthews S; Department of Life Sciences, Faculty of Natural Sciences, Imperial College London. Electronic address: s.j.matthews@imperial.ac.uk.
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics [Biochim Biophys Acta Proteins Proteom] 2024 Feb 01; Vol. 1872 (2), pp. 140949. Date of Electronic Publication: 2023 Aug 11.
Autor:
Karamanos TK; Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London, UK.
Publikováno v:
Biopolymers [Biopolymers] 2023 Mar; Vol. 114 (3), pp. e23530. Date of Electronic Publication: 2023 Feb 08.