Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kolja Stahl"'
Autor:
Kolja Stahl, Robert Warneke, Lorenz Demann, Rica Bremenkamp, Björn Hormes, Oliver Brock, Jörg Stülke, Juri Rappsilber
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-10 (2024)
Abstract Scarcity of structural and evolutionary information on protein complexes poses a challenge to deep learning-based structure modelling. We integrate experimental distance restraints obtained by crosslinking mass spectrometry (MS) into AlphaFo
Externí odkaz:
https://doaj.org/article/df6ffcb787c145dca5539fdb3ef99902
Publikováno v:
BMC Bioinformatics, Vol 18, Iss 1, Pp 1-11 (2017)
Abstract Background Accurately predicted contacts allow to compute the 3D structure of a protein. Since the solution space of native residue-residue contact pairs is very large, it is necessary to leverage information to identify relevant regions of
Externí odkaz:
https://doaj.org/article/5344f4cc3fcf469a95d555354c13fa27
Autor:
Adam Belsom, Michael Schneider, Lutz Fischer, Mahmoud Mabrouk, Kolja Stahl, Oliver Brock, Juri Rappsilber
Publikováno v:
Wellcome Open Research, Vol 1 (2016)
Determining the structure of a protein by any method requires various contributions from experimental and computational sides. In a recent study, high-density cross-linking/mass spectrometry (HD-CLMS) data in combination with ab initio structure pred
Externí odkaz:
https://doaj.org/article/08e0dff986974d9582c7bb51d91d4f9d
Publikováno v:
Stahl, K, Graziadei, A, Dau, T, Brock, O & Rappsilber, J 2023, ' Protein structure prediction with in-cell photo-crosslinking mass spectrometry and deep learning ', Nature Biotechnology . https://doi.org/10.1038/s41587-023-01704-z
While AlphaFold2 can predict accurate protein structures from the primary sequence, challenges remain for proteins that undergo conformational changes or for which few homologous sequences are known. Here we introduce AlphaLink, a modified version of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb146c0b69461f20fe053f53612f4dcf
https://www.pure.ed.ac.uk/ws/files/341650964/s41587_023_01704_z.pdf
https://www.pure.ed.ac.uk/ws/files/341650964/s41587_023_01704_z.pdf
Publikováno v:
Scopus-Elsevier
Both the Chamberlin–Courant and Monroe rules are voting rules that solve the problem of fully proportional representation: given a set of candidates and a set of voters, they select committees of candidates whose members represent the voters so tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::596f5817fcf8606c4bafdb6aef143c3c
https://doi.org/10.1007/s10732-018-9376-y
https://doi.org/10.1007/s10732-018-9376-y
Autor:
Adam, Belsom, Michael, Schneider, Lutz, Fischer, Mahmoud, Mabrouk, Kolja, Stahl, Oliver, Brock, Juri, Rappsilber
Publikováno v:
Wellcome Open Research
Determining the structure of a protein by any method requires various contributions from experimental and computational sides. In a recent study, high-density cross-linking/mass spectrometry (HD-CLMS) data in combination with ab initio structure pred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::96a4ba6eceaa68e07051293acf3942d2
https://pubmed.ncbi.nlm.nih.gov/28317030
https://pubmed.ncbi.nlm.nih.gov/28317030
Autor:
Adam Belsom, Kolja Stahl, Juri Rappsilber, Oliver Brock, Michael Schneider, Lutz Fischer, Mahmoud Mabrouk
Publikováno v:
Belsom, A, Schneider, M, Fischer, L, Mabrouk, M, Stahl, K, Brock, O & Rappsilber, J 2017, ' Blind testing cross-linking/mass spectrometry under the auspices of the 11th critical assessment of methods of protein structure prediction (CASP11) ', Wellcome Open Research . https://doi.org/10.12688/wellcomeopenres.10046.1
Determining the structure of a protein by any method requires various contributions from experimental and computational sides. In a recent study, high-density cross-linking/mass spectrometry (HD-CLMS) data in combination with ab initio structure pred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c48fb4d1c5e1dbd6a9ed8c2f91099760
https://www.pure.ed.ac.uk/ws/files/35256181/CLMS_CASP_Rappsilber_accepted_version.pdf
https://www.pure.ed.ac.uk/ws/files/35256181/CLMS_CASP_Rappsilber_accepted_version.pdf
Publikováno v:
Experimental Algorithms ISBN: 9783319200859
SEA
SEA
We consider the following problem. Given a graph and a rational numberi¾?$$\mu $$, $$0 < \mu \le 1$$, find a connected subgraph of density at leasti¾?$$\mu $$ with the largest number of vertices. Here, the density of an $$n$$-vertex graph with $$m$
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1dce4e41e7383c3ee1cd85b278afcdb
https://doi.org/10.1007/978-3-319-20086-6_7
https://doi.org/10.1007/978-3-319-20086-6_7