Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Yuanpeng J, Huang"'
Autor:
Keith J. Fraga, Yuanpeng J. Huang, Theresa A. Ramelot, G.V.T. Swapna, Arwin Lashawn Anak Kendary, Ethan Li, Ian Korf, Gaetano T. Montelione
Publikováno v:
J Magn Reson
NMR is a valuable experimental tool in the structural biologist's toolkit to elucidate the structures, functions, and motions of biomolecules. The progress of machine learning, particularly in structural biology, reveals the critical importance of la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2581f7d857ed640909e0263b24da27c4
https://escholarship.org/uc/item/9z15792m
https://escholarship.org/uc/item/9z15792m
Recent advances in molecular modeling using deep learning have the potential to revolutionize the field of structural biology. In particular, AlphaFold has been observed to provide models of protein structures with accuracy rivaling medium-resolution
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94b8c661afa57058124dc54bbbe7ce49
https://doi.org/10.1101/2022.03.09.483701
https://doi.org/10.1101/2022.03.09.483701
Autor:
Casey A. Cole, David A. Snyder, Yuanpeng J. Huang, Gaetano T. Montelione, Antonio Rosato, Andriy Kryshtafovych, Roberto Tejero, Homayoun Valafar, Chris Sander, Davide Sala, Gaohua Liu, G. V. T. Swapna, Krzysztof Fidelis, Yojiro Ishida, Masayori Inouye, Kelly P Brock
Publikováno v:
Proteins
CASP13 has investigated the impact of sparse NMR data on the accuracy of protein structure prediction. NOESY and 15 N-1 H residual dipolar coupling data, typical of that obtained for 15 N,13 C-enriched, perdeuterated proteins up to about 40 kDa, were
Autor:
Masayori Inouye, Swapna Gurla, Andriy Kryshtafovych, Gaohua Liu, Naohiro Kobayashi, Yojiro Ishida, Beate Bersch, Gaetano T. Montelione, Yutaka Kuroda, Yuanpeng J. Huang, Nan Wu, Ning Zhang, Krzysztof Fidelis, Toshio Yamazaki, Andy LiWang
Publikováno v:
Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, In press, ⟨10.1002/prot.26246⟩
Proteins, vol 89, iss 12
Proteins-Structure, Function and Bioinformatics, In press, ⟨10.1002/prot.26246⟩
Proteins-Structure, Function and Bioinformatics, Wiley, In press, ⟨10.1002/prot.26246⟩
Proteins, vol 89, iss 12
Proteins-Structure, Function and Bioinformatics, In press, ⟨10.1002/prot.26246⟩
NMR studies can provide unique information about protein conformations in solution. In CASP14, three reference structures provided by solution NMR methods were available (T1027, T1029, and T1055), as well as a fourth data set of NMR-derived contacts
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::090ed853abaf8daa5ef12173b5abb054
https://hal.archives-ouvertes.fr/hal-03357450/document
https://hal.archives-ouvertes.fr/hal-03357450/document
Autor:
John Everett, Davide Comoletti, Natalia G. Denissova, Sventja von Daake, Gaetano T. Montelione, Sinem Ozgul, Yuanpeng J. Huang, Cuifeng Yin, Davide Sereni, Sumie Kakehi, Carlie Hanlon
Cell surface molecules are important for development and function of multicellular organisms. Although several methods are available to identify ligand-receptor pairs, ELISA-based methods are particularly amenable to high-throughput screens. ELISA-ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::101a67ccf3844fa296cfb887e119645c
https://doi.org/10.1016/bs.mie.2018.10.001
https://doi.org/10.1016/bs.mie.2018.10.001
Autor:
Chris Sander, Yojiro Ishida, Gaetano T. Montelione, Debora S. Marks, Kelly P Brock, Masayori Inouye, Yuanpeng J. Huang, G. V. T. Swapna
Accurate protein structure determination by solution-state NMR is challenging for proteins greater than about 20 kDa, for which extensive perdeuteration is generally required, providing experimental data that is incomplete (sparse) and ambiguous. How
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36b6f4c8c998439d887432532db36f82
https://doi.org/10.1016/bs.mie.2018.11.004
https://doi.org/10.1016/bs.mie.2018.11.004
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9789811321993
While 3D structure determination of small (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63efec2acaea6d07c6160735ea58625b
https://europepmc.org/articles/PMC6630173/
https://europepmc.org/articles/PMC6630173/
Autor:
Gaetano T. Montelione, Yuanpeng J. Huang, Debora S. Marks, Yuefeng Tang, Thomas A. Hopf, Chris Sander
Publikováno v:
Nature methods
Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistica
Publikováno v:
Journal of Biomolecular NMR. 62:439-451
ASDP is an automated NMR NOE assignment program. It uses a distinct bottom-up topology-constrained network anchoring approach for NOE interpretation, with 2D, 3D and/or 4D NOESY peak lists and resonance assignments as input, and generates unambiguous
Autor:
Yuanpeng J. Huang, John Everett, Gaetano T. Montelione, Surya V.S.R.K. Pulavarti, Thomas Acton, Alexander Eletsky, Thomas Szyperski, Rong Xiao
Publikováno v:
Biomolecular NMR Assignments. 9:135-138
The 500 kDa protein plectin is essential for the cytoskeletal organization of most mammalian cells and it is up-regulated in some types of cancer. Here, we report nearly complete sequence-specific polypeptide backbone, (13)C(β) and methyl group reso