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1
Protein conformational transitions explored by a morphing approach based on normal mode analysis in internal coordinates
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Protein conformational transitions explored by a morphing approach based on normal mode analysis in internal coordinates

PloS one, 2021-11, Vol.16 (11), p.e0258818-e0258818 [Tạp chí có phản biện]

COPYRIGHT 2021 Public Library of Science ;2021 Lee et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2021 Lee et al 2021 Lee et al ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0258818 ;PMID: 34735476

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2
Computational assessment of the feasibility of protonation-based protein sequencing
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Computational assessment of the feasibility of protonation-based protein sequencing

PloS one, 2020-09, Vol.15 (9), p.e0238625-e0238625 [Tạp chí có phản biện]

COPYRIGHT 2020 Public Library of Science ;COPYRIGHT 2020 Public Library of Science ;2020 Miclotte et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2020 Miclotte et al 2020 Miclotte et al ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0238625 ;PMID: 32915813

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3
In silico identification of genetic mutations conferring resistance to acetohydroxyacid synthase inhibitors: A case study of Kochia scoparia
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In silico identification of genetic mutations conferring resistance to acetohydroxyacid synthase inhibitors: A case study of Kochia scoparia

PloS one, 2019-05, Vol.14 (5), p.e0216116-e0216116 [Tạp chí có phản biện]

COPYRIGHT 2019 Public Library of Science ;COPYRIGHT 2019 Public Library of Science ;This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication: https://creativecommons.org/publicdomain/zero/1.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/JOURNAL.PONE.0216116 ;PMID: 31063467

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4
Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains
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Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains

Proceedings of the National Academy of Sciences - PNAS, 2014-07, Vol.111 (29), p.10550-10555 [Tạp chí có phản biện]

copyright © 1993—2008 National Academy of Sciences of the United States of America ;Copyright National Academy of Sciences Jul 22, 2014 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.1402768111 ;PMID: 25002491

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5
Energy landscape and multiroute folding of topologically complex proteins adenylate kinase and 2ouf-knot
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Energy landscape and multiroute folding of topologically complex proteins adenylate kinase and 2ouf-knot

Proceedings of the National Academy of Sciences - PNAS, 2012-10, Vol.109 (44), p.17789-17794 [Tạp chí có phản biện]

copyright © 1993-2008 National Academy of Sciences of the United States of America ;Copyright National Academy of Sciences Oct 30, 2012 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.1201807109 ;PMID: 22753508

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6
Allostery and molecular stripping mechanism in profilin regulated actin filament growth
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Allostery and molecular stripping mechanism in profilin regulated actin filament growth

New journal of physics, 2021-12, Vol.23 (12), p.123010 [Tạp chí có phản biện]

2021 The Author(s). Published by IOP Publishing Ltd on behalf of the Institute of Physics and Deutsche Physikalische Gesellschaft ;2021. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;ISSN: 1367-2630 ;EISSN: 1367-2630 ;DOI: 10.1088/1367-2630/ac3b2d ;CODEN: NJOPFM

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7
Frustration, specific sequence dependence, and nonlinearity in large-amplitude fluctuations of allosteric proteins
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Frustration, specific sequence dependence, and nonlinearity in large-amplitude fluctuations of allosteric proteins

Proceedings of the National Academy of Sciences - PNAS, 2011-03, Vol.108 (9), p.3504-3509 [Tạp chí có phản biện]

Copyright National Academy of Sciences Mar 1, 2011 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.1018983108 ;PMID: 21307307

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8
A comparison of pyogenic liver abscess in patients with or without diabetes: a retrospective study of 246 cases
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A comparison of pyogenic liver abscess in patients with or without diabetes: a retrospective study of 246 cases

BMC gastroenterology, 2018-10, Vol.18 (1), p.144-144, Article 144 [Tạp chí có phản biện]

COPYRIGHT 2018 BioMed Central Ltd. ;Copyright © 2018. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s). 2018 ;ISSN: 1471-230X ;EISSN: 1471-230X ;DOI: 10.1186/s12876-018-0875-y ;PMID: 30285638

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9
RNA3DCNN: Local and global quality assessments of RNA 3D structures using 3D deep convolutional neural networks
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RNA3DCNN: Local and global quality assessments of RNA 3D structures using 3D deep convolutional neural networks

PLoS computational biology, 2018-11, Vol.14 (11), p.e1006514-e1006514 [Tạp chí có phản biện]

COPYRIGHT 2018 Public Library of Science ;COPYRIGHT 2018 Public Library of Science ;2018 Li et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2018 Li et al 2018 Li et al ;ISSN: 1553-7358 ;ISSN: 1553-734X ;EISSN: 1553-7358 ;DOI: 10.1371/journal.pcbi.1006514 ;PMID: 30481171

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10
Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations
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Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations

PLoS computational biology, 2017-09, Vol.13 (9), p.e1005748 [Tạp chí có phản biện]

COPYRIGHT 2017 Public Library of Science ;COPYRIGHT 2017 Public Library of Science ;2017 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Kubo S, Li W, Takada S (2017) Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations. PLoS Comput Biol13(9): e1005748. https://doi.org/10.1371/journal.pcbi.1005748 ;2017 Kubo et al 2017 Kubo et al ;2017 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Kubo S, Li W, Takada S (2017) Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations. PLoS Comput Biol13(9): e1005748. https://doi.org/10.1371/journal.pcbi.1005748 ;ISSN: 1553-7358 ;ISSN: 1553-734X ;EISSN: 1553-7358 ;DOI: 10.1371/journal.pcbi.1005748 ;PMID: 28892477

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