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Wyszukujesz frazę ""Protein Conformation"" wg kryterium: Temat


Tytuł :
Structural snapshot of the mitochondrial protein import gate.
Autorzy :
Araiso Y; Department of Clinical Laboratory Science, Division of Health Sciences, Graduate School of Medical Science, Kanazawa University, Japan.
Imai K; Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan.
Endo T; Faculty of Life Sciences, Kyoto Sangyo University, Japan.; Institute for Protein Dynamics, Kyoto Sangyo University, Japan.
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Źródło :
The FEBS journal [FEBS J] 2021 Sep; Vol. 288 (18), pp. 5300-5310. Date of Electronic Publication: 2020 Dec 26.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation*
Carrier Proteins/*ultrastructure
Mitochondrial Membrane Transport Proteins/*ultrastructure
Saccharomyces cerevisiae Proteins/*ultrastructure
Carrier Proteins/genetics ; Mitochondria/genetics ; Mitochondria/ultrastructure ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/ultrastructure ; Multiprotein Complexes/genetics ; Multiprotein Complexes/ultrastructure ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand/genetics ; Protein Transport/genetics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/ultrastructure ; Saccharomyces cerevisiae Proteins/genetics
Czasopismo naukowe
Tytuł :
De novo design of transmembrane β barrels.
Autorzy :
Vorobieva AA; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
White P; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.
Liang B; Department of Molecular Physiology and Biological Physics and Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA 22903, USA.
Horne JE; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.
Bera AK; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Chow CM; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Gerben S; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Marx S; Department of Molecular Engineering and Sciences, University of Washington, Seattle, WA 98195, USA.
Kang A; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Stiving AQ; Department of Chemistry and Biochemistry, Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.
Harvey SR; Department of Chemistry and Biochemistry, Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.
Marx DC; TC Jenkins Department of Biophysics Johns Hopkins University, Baltimore, MD 21218, USA.
Khan GN; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.
Fleming KG; TC Jenkins Department of Biophysics Johns Hopkins University, Baltimore, MD 21218, USA.
Wysocki VH; Department of Chemistry and Biochemistry, Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.
Brockwell DJ; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.
Tamm LK; Department of Molecular Physiology and Biological Physics and Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA 22903, USA.
Radford SE; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.
Baker D; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. .; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
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Źródło :
Science (New York, N.Y.) [Science] 2021 Feb 19; Vol. 371 (6531).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Computer Simulation*
Models, Molecular*
Protein Conformation, beta-Strand*
Protein Engineering*
Membrane Proteins/*chemistry
Amino Acid Sequence ; Crystallography, X-Ray ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers ; Magnetic Resonance Spectroscopy ; Membranes, Artificial ; Micelles ; Protein Conformation ; Protein Folding ; Protein Stability
Czasopismo naukowe
Tytuł :
Structural Water Stabilizes Protein Motifs in Liquid Protein Phase: The Folding Mechanism of Short β-Sheets Coupled to Phase Transition.
Autorzy :
Papp D; Laboratory of Structural Chemistry and Biology, MTA ELTE Protein Modelling Research Group, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, H-1117 Budapest, Hungary.; MTA-SZTE Lendület Computational Reaction Dynamics Research Group, Interdisciplinary Excellence Centre, Department of Physical Chemistry and Materials Science, Institute of Chemistry, University of Szeged, Rerrich Béla tér 1, H-6720 Szeged, Hungary.
Szigyártó IC; Biomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary.
Nordén B; Department of Chemical and Biological Engineering, Physical Chemistry, Chalmers University of Technology, SE-412 96 Göteborg, Sweden.
Perczel A; Laboratory of Structural Chemistry and Biology, MTA ELTE Protein Modelling Research Group, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, H-1117 Budapest, Hungary.
Beke-Somfai T; Biomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Aug 10; Vol. 22 (16). Date of Electronic Publication: 2021 Aug 10.
Typ publikacji :
Journal Article
MeSH Terms :
Phase Transition/*drug effects
Protein Conformation, beta-Strand/*drug effects
Water/*pharmacology
Amino Acid Motifs/drug effects ; Chemical Fractionation/methods ; Computer Simulation ; Hydrophobic and Hydrophilic Interactions/drug effects ; Kinetics ; Macromolecular Substances/chemistry ; Models, Molecular ; Protein Conformation/drug effects ; Protein Folding/drug effects ; Protein Stability/drug effects ; Quantum Theory ; Viscosity ; Water/chemistry
Czasopismo naukowe
Tytuł :
Structure relationship of metalloporphyrins in inhibiting the aggregation of hIAPP.
Autorzy :
Wu J; Hubei Key Laboratory of Bioinorganic Chemistry & Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science & Technology, Wuhan 430074, PR China; Department of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, Switzerland.
Yin X; Hubei Key Laboratory of Bioinorganic Chemistry & Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science & Technology, Wuhan 430074, PR China.
Ye H; Hubei Key Laboratory of Bioinorganic Chemistry & Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science & Technology, Wuhan 430074, PR China; School of Chemistry and Chemical Engineering, Jinggangshan University, Ji'an, Jiangxi 343009, PR China.
Gao Z; Hubei Key Laboratory of Bioinorganic Chemistry & Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science & Technology, Wuhan 430074, PR China. Electronic address: .
Li H; Hubei Key Laboratory of Bioinorganic Chemistry & Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science & Technology, Wuhan 430074, PR China. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2021 Jan 15; Vol. 167, pp. 141-150. Date of Electronic Publication: 2020 Nov 27.
Typ publikacji :
Journal Article
MeSH Terms :
Models, Molecular*
Protein Aggregates*
Protein Conformation*
Islet Amyloid Polypeptide/*chemistry
Metalloporphyrins/*chemistry
Amyloid/chemistry ; Amyloid/ultrastructure ; Circular Dichroism ; Humans ; Islet Amyloid Polypeptide/metabolism ; Microscopy, Atomic Force ; Molecular Structure ; Protein Conformation, beta-Strand ; Protein Stability ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
An S/T motif controls reversible oligomerization of the Hsp40 chaperone DNAJB6b through subtle reorganization of a β sheet backbone.
Autorzy :
Karamanos TK; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Tugarinov V; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Clore GM; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 .
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Dec 01; Vol. 117 (48), pp. 30441-30450. Date of Electronic Publication: 2020 Nov 16.
Typ publikacji :
Journal Article; Research Support, N.I.H., Intramural
MeSH Terms :
Amino Acid Motifs*
Models, Molecular*
Protein Conformation, beta-Strand*
Protein Interaction Domains and Motifs*
Protein Multimerization*
HSP40 Heat-Shock Proteins/*chemistry
Amino Acid Sequence ; HSP40 Heat-Shock Proteins/metabolism ; Kinetics ; Protein Binding ; Protein Conformation
Czasopismo naukowe
Tytuł :
Cross-Talk between Overlap Interactions in Biomolecules: A Case Study of the β -Turn Motif.
Autorzy :
Nagesh J; Solid State and Structural Chemistry Unit, Indian Institute of Science Bangalore, Bengaluru 560012, Karnataka, India.
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Źródło :
Molecules (Basel, Switzerland) [Molecules] 2021 Mar 11; Vol. 26 (6). Date of Electronic Publication: 2021 Mar 11.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Conformation, beta-Strand/*physiology
Proteins/*chemistry
Hydrogen Bonding ; Models, Molecular ; Peptides/chemistry ; Protein Conformation ; Protein Stability ; Thermodynamics
Czasopismo naukowe
Tytuł :
Structural effects of the highly protective V127 polymorphism on human prion protein.
Autorzy :
Hosszu LLP; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK.
Conners R; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK.; University of Bristol, School of Biochemistry, Biomedical Sciences Building, University Walk, Clifton, BS8 1TD, UK.; Living Systems Institute, University of Exeter, Stocker Road, Exeter, EX4 4QD, UK.
Sangar D; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK.
Batchelor M; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK.
Sawyer EB; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK.; London School of Hygiene & Tropical Medicine, Keppel Street, London, WC1E 7HT, UK.
Fisher S; Diamond Light Source, Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, UK.; ESRF, 71, Avenue des Martyrs, CS 40220, 38043, Grenoble Cedex 9, France.
Cliff MJ; Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Hounslow AM; Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
McAuley K; Diamond Light Source, Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, UK.
Leo Brady R; University of Bristol, School of Biochemistry, Biomedical Sciences Building, University Walk, Clifton, BS8 1TD, UK.
Jackson GS; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK.
Bieschke J; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK.
Waltho JP; Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.; Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Collinge J; MRC Prion Unit at UCL, UCL Institute of Prion Diseases, 33 Cleveland Street, London, W1W 7FF, UK. .
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Źródło :
Communications biology [Commun Biol] 2020 Jul 29; Vol. 3 (1), pp. 402. Date of Electronic Publication: 2020 Jul 29.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation*
Prion Diseases/*genetics
Prion Proteins/*genetics
Prions/*genetics
Animals ; Humans ; Point Mutation/genetics ; Prion Diseases/pathology ; Prion Proteins/ultrastructure ; Prions/ultrastructure ; Protein Conformation, beta-Strand/genetics
Czasopismo naukowe
Tytuł :
A comparison between internal protein nanoenvironments of α-helices and β-sheets.
Autorzy :
Mazoni I; Computational Biology Research Group, Embrapa Agricultural Informatics, Campinas, SP, Brazil.
Salim JA; Research Center on Biodiversity and Computing (BIOCOMP), Polytechnic School of the University of São Paulo (USP), São Paulo, Brazil.
de Moraes FR; Physics Department, Institute of Biosciences, Languages, and Exact Sciences (IBILCE), São Paulo State University (Unesp), Ribeirão Preto, SP, Brazil.
Borro L; IoT & AI Solutions, CPqD Foundation, Campinas, SP, Brazil.
Neshich G; Computational Biology Research Group, Embrapa Agricultural Informatics, Campinas, SP, Brazil.
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Źródło :
PloS one [PLoS One] 2020 Dec 30; Vol. 15 (12), pp. e0244315. Date of Electronic Publication: 2020 Dec 30 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation, alpha-Helical/*physiology
Protein Conformation, beta-Strand/*physiology
Protein Structure, Secondary/*physiology
Algorithms ; Animals ; Databases, Protein ; Humans ; Models, Molecular ; Protein Conformation ; Proteins/chemistry ; Software
Czasopismo naukowe
Tytuł :
Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.
Autorzy :
Wang H; Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden.
Logan DT; Department of Chemistry, Division of Biochemistry & Structural Biology, Lund University, 22100 Lund, Sweden.
Danielsson J; Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden.
Oliveberg M; Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden; .
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Nov 17; Vol. 117 (46), pp. 28775-28783. Date of Electronic Publication: 2020 Nov 04.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation, alpha-Helical/*physiology
Protein Conformation, beta-Strand/*physiology
Protein Structure, Secondary/*physiology
Crystallography, X-Ray/methods ; Hydrogen Bonding ; Kinetics ; Protein Conformation ; Protein Denaturation ; Protein Folding ; Proteins/chemistry ; Thermodynamics
Czasopismo naukowe
Tytuł :
Crystal structure of an inulosucrase from Halalkalicoccus jeotgali B3T, a halophilic archaeal strain.
Autorzy :
Ghauri K; Industrial Biotechnology Division, National Institute for Biotechnology and Genetic Engineering, Constituent College of Pakistan Institute of Engineering and Applied Sciences, Faisalabad, Pakistan.
Pijning T; Department of Biomolecular X-ray Crystallography, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands.
Munawar N; Department of Chemistry, College of Sciences, United Arab Emirates University, Al-Ain, UAE.
Ali H; Industrial Biotechnology Division, National Institute for Biotechnology and Genetic Engineering, Constituent College of Pakistan Institute of Engineering and Applied Sciences, Faisalabad, Pakistan.
Ghauri MA; Industrial Biotechnology Division, National Institute for Biotechnology and Genetic Engineering, Constituent College of Pakistan Institute of Engineering and Applied Sciences, Faisalabad, Pakistan.
Anwar MA; Industrial Biotechnology Division, National Institute for Biotechnology and Genetic Engineering, Constituent College of Pakistan Institute of Engineering and Applied Sciences, Faisalabad, Pakistan.
Wallis R; Department of Respiratory Sciences, Maurice Shock Medical Sciences Building, University of Leicester, UK.
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Źródło :
The FEBS journal [FEBS J] 2021 Oct; Vol. 288 (19), pp. 5723-5736. Date of Electronic Publication: 2021 Apr 22.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation*
Apoenzymes/*ultrastructure
Halobacteriaceae/*ultrastructure
Hexosyltransferases/*ultrastructure
Apoenzymes/chemistry ; Archaea/enzymology ; Archaea/ultrastructure ; Crystallography, X-Ray ; Halobacteriaceae/enzymology ; Hexosyltransferases/chemistry ; Protein Folding ; Sucrose/chemistry ; Trisaccharides/chemistry
SCR Organism :
Halalkalicoccus
Czasopismo naukowe
Tytuł :
Conserved residues Glu37 and Trp229 play an essential role in protein folding of β-lactamase.
Autorzy :
Chikunova A; Leiden Institute of Chemistry, Leiden University, the Netherlands.
Manley MP; Leiden Institute of Chemistry, Leiden University, the Netherlands.
Ud Din Ahmad M; Oncode Institute and Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands.
Bilman T; Leiden Institute of Chemistry, Leiden University, the Netherlands.
Perrakis A; Oncode Institute and Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands.
Ubbink M; Leiden Institute of Chemistry, Leiden University, the Netherlands.
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Źródło :
The FEBS journal [FEBS J] 2021 Oct; Vol. 288 (19), pp. 5708-5722. Date of Electronic Publication: 2021 May 02.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation*
Drug Resistance, Bacterial/*genetics
Protein Folding/*drug effects
beta-Lactamases/*genetics
Amino Acid Sequence/genetics ; Amino Acid Substitution/genetics ; Anti-Bacterial Agents/adverse effects ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/therapeutic use ; Catalytic Domain/genetics ; Conserved Sequence/genetics ; Escherichia coli/chemistry ; Escherichia coli/enzymology ; Humans ; Kinetics ; Mutagenesis, Site-Directed ; beta-Lactamases/ultrastructure
Czasopismo naukowe
Tytuł :
CryoEM structure of the super-constricted two-start dynamin 1 filament.
Autorzy :
Liu J; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.
Alvarez FJD; Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15260, USA.
Clare DK; Electron Bio-Imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK.
Noel JK; Electric Ant Lab, Amsterdam, The Netherlands.
Zhang P; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK. .; Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15260, USA. .; Electron Bio-Imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. .
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Źródło :
Nature communications [Nat Commun] 2021 Sep 13; Vol. 12 (1), pp. 5393. Date of Electronic Publication: 2021 Sep 13.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Molecular Dynamics Simulation*
Pleckstrin Homology Domains*
Protein Conformation*
Protein Multimerization*
Cryoelectron Microscopy/*methods
Dynamin I/*chemistry
Dynamin I/*ultrastructure
Algorithms ; Dynamin I/genetics ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Mutation ; Thermodynamics
Czasopismo naukowe
Tytuł :
Exploring the cytotoxic mechanisms of Pediocin PA-1 towards HeLa and HT29 cells by comparison to known bacteriocins: Microcin E492, enterocin heterodimer and Divercin V41.
Autorzy :
Buss GP; School of Life Sciences, Canterbury Christ Church University, Canterbury, United Kingdom.
Wilson CM; School of Life Sciences, Canterbury Christ Church University, Canterbury, United Kingdom.
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Źródło :
PloS one [PLoS One] 2021 Sep 02; Vol. 16 (9), pp. e0251951. Date of Electronic Publication: 2021 Sep 02 (Print Publication: 2021).
Typ publikacji :
Comparative Study; Journal Article
MeSH Terms :
Protein Conformation*
Bacteriocins/*chemistry
Bacteriocins/*pharmacology
Pediocins/*chemistry
Pediocins/*pharmacology
Amino Acid Sequence ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Apoptosis/drug effects ; Bacteriocins/genetics ; Bridged-Ring Compounds/chemistry ; Bridged-Ring Compounds/pharmacology ; COVID-19/epidemiology ; COVID-19/prevention & control ; COVID-19/virology ; Cell Survival/drug effects ; HT29 Cells ; HeLa Cells ; Humans ; Models, Molecular ; Pandemics ; Pediocins/genetics ; SARS-CoV-2/physiology ; Sequence Homology, Amino Acid ; Toll-Like Receptor 4/metabolism
Czasopismo naukowe
Tytuł :
AlphaFold2 and the future of structural biology.
Autorzy :
Cramer P; Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany. .
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Źródło :
Nature structural & molecular biology [Nat Struct Mol Biol] 2021 Sep; Vol. 28 (9), pp. 704-705.
Typ publikacji :
Letter
MeSH Terms :
Algorithms*
Deep Learning*
Protein Conformation*
Amino Acid Sequence ; Computational Biology/methods ; Internet ; Protein Folding ; Sequence Alignment ; Structure-Activity Relationship
Opinia redakcyjna
Tytuł :
Effects of Cardiolipin on the Conformational Dynamics of Membrane-Anchored Bcl-xL.
Autorzy :
Tyagi V; Department of Materials Science and Engineering, University of California, Irvine, CA 92697, USA.
Vasquez-Montes V; Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS 66160, USA.
Freites JA; Department of Chemistry, University of California, Irvine, CA 92697, USA.
Kyrychenko A; Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS 66160, USA.; Institute of Chemistry & School of Chemistry, V. N. Karazin Kharkiv National University, 4 Svobody Square, 61022 Kharkiv, Ukraine.
Tobias DJ; Department of Chemistry, University of California, Irvine, CA 92697, USA.
Ladokhin AS; Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS 66160, USA.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Aug 30; Vol. 22 (17). Date of Electronic Publication: 2021 Aug 30.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Conformation*
Cardiolipins/*metabolism
Cell Membrane/*metabolism
bcl-X Protein/*chemistry
bcl-X Protein/*metabolism
Apoptosis ; Cardiolipins/chemistry ; Humans ; Molecular Dynamics Simulation
Czasopismo naukowe
Tytuł :
Accurate prediction of protein structures and interactions using a three-track neural network.
Autorzy :
Baek M; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
DiMaio F; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Anishchenko I; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Dauparas J; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Ovchinnikov S; Faculty of Arts and Sciences, Division of Science, Harvard University, Cambridge, MA 02138, USA.; John Harvard Distinguished Science Fellowship Program, Harvard University, Cambridge, MA 02138, USA.
Lee GR; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Wang J; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Cong Q; Eugene McDermott Center for Human Growth and Development, University of Texas Southwestern Medical Center, Dallas, TX, USA.; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Kinch LN; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Schaeffer RD; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Millán C; Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.
Park H; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Adams C; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
Glassman CR; Program in Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.; Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
DeGiovanni A; Molecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Pereira JH; Molecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Rodrigues AV; Molecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
van Dijk AA; Department of Biochemistry, Focus Area Human Metabolomics, North-West University, 2531 Potchefstroom, South Africa.
Ebrecht AC; Department of Biochemistry, Focus Area Human Metabolomics, North-West University, 2531 Potchefstroom, South Africa.
Opperman DJ; Department of Biotechnology, University of the Free State, 205 Nelson Mandela Drive, Bloemfontein 9300, South Africa.
Sagmeister T; Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Buhlheller C; Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.; Medical University of Graz, Graz, Austria.
Pavkov-Keller T; Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.; BioTechMed-Graz, Graz, Austria.
Rathinaswamy MK; Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
Dalwadi U; Life Sciences Institute, Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Yip CK; Life Sciences Institute, Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Burke JE; Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
Garcia KC; Program in Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.; Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.; Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA.
Grishin NV; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Adams PD; Molecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.; Department of Bioengineering, University of California, Berkeley, Berkeley, CA 94720, USA.
Read RJ; Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.
Baker D; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. .; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
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Źródło :
Science (New York, N.Y.) [Science] 2021 Aug 20; Vol. 373 (6557), pp. 871-876. Date of Electronic Publication: 2021 Jul 15.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Deep Learning*
Protein Conformation*
Protein Folding*
Proteins/*chemistry
ADAM Proteins/chemistry ; Amino Acid Sequence ; Computer Simulation ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Databases, Protein ; Membrane Proteins/chemistry ; Models, Molecular ; Multiprotein Complexes/chemistry ; Neural Networks, Computer ; Protein Subunits/chemistry ; Proteins/physiology ; Receptors, G-Protein-Coupled/chemistry ; Sphingosine N-Acyltransferase/chemistry
Czasopismo naukowe
Tytuł :
Molecular basis for recognition of Gly/N-degrons by CRL2 .
Autorzy :
Yan X; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Li Y; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Wang G; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Zhou Z; Department of Immunology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Key Laboratory of Cellular and Molecular Immunology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Song G; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Feng Q; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Zhao Y; Department of Immunology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Key Laboratory of Cellular and Molecular Immunology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Mi W; Department of Immunology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Key Laboratory of Cellular and Molecular Immunology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Ma Z; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China.
Dong C; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China. Electronic address: .
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Źródło :
Molecular cell [Mol Cell] 2021 Aug 19; Vol. 81 (16), pp. 3262-3274.e3. Date of Electronic Publication: 2021 Jul 01.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation*
Cell Cycle Proteins/*ultrastructure
Glycine/*chemistry
Receptors, Cytokine/*ultrastructure
Amino Acid Sequence/genetics ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Crystallography, X-Ray ; Glycine/genetics ; HEK293 Cells ; Humans ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/ultrastructure ; Protein Binding/genetics ; Protein Domains/genetics ; Proteolysis ; Receptors, Cytokine/chemistry ; Receptors, Cytokine/genetics ; Substrate Specificity ; Ubiquitin/genetics
Czasopismo naukowe
Tytuł :
PYTHIA: Deep Learning Approach for Local Protein Conformation Prediction.
Autorzy :
Cretin G; Biologie Intégrée du Globule Rouge, Université de Paris, UMR_S1134, BIGR, INSERM, 75015 Paris, France.; Laboratoire d'Excellence GR-Ex, 75015 Paris, France.
Galochkina T; Biologie Intégrée du Globule Rouge, Université de Paris, UMR_S1134, BIGR, INSERM, 75015 Paris, France.; Laboratoire d'Excellence GR-Ex, 75015 Paris, France.
de Brevern AG; Biologie Intégrée du Globule Rouge, Université de Paris, UMR_S1134, BIGR, INSERM, 75015 Paris, France.; Laboratoire d'Excellence GR-Ex, 75015 Paris, France.
Gelly JC; Biologie Intégrée du Globule Rouge, Université de Paris, UMR_S1134, BIGR, INSERM, 75015 Paris, France.; Laboratoire d'Excellence GR-Ex, 75015 Paris, France.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Aug 17; Vol. 22 (16). Date of Electronic Publication: 2021 Aug 17.
Typ publikacji :
Journal Article
MeSH Terms :
Algorithms*
Deep Learning*
Neural Networks, Computer*
Protein Conformation*
Software*
Proteins/*chemistry
Sequence Analysis, Protein/*methods
Databases, Protein ; Humans ; Models, Molecular
Czasopismo naukowe
Tytuł :
The Crystal Structure of the Ca -ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation.
Autorzy :
Hansen SB; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Dyla M; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Neumann C; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Quistgaard EMH; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Andersen JL; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Kjaergaard M; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark; Aarhus Institute of Advanced Studies (AIAS), Denmark; The Danish National Research Foundation Center for Proteins in Memory (PROMEMO), Denmark.
Nissen P; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark; The Danish National Research Foundation Center for Proteins in Memory (PROMEMO), Denmark. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Aug 06; Vol. 433 (16), pp. 167015. Date of Electronic Publication: 2021 Apr 30.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Models, Molecular*
Protein Binding*
Protein Conformation*
Structure-Activity Relationship*
Listeria monocytogenes/*enzymology
Sarcoplasmic Reticulum Calcium-Transporting ATPases/*chemistry
Sarcoplasmic Reticulum Calcium-Transporting ATPases/*metabolism
Calcium/chemistry ; Calcium/metabolism ; Crystallography, X-Ray ; Phosphorylation
Czasopismo naukowe

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