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Wyszukujesz frazę ""Protein Interaction Domains and Motifs"" wg kryterium: Temat


Tytuł:
Analysis of the SNARE Stx8 recycling reveals that the retromer-sorting motif has undergone evolutionary divergence.
Autorzy:
Yanguas F; Departamento de Microbiología y Genética, Universidad de Salamanca. Salamanca. Spain.; Instituto de Biología Funcional y Genómica (IBFG), Consejo Superior de Investigaciones Científicas (CSIC). Salamanca. Spain.
Valdivieso MH; Departamento de Microbiología y Genética, Universidad de Salamanca. Salamanca. Spain.; Instituto de Biología Funcional y Genómica (IBFG), Consejo Superior de Investigaciones Científicas (CSIC). Salamanca. Spain.
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Źródło:
PLoS genetics [PLoS Genet] 2021 Mar 31; Vol. 17 (3), pp. e1009463. Date of Electronic Publication: 2021 Mar 31 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Amino Acid Motifs*
Evolution, Molecular*
Protein Interaction Domains and Motifs*
SNARE Proteins/*genetics
SNARE Proteins/*metabolism
Amino Acid Sequence ; Endosomes/metabolism ; Fungal Proteins ; Humans ; Protein Binding ; Protein Transport ; SNARE Proteins/chemistry ; Salt Stress ; Salt Tolerance/genetics ; Vesicular Transport Proteins/metabolism
Czasopismo naukowe
Tytuł:
A cohesin cancer mutation reveals a role for the hinge domain in genome organization and gene expression.
Autorzy:
Carico ZM; Cancer Epigenetics Training Program, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Integrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
Stefan HC; Integrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
Justice M; Integrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
Yimit A; Integrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
Dowen JM; Cancer Epigenetics Training Program, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Integrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
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Źródło:
PLoS genetics [PLoS Genet] 2021 Mar 24; Vol. 17 (3), pp. e1009435. Date of Electronic Publication: 2021 Mar 24 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms:
Gene Expression Regulation, Neoplastic*
Mutation*
Protein Interaction Domains and Motifs*
Cell Cycle Proteins/*genetics
Chromosomal Proteins, Non-Histone/*genetics
Neoplasms/*genetics
Animals ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/metabolism ; Embryonic Stem Cells/metabolism ; Enhancer Elements, Genetic ; Gene Expression Profiling ; Histones ; Mice ; Neoplasms/metabolism ; Promoter Regions, Genetic ; Protein Binding ; Cohesins
Czasopismo naukowe
Tytuł:
Structure-function analysis of fission yeast cleavage and polyadenylation factor (CPF) subunit Ppn1 and its interactions with Dis2 and Swd22.
Autorzy:
Benjamin B; Molecular Biology Program, Sloan-Kettering Institute, New York, New York, United States of America.; Gerstner Sloan Kettering Graduate School of Biomedical Sciences, New York, New York, United States of America.
Sanchez AM; Molecular Biology Program, Sloan-Kettering Institute, New York, New York, United States of America.; Gerstner Sloan Kettering Graduate School of Biomedical Sciences, New York, New York, United States of America.
Garg A; Molecular Biology Program, Sloan-Kettering Institute, New York, New York, United States of America.
Schwer B; Dept. of Microbiology and Immunology, Weill Cornell Medical College, New York, New York, United States of America.
Shuman S; Molecular Biology Program, Sloan-Kettering Institute, New York, New York, United States of America.
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Źródło:
PLoS genetics [PLoS Genet] 2021 Mar 12; Vol. 17 (3), pp. e1009452. Date of Electronic Publication: 2021 Mar 12 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms:
Protein Interaction Domains and Motifs*
Acid Anhydride Hydrolases/*metabolism
Protein Phosphatase 1/*metabolism
Schizosaccharomyces/*physiology
mRNA Cleavage and Polyadenylation Factors/*metabolism
Alleles ; Amino Acid Sequence ; Computational Biology/methods ; Gene Expression Profiling ; Gene Expression Regulation, Fungal ; Models, Biological ; Mutation ; Phenotype ; Phosphorylation ; Transcription, Genetic ; Transcriptome ; mRNA Cleavage and Polyadenylation Factors/chemistry
Czasopismo naukowe
Tytuł:
A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols.
Autorzy:
Yan R; Westlake Laboratory of Life Sciences and Biomedicine, Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou 310024, Zhejiang Province, China.; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou 310024, Zhejiang Province, China.
Cao P; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Song W; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Qian H; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Du X; School of Biotechnology and Biomolecular Science, University of New South Wales, Sydney, NSW 2052, Australia.
Coates HW; School of Biotechnology and Biomolecular Science, University of New South Wales, Sydney, NSW 2052, Australia.
Zhao X; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Li Y; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Gao S; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Gong X; Department of Biology, Southern University of Science and Technology, Shenzhen, Guangdong 518055, China.
Liu X; National Institute of Biological Sciences (NIBS), Beijing 102206, China.
Sui J; National Institute of Biological Sciences (NIBS), Beijing 102206, China.; Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing 102206, China.
Lei J; Technology Center for Protein Sciences, Ministry of Education Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Yang H; School of Biotechnology and Biomolecular Science, University of New South Wales, Sydney, NSW 2052, Australia.
Brown AJ; School of Biotechnology and Biomolecular Science, University of New South Wales, Sydney, NSW 2052, Australia.
Zhou Q; Westlake Laboratory of Life Sciences and Biomedicine, Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou 310024, Zhejiang Province, China.; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou 310024, Zhejiang Province, China.
Yan C; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. .
Yan N; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. .
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Źródło:
Science (New York, N.Y.) [Science] 2021 Mar 05; Vol. 371 (6533). Date of Electronic Publication: 2021 Jan 14.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Interaction Domains and Motifs*
Hydroxycholesterols/*chemistry
Intracellular Signaling Peptides and Proteins/*chemistry
Membrane Proteins/*chemistry
Cryoelectron Microscopy ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Membrane Proteins/genetics ; Mutation
Czasopismo naukowe
Tytuł:
Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding.
Autorzy:
Buchholz I; Institute of Biochemistry, University of Greifswald, Greifswald, Germany.; ZIK HIKE, University of Greifswald, Greifswald, Germany.
McDonnell T; Division of Biochemical Engineering, Bernard Katz Institute, University College London, London, UK.
Nestler P; Institute of Physics, University of Greifswald, Greifswald, Germany.
Tharad S; Institute for Biophysics, University of Natural Resources and Life Sciences Vienna, Vienna, Austria.
Kulke M; Institute of Biochemistry, University of Greifswald, Greifswald, Germany.
Radziszewska A; Centre for Adolescent Rheumatology Versus Arthritis at UCL, UCLH, GOSH, London, UK.; Division of Medicine, Centre for Rheumatology, University College London, London, UK.
Ripoll VM; Division of Medicine, Centre for Rheumatology, University College London, London, UK.
Schmidt F; Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, Greifswald, Germany.; Proteomics Core, Weill Cornell Medicine-Qatar, Doha, Qatar.
Hammer E; Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, Greifswald, Germany.; DZHK (German Centre for Cardiovascular Research), Partner Site Greifswald, Greifswald, Germany.
Toca-Herrera JL; Institute for Biophysics, University of Natural Resources and Life Sciences Vienna, Vienna, Austria.
Rahman A; Division of Medicine, Centre for Rheumatology, University College London, London, UK. .
Delcea M; Institute of Biochemistry, University of Greifswald, Greifswald, Germany. .; ZIK HIKE, University of Greifswald, Greifswald, Germany. .; DZHK (German Centre for Cardiovascular Research), Partner Site Greifswald, Greifswald, Germany. .
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Źródło:
Scientific reports [Sci Rep] 2021 Feb 25; Vol. 11 (1), pp. 4542. Date of Electronic Publication: 2021 Feb 25.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Conformation*
Protein Folding*
Protein Interaction Domains and Motifs*
Autoantibodies/*chemistry
beta 2-Glycoprotein I/*chemistry
Autoantibodies/immunology ; Cysteine/chemistry ; Cysteine/metabolism ; Disulfides/chemistry ; Immunoglobulin G/chemistry ; Immunoglobulin G/immunology ; Microscopy, Atomic Force ; Models, Molecular ; Protein Binding/immunology ; Structure-Activity Relationship ; beta 2-Glycoprotein I/immunology ; beta 2-Glycoprotein I/metabolism
Czasopismo naukowe
Tytuł:
The analysis on the human protein domain targets and host-like interacting motifs for the MERS-CoV and SARS-CoV/CoV-2 infers the molecular mimicry of coronavirus.
Autorzy:
Martínez YA; Unidad de Investigación Biomédica de Zacatecas, Instituto Mexicano Del Seguro Social, Zacatecas, México.; Laboratorio de Inmunología y Biología Celular y Molecular, Facultad de Ciencias Químicas, Universidad Autónoma de San Luis Potosí, San Luis Potosí, México.
Guo X; Laboratorio de Biotecnología Genómica, Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Reynosa, México.
Portales-Pérez DP; Laboratorio de Inmunología y Biología Celular y Molecular, Facultad de Ciencias Químicas, Universidad Autónoma de San Luis Potosí, San Luis Potosí, México.
Rivera G; Laboratorio de Biotecnología Farmacéutica, Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Reynosa, México.
Castañeda-Delgado JE; Unidad de Investigación Biomédica de Zacatecas, Instituto Mexicano Del Seguro Social, Zacatecas, México.; Cátedras-CONACYT, Unidad de Investigación Biomédica de Zacatecas, Instituto Mexicano Del Seguro Social, Zacatecas, México.
García-Pérez CA; Information and Communication Technology Department (ICT), Complex Systems, Helmholtz Zentrum München, Neuherberg, Germany.
Enciso-Moreno JA; Unidad de Investigación Biomédica de Zacatecas, Instituto Mexicano Del Seguro Social, Zacatecas, México.
Lara-Ramírez EE; Unidad de Investigación Biomédica de Zacatecas, Instituto Mexicano Del Seguro Social, Zacatecas, México.
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Źródło:
PloS one [PLoS One] 2021 Feb 17; Vol. 16 (2), pp. e0246901. Date of Electronic Publication: 2021 Feb 17 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Betacoronavirus/*metabolism
Coronavirus Infections/*metabolism
Coronavirus Infections/*virology
Molecular Mimicry/*physiology
Protein Interaction Domains and Motifs/*immunology
Betacoronavirus/genetics ; COVID-19/metabolism ; COVID-19/virology ; Coronavirus Infections/genetics ; Databases, Genetic ; Host-Pathogen Interactions ; Humans ; Middle East Respiratory Syndrome Coronavirus/genetics ; Middle East Respiratory Syndrome Coronavirus/metabolism ; Protein Domains ; Protein Interaction Domains and Motifs/genetics ; Proteome ; Severe acute respiratory syndrome-related coronavirus/genetics ; Severe acute respiratory syndrome-related coronavirus/metabolism ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; Viral Proteins/metabolism
Czasopismo naukowe
Tytuł:
Biased Brownian Motion of KIF1A and the Role of Tubulin's C-Terminal Tail Studied by Molecular Dynamics Simulation.
Autorzy:
Mizuhara Y; Department of Pure and Applied Physics, Waseda University, Okubo 3-4-1, Sinjuku-Ku, Tokyo 169-8555, Japan.
Takano M; Department of Pure and Applied Physics, Waseda University, Okubo 3-4-1, Sinjuku-Ku, Tokyo 169-8555, Japan.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Feb 04; Vol. 22 (4). Date of Electronic Publication: 2021 Feb 04.
Typ publikacji:
Journal Article
MeSH Terms:
Biophysical Phenomena*
Molecular Docking Simulation*
Molecular Dynamics Simulation*
Protein Interaction Domains and Motifs*
Kinesins/*chemistry
Tubulin/*chemistry
Algorithms ; Axonal Transport ; Kinesins/metabolism ; Microtubules/chemistry ; Microtubules/metabolism ; Models, Theoretical ; Neurons/metabolism ; Protein Binding ; Tubulin/metabolism
Czasopismo naukowe
Tytuł:
Pneumoviral Phosphoprotein, a Multidomain Adaptor-Like Protein of Apparent Low Structural Complexity and High Conformational Versatility.
Autorzy:
Cardone C; CNRS, Université Paris-Saclay, Institut de Chimie des Substances Naturelles, 91198 Gif-sur-Yvette, France.
Caseau CM; CNRS, Université Paris-Saclay, Institut de Chimie des Substances Naturelles, 91198 Gif-sur-Yvette, France.
Pereira N; CNRS, Université Paris-Saclay, Institut de Chimie des Substances Naturelles, 91198 Gif-sur-Yvette, France.
Sizun C; CNRS, Université Paris-Saclay, Institut de Chimie des Substances Naturelles, 91198 Gif-sur-Yvette, France.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Feb 03; Vol. 22 (4). Date of Electronic Publication: 2021 Feb 03.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Models, Molecular*
Protein Conformation*
Protein Interaction Domains and Motifs*
Phosphoproteins/*chemistry
Phosphoproteins/*metabolism
Pneumovirus/*metabolism
Viral Proteins/*chemistry
Viral Proteins/*metabolism
Amino Acid Sequence ; Animals ; Binding Sites ; Gene Expression Regulation, Viral ; Humans ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Mononegavirales ; Phosphoproteins/genetics ; Pneumovirus/genetics ; Protein Binding ; Protein Folding ; Respiratory Syncytial Virus, Human ; Structure-Activity Relationship ; Viral Proteins/genetics
Czasopismo naukowe
Tytuł:
The Full Region of N-Terminal in Polymerase of IBDV Plays an Important Role in Viral Replication and Pathogenicity: Either Partial Region or Single Amino Acid V4I Substitution Does Not Completely Lead to the Virus Attenuation to Three-Yellow Chickens.
Autorzy:
Wang W; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Huang Y; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Ji Z; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Chen G; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Zhang Y; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Qiao Y; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Shi M; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Li M; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Huang T; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Wei T; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
Mo M; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
He X; School of Marine Sciences and Biotechnology, Guangxi University for Nationalities, Nanning 530006, China.; Guangxi Key Laboratory Cultivation Base for Polysaccharide Materials and Modifications, Guangxi University for Nationalities, Nanning 530006, China.
Wei P; Institute for Poultry Science and Health, Guangxi University, Nanning 530005, China.
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Źródło:
Viruses [Viruses] 2021 Jan 14; Vol. 13 (1). Date of Electronic Publication: 2021 Jan 14.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Interaction Domains and Motifs*
Virus Replication*/genetics
Birnaviridae Infections/*veterinary
DNA-Directed RNA Polymerases/*metabolism
Infectious bursal disease virus/*physiology
Poultry Diseases/*virology
Amino Acid Substitution ; Animals ; Cells, Cultured ; Chick Embryo ; Cloning, Molecular ; DNA-Directed RNA Polymerases/chemistry ; Fibroblasts ; Genome, Viral ; Infectious bursal disease virus/pathogenicity ; Mutation ; Protein Binding ; Reverse Genetics ; Viral Structural Proteins/chemistry ; Viral Structural Proteins/metabolism ; Virulence
Czasopismo naukowe
Tytuł:
Evolution of ribosomal protein network architectures.
Autorzy:
Timsit Y; Mediterranean Institute of Oceanography UM 110, Aix-Marseille Université, CNRS, IRD, Campus de Luminy, Marseille, France. .
Sergeant-Perthuis G; Institut de Mathématiques de Jussieu - Paris Rive Gauche (IMJ-PRG), UMR 7586, CNRS, Université Paris Diderot, Paris, France.
Bennequin D; Institut de Mathématiques de Jussieu - Paris Rive Gauche (IMJ-PRG), UMR 7586, CNRS, Université Paris Diderot, Paris, France.
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Źródło:
Scientific reports [Sci Rep] 2021 Jan 12; Vol. 11 (1), pp. 625. Date of Electronic Publication: 2021 Jan 12.
Typ publikacji:
Journal Article
MeSH Terms:
Evolution, Molecular*
Protein Biosynthesis*
Protein Interaction Domains and Motifs*
RNA, Transfer/*metabolism
Ribosomal Proteins/*chemistry
Ribosomal Proteins/*metabolism
Ribosomes/*metabolism
Binding Sites ; Humans ; Models, Molecular ; Phylogeny ; Protein Conformation ; RNA, Transfer/chemistry
Czasopismo naukowe
Tytuł:
The Cryogenic Electron Microscopy Structure of the Cell Adhesion Regulator Metavinculin Reveals an Isoform-Specific Kinked Helix in Its Cytoskeleton Binding Domain.
Autorzy:
Rangarajan ES; Cell Adhesion Laboratory, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Izard T; Cell Adhesion Laboratory, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL 33458, USA.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Jan 11; Vol. 22 (2). Date of Electronic Publication: 2021 Jan 11.
Typ publikacji:
Journal Article
MeSH Terms:
Cryoelectron Microscopy*
Protein Interaction Domains and Motifs*
Cytoskeleton/*chemistry
Vinculin/*chemistry
Actins/chemistry ; Actins/metabolism ; Cell Adhesion ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Cytoskeleton/metabolism ; Humans ; Models, Molecular ; Peptides ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; Vinculin/metabolism
Czasopismo naukowe
Tytuł:
Catalytic activity of human guanylate-binding protein 1 coupled to the release of structural restraints imposed by the C-terminal domain.
Autorzy:
Ince S; Physical Chemistry I, Ruhr-University, Bochum, Germany.
Zhang P; Physical Chemistry I, Ruhr-University, Bochum, Germany.
Kutsch M; Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC, USA.
Krenczyk O; Physical Chemistry I, Ruhr-University, Bochum, Germany.
Shydlovskyi S; Physical Chemistry I, Ruhr-University, Bochum, Germany.
Herrmann C; Physical Chemistry I, Ruhr-University, Bochum, Germany.
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Źródło:
The FEBS journal [FEBS J] 2021 Jan; Vol. 288 (2), pp. 582-599. Date of Electronic Publication: 2020 May 19.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Interaction Domains and Motifs*
GTP-Binding Proteins/*chemistry
Guanosine Diphosphate/*chemistry
Guanosine Triphosphate/*chemistry
Binding Sites ; Biocatalysis ; Cloning, Molecular ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/chemistry ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Kinetics ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Multimerization ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Substrate Specificity
Czasopismo naukowe
Tytuł:
Large Multidomain Protein NMR: HIV-1 Reverse Transcriptase Precursor in Solution.
Autorzy:
Ilina TV; Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Xi Z; Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Brosenitsch T; Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Sluis-Cremer N; Department of Medicine, Division of Infectious Diseases, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA.
Ishima R; Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2020 Dec 15; Vol. 21 (24). Date of Electronic Publication: 2020 Dec 15.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Magnetic Resonance Spectroscopy*
Protein Interaction Domains and Motifs*
HIV Reverse Transcriptase/*chemistry
HIV-1/*enzymology
Binding Sites ; HIV Infections/microbiology ; HIV Reverse Transcriptase/metabolism ; Humans ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Multimerization ; Solubility ; Solutions
Czasopismo naukowe
Tytuł:
Identification of the Cleavage Domain within Glycoprotein G of Herpes Simplex Virus Type 2.
Autorzy:
Kropp KA; Institute of Virology, Hannover Medical School, 30625 Hannover, Germany.
Srivaratharajan S; Institute of Virology, Hannover Medical School, 30625 Hannover, Germany.
Ritter B; Institute of Virology, Hannover Medical School, 30625 Hannover, Germany.
Yu P; Institute of Virology, Hannover Medical School, 30625 Hannover, Germany.
Krooss S; Institute of Virology, Hannover Medical School, 30625 Hannover, Germany.; Department of Gastroenterology, Hepatology and Endocrinology, Hannover Medical School, 30625 Hannover, Germany.
Polten F; Core Facility Proteomics, Hannover Medical School, 30625 Hannover, Germany.
Pich A; Core Facility Proteomics, Hannover Medical School, 30625 Hannover, Germany.; Institute for Toxicology, Hannover Medical School, 30625 Hannover, Germany.
Alcami A; Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, 28049 Madrid, Spain.
Viejo-Borbolla A; Institute of Virology, Hannover Medical School, 30625 Hannover, Germany.
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Źródło:
Viruses [Viruses] 2020 Dec 12; Vol. 12 (12). Date of Electronic Publication: 2020 Dec 12.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Interaction Domains and Motifs*
Herpes Simplex/*virology
Herpesvirus 2, Human/*physiology
Viral Envelope Proteins/*metabolism
Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Line ; Chromatography, Liquid ; Gene Expression ; Genes, Reporter ; Humans ; Mass Spectrometry ; Proteolysis
Czasopismo naukowe
Tytuł:
Novel NMR Assignment Strategy Reveals Structural Heterogeneity in Solution of the nsP3 HVD Domain of Venezuelan Equine Encephalitis Virus.
Autorzy:
Agback P; Department of Molecular Sciences, Swedish University of Agricultural Sciences, P.O. Box 7015, SE-750 07 Uppsala, Sweden.
Shernyukov A; Department of Molecular Sciences, Swedish University of Agricultural Sciences, P.O. Box 7015, SE-750 07 Uppsala, Sweden.; Laboratory of Magnetic Radiospectroscopy, N.N. Vorozhtsov Institute of Organic Chemistry, SB RAS, 630090 Novosibirsk, Russia.
Dominguez F; Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294-2170, USA.
Agback T; Department of Molecular Sciences, Swedish University of Agricultural Sciences, P.O. Box 7015, SE-750 07 Uppsala, Sweden.
Frolova EI; Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294-2170, USA.
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Źródło:
Molecules (Basel, Switzerland) [Molecules] 2020 Dec 10; Vol. 25 (24). Date of Electronic Publication: 2020 Dec 10.
Typ publikacji:
Journal Article
MeSH Terms:
Magnetic Resonance Spectroscopy*
Protein Interaction Domains and Motifs*
Encephalitis Virus, Venezuelan Equine/*enzymology
Viral Nonstructural Proteins/*chemistry
Amino Acid Sequence ; Animals ; Chemical Fractionation ; Intrinsically Disordered Proteins/chemistry ; Protein Binding ; Solubility ; Structure-Activity Relationship ; Viral Nonstructural Proteins/isolation & purification
Czasopismo naukowe
Tytuł:
Involvement of NEK2 and its interaction with NDC80 and CEP250 in hepatocellular carcinoma.
Autorzy:
Zeng L; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.; Xi'an Medical University, Xi'an, 710021, Shaanxi Province, People's Republic of China.
Fan X; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.
Wang X; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.
Deng H; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.
Zhang X; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.
Zhang K; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.
He S; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.; Xi'an Medical University, Xi'an, 710021, Shaanxi Province, People's Republic of China.
Li N; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.
Han Q; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China.
Liu Z; Department of Infectious Diseases, First Affiliated Hospital of Xi'an Jiaotong University, No. 277 Yanta West Road, Xi'an, 710061, Shaanxi Province, People's Republic of China. .
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Źródło:
BMC medical genomics [BMC Med Genomics] 2020 Oct 27; Vol. 13 (1), pp. 158. Date of Electronic Publication: 2020 Oct 27.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Interaction Domains and Motifs*
Autoantigens/*metabolism
Biomarkers, Tumor/*metabolism
Carcinoma, Hepatocellular/*metabolism
Carcinoma, Hepatocellular/*pathology
Cell Cycle Proteins/*metabolism
Cytoskeletal Proteins/*metabolism
NIMA-Related Kinases/*metabolism
Autoantigens/genetics ; Biomarkers, Tumor/genetics ; Carcinoma, Hepatocellular/genetics ; Case-Control Studies ; Cell Cycle Proteins/genetics ; Cytoskeletal Proteins/genetics ; Female ; Follow-Up Studies ; Gene Expression Regulation, Neoplastic ; Humans ; Liver Neoplasms/genetics ; Liver Neoplasms/metabolism ; Liver Neoplasms/pathology ; Male ; NIMA-Related Kinases/genetics ; Prognosis ; Survival Rate
Czasopismo naukowe
Tytuł:
Antibodies exhibit multiple paratope states influencing V H -V L domain orientations.
Autorzy:
Fernández-Quintero ML; Institute of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80-82, A-6020, Innsbruck, Austria.
Pomarici ND; Institute of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80-82, A-6020, Innsbruck, Austria.
Math BA; Institute of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80-82, A-6020, Innsbruck, Austria.
Kroell KB; Institute of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80-82, A-6020, Innsbruck, Austria.
Waibl F; Institute of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80-82, A-6020, Innsbruck, Austria.
Bujotzek A; Roche Pharma Research and Early Development, Large Molecule Research, Roche Innovation Center Munich, Penzberg, Germany.
Georges G; Roche Pharma Research and Early Development, Large Molecule Research, Roche Innovation Center Munich, Penzberg, Germany.
Liedl KR; Institute of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80-82, A-6020, Innsbruck, Austria. .
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Źródło:
Communications biology [Commun Biol] 2020 Oct 20; Vol. 3 (1), pp. 589. Date of Electronic Publication: 2020 Oct 20.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Binding Sites, Antibody*
Protein Interaction Domains and Motifs*
Antibodies/*chemistry
Immunoglobulin Heavy Chains/*chemistry
Immunoglobulin Light Chains/*chemistry
Immunoglobulin Variable Region/*chemistry
Antibodies/immunology ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Fab Fragments/immunology ; Immunoglobulin Heavy Chains/immunology ; Immunoglobulin Light Chains/immunology ; Immunoglobulin Variable Region/immunology ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation
Czasopismo naukowe
Tytuł:
All-Atomic Molecular Dynamic Studies of Human and Drosophila CDK8: Insights into Their Kinase Domains, the LXXLL Motifs, and Drug Binding Site.
Autorzy:
Xu W; Department of Chemistry, University of Louisiana at Lafayette, P.O. Box 44370, Lafayette, LA 70504, USA.
Xie XJ; Department of Molecular and Cellular Medicine, College of Medicine, Texas A&M University Health Science Center, 8447 Riverside Parkway, Bryan, TX 77807, USA.
Faust AK; Department of Chemistry, University of Louisiana at Lafayette, P.O. Box 44370, Lafayette, LA 70504, USA.
Liu M; Department of Molecular and Cellular Medicine, College of Medicine, Texas A&M University Health Science Center, 8447 Riverside Parkway, Bryan, TX 77807, USA.
Li X; Department of Molecular and Cellular Medicine, College of Medicine, Texas A&M University Health Science Center, 8447 Riverside Parkway, Bryan, TX 77807, USA.
Chen F; High Performance Computing, 329 Frey Computing Services Center, Louisiana State University, Baton Rouge, LA 70803, USA.
Naquin AA; Department of Chemistry, University of Louisiana at Lafayette, P.O. Box 44370, Lafayette, LA 70504, USA.
Walton AC; Department of Chemistry, University of Louisiana at Lafayette, P.O. Box 44370, Lafayette, LA 70504, USA.
Kishbaugh PW; Department of Chemistry, University of Louisiana at Lafayette, P.O. Box 44370, Lafayette, LA 70504, USA.
Ji JY; Department of Molecular and Cellular Medicine, College of Medicine, Texas A&M University Health Science Center, 8447 Riverside Parkway, Bryan, TX 77807, USA.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2020 Oct 12; Vol. 21 (20). Date of Electronic Publication: 2020 Oct 12.
Typ publikacji:
Journal Article
MeSH Terms:
Amino Acid Motifs*
Binding Sites*
Models, Molecular*
Protein Interaction Domains and Motifs*
Cyclin-Dependent Kinase 8/*chemistry
Drosophila Proteins/*chemistry
Protein Kinase Inhibitors/*chemistry
Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cyclin-Dependent Kinase 8/antagonists & inhibitors ; Drosophila Proteins/antagonists & inhibitors ; Humans ; Hydrogen Bonding ; Ligands ; Molecular Conformation ; Mutation ; Protein Binding ; Protein Kinase Inhibitors/pharmacology ; Species Specificity ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł:
Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases.
Autorzy:
Lai CH; Institute of Bioinformatics and Structural Biology, Department of Life Science, National Tsing Hua University, Hsinchu 30013, Taiwan.
Chang CC; Institute of Bioinformatics and Structural Biology, Department of Life Science, National Tsing Hua University, Hsinchu 30013, Taiwan.
Chuang HC; Immunology Research Center, National Health Research Institutes, Zhunan 35053, Taiwan.
Tan TH; Immunology Research Center, National Health Research Institutes, Zhunan 35053, Taiwan.
Lyu PC; Institute of Bioinformatics and Structural Biology, Department of Life Science, National Tsing Hua University, Hsinchu 30013, Taiwan.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2020 Oct 12; Vol. 21 (20). Date of Electronic Publication: 2020 Oct 12.
Typ publikacji:
Journal Article
MeSH Terms:
Binding Sites*
Catalytic Domain*
Models, Molecular*
Protein Interaction Domains and Motifs*
Dual-Specificity Phosphatases/*chemistry
Mitogen-Activated Protein Kinase Phosphatases/*chemistry
Protein Tyrosine Phosphatases/*chemistry
Amino Acid Sequence ; Amino Acids ; Conserved Sequence ; Dual-Specificity Phosphatases/genetics ; Dual-Specificity Phosphatases/metabolism ; Humans ; Hydrogen Bonding ; Mitogen-Activated Protein Kinase Phosphatases/genetics ; Mitogen-Activated Protein Kinase Phosphatases/metabolism ; Mutation ; Protein Binding ; Protein Conformation ; Protein Tyrosine Phosphatases/genetics ; Protein Tyrosine Phosphatases/metabolism
Czasopismo naukowe
Tytuł:
A new soaking procedure for X-ray crystallographic structural determination of protein-peptide complexes.
Autorzy:
Ballone A; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.
Lau RA; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.
Zweipfenning FPA; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.
Ottmann C; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.
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Źródło:
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2020 Oct 01; Vol. 76 (Pt 10), pp. 501-507. Date of Electronic Publication: 2020 Sep 15.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Interaction Domains and Motifs*
14-3-3 Proteins/*chemistry
14-3-3 Proteins/*metabolism
Exoribonucleases/*chemistry
Exoribonucleases/*metabolism
Peptide Fragments/*chemistry
Peptide Fragments/*metabolism
Crystallization ; Crystallography, X-Ray ; Humans ; Protein Conformation
Czasopismo naukowe

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