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


Tytuł :
Acidic pH-Induced Conformational Changes in Chikungunya Virus Fusion Protein E1: a Spring-Twisted Region in the Domain I-III Linker Acts as a Hinge Point for Swiveling Motion of Domains.
Autorzy :
Sahoo B; School of Biological Sciences, National Institute of Science Education and Research (NISER), Homi Bhabha National Institute (HBNI), Bhubaneswar, India.
Gudigamolla NK; School of Biological Sciences, National Institute of Science Education and Research (NISER), Homi Bhabha National Institute (HBNI), Bhubaneswar, India.
Chowdary TK; School of Biological Sciences, National Institute of Science Education and Research (NISER), Homi Bhabha National Institute (HBNI), Bhubaneswar, India .
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Źródło :
Journal of virology [J Virol] 2020 Nov 09; Vol. 94 (23). Date of Electronic Publication: 2020 Nov 09 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Chikungunya virus/*metabolism
Viral Fusion Proteins/*chemistry
Viral Fusion Proteins/*metabolism
Chikungunya Fever/virology ; Chikungunya virus/genetics ; Endocytosis ; Hydrogen-Ion Concentration ; Membrane Fusion ; Membrane Glycoproteins/chemistry ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/metabolism ; Viral Fusion Proteins/genetics ; Virus Internalization
Czasopismo naukowe
Tytuł :
Regulation of single-cell genome organization into TADs and chromatin nanodomains.
Autorzy :
Szabo Q; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France.
Donjon A; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France.
Jerković I; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France.
Papadopoulos GL; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France.
Cheutin T; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France.
Bonev B; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France.; Helmholtz Pioneer Campus, Helmholtz Zentrum München, Neuherberg, Germany.
Nora EP; Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA, USA.
Bruneau BG; Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA, USA.; Gladstone Institutes, San Francisco, CA, USA.; Department of Pediatrics, University of California, San Francisco, San Francisco, CA, USA.
Bantignies F; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France. .
Cavalli G; Institute of Human Genetics, Centre National de la Recherche Scientifique, University of Montpellier, Montpellier, France. .
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Źródło :
Nature genetics [Nat Genet] 2020 Nov; Vol. 52 (11), pp. 1151-1157. Date of Electronic Publication: 2020 Oct 19.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Chromatin/*chemistry
Embryonic Stem Cells/*ultrastructure
Animals ; Cell Differentiation/genetics ; Cell Line ; Chromosome Painting ; Drosophila/genetics ; In Situ Hybridization, Fluorescence ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Conformation ; Nanostructures ; Nuclear Microscopy
Czasopismo naukowe
Tytuł :
Bacillus thuringiensis Cry1Ab Domain III β-22 Mutants with Enhanced Toxicity to Spodoptera frugiperda (J. E. Smith).
Autorzy :
Gómez I; Instituto de Biotecnología, Universidad Nacional Autónoma de Mexico, Cuernavaca, Morelos, México.
Ocelotl J; Instituto de Biotecnología, Universidad Nacional Autónoma de Mexico, Cuernavaca, Morelos, México.
Sánchez J; Instituto de Biotecnología, Universidad Nacional Autónoma de Mexico, Cuernavaca, Morelos, México.
Aguilar-Medel S; Centro Universitario UAEMex Tenancingo de la Universidad Autónoma del Estado de Mexico, Tenancingo, México.
Peña-Chora G; Centro de Investigaciones Biológicas, Universidad Autónoma del Estado de Morelos, Cuernavaca, Morelos, México.
Lina-Garcia L; Centro de Investigaciones en Biotecnología, Universidad Autónoma del Estado de Morelos, Cuernavaca, Morelos, México.
Bravo A; Instituto de Biotecnología, Universidad Nacional Autónoma de Mexico, Cuernavaca, Morelos, México.
Soberón M; Instituto de Biotecnología, Universidad Nacional Autónoma de Mexico, Cuernavaca, Morelos, México .
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Źródło :
Applied and environmental microbiology [Appl Environ Microbiol] 2020 Oct 28; Vol. 86 (22). Date of Electronic Publication: 2020 Oct 28 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Bacillus thuringiensis/*genetics
Bacillus thuringiensis Toxins/*chemistry
Biological Control Agents/*pharmacology
Endotoxins/*chemistry
Hemolysin Proteins/*chemistry
Insecticides/*pharmacology
Spodoptera/*drug effects
Animals ; Bacillus thuringiensis/chemistry ; Mutation
Czasopismo naukowe
Tytuł :
Interaction between influenza A virus nucleoprotein and PB2 cap-binding domain is mediated by RNA.
Autorzy :
Szeto WC; Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Hsia HP; Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Tang YS; Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Shaw PC; Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
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Źródło :
PloS one [PLoS One] 2020 Sep 28; Vol. 15 (9), pp. e0239899. Date of Electronic Publication: 2020 Sep 28 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Host Microbial Interactions/*genetics
RNA, Messenger/*metabolism
RNA-Binding Proteins/*metabolism
RNA-Dependent RNA Polymerase/*metabolism
Viral Core Proteins/*metabolism
Viral Proteins/*metabolism
Binding Sites ; HEK293 Cells ; Humans ; Immunoprecipitation ; Nucleocapsid Proteins ; Plasmids/genetics ; Protein Binding/genetics ; RNA, Viral/metabolism ; RNA-Binding Proteins/genetics ; RNA-Dependent RNA Polymerase/chemistry ; RNA-Dependent RNA Polymerase/genetics ; Transfection ; Viral Core Proteins/genetics ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Virus Replication/genetics
Czasopismo naukowe
Tytuł :
Computational Alanine Scanning and Structural Analysis of the SARS-CoV-2 Spike Protein/Angiotensin-Converting Enzyme 2 Complex.
Autorzy :
Laurini E; Molecular Biology and Nanotechnology Laboratory (), DEA, University of Trieste, 34127 Trieste, Italy.
Marson D; Molecular Biology and Nanotechnology Laboratory (), DEA, University of Trieste, 34127 Trieste, Italy.
Aulic S; Molecular Biology and Nanotechnology Laboratory (), DEA, University of Trieste, 34127 Trieste, Italy.
Fermeglia M; Molecular Biology and Nanotechnology Laboratory (), DEA, University of Trieste, 34127 Trieste, Italy.
Pricl S; Molecular Biology and Nanotechnology Laboratory (), DEA, University of Trieste, 34127 Trieste, Italy.; Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, 90-136 Lodz, Poland.
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Źródło :
ACS nano [ACS Nano] 2020 Sep 22; Vol. 14 (9), pp. 11821-11830. Date of Electronic Publication: 2020 Aug 26.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Betacoronavirus/*metabolism
Peptidyl-Dipeptidase A/*metabolism
Spike Glycoprotein, Coronavirus/*metabolism
Angiotensin-Converting Enzyme 2 ; COVID-19 ; Computational Biology ; Coronavirus Infections/metabolism ; Humans ; Pandemics ; Pneumonia, Viral/metabolism ; Protein Binding ; Protein Conformation ; SARS-CoV-2
Czasopismo naukowe
Tytuł :
Evolutionary and functional classification of the CARF domain superfamily, key sensors in prokaryotic antivirus defense.
Autorzy :
Makarova KS; National Center for Biotechnology Information, National Library of Medicine, Bethesda, MD 20894, USA.
Timinskas A; Institute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Wolf YI; National Center for Biotechnology Information, National Library of Medicine, Bethesda, MD 20894, USA.
Gussow AB; National Center for Biotechnology Information, National Library of Medicine, Bethesda, MD 20894, USA.
Siksnys V; Institute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Venclovas Č; Institute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Koonin EV; National Center for Biotechnology Information, National Library of Medicine, Bethesda, MD 20894, USA.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2020 Sep 18; Vol. 48 (16), pp. 8828-8847.
Typ publikacji :
Journal Article; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't
MeSH Terms :
CRISPR-Cas Systems*
Protein Domains*
Archaea/*genetics
Archaeal Proteins/*genetics
Bacteria/*genetics
Bacterial Proteins/*genetics
Archaea/enzymology ; Archaeal Proteins/chemistry ; Bacteria/enzymology ; Bacterial Proteins/chemistry ; Evolution, Molecular
Czasopismo naukowe
Tytuł :
Efficient rational modification of non-ribosomal peptides by adenylation domain substitution.
Autorzy :
Calcott MJ; School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand.; Centre for Biodiscovery and Maurice Wilkins Centre for Molecular Biodiscovery, Victoria University of Wellington, Wellington, New Zealand.
Owen JG; School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand.; Centre for Biodiscovery and Maurice Wilkins Centre for Molecular Biodiscovery, Victoria University of Wellington, Wellington, New Zealand.
Ackerley DF; School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand. .; Centre for Biodiscovery and Maurice Wilkins Centre for Molecular Biodiscovery, Victoria University of Wellington, Wellington, New Zealand. .
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Źródło :
Nature communications [Nat Commun] 2020 Sep 11; Vol. 11 (1), pp. 4554. Date of Electronic Publication: 2020 Sep 11.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Adenosine Monophosphate/*metabolism
Peptides/*chemistry
Peptides/*metabolism
Bacterial Proteins/metabolism ; Catalytic Domain ; DNA Shuffling ; Models, Molecular ; Multigene Family ; Oligopeptides/chemistry ; Oligopeptides/metabolism ; Peptide Synthases/genetics ; Peptide Synthases/metabolism ; Protein Conformation ; Pseudomonas ; Substrate Specificity
Czasopismo naukowe
Tytuł :
A folding reaction at the C-terminal domain drives temperature sensing in TRPM8 channels.
Autorzy :
Díaz-Franulic I; Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso, Chile, 2340000; .; Center for Bioinformatics and Integrative Biology, Facultad de Ciencias de la Vida, Universidad Andrés Bello, Santiago, Chile, 8370146.
Raddatz N; Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso, Chile, 2340000.
Castillo K; Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso, Chile, 2340000.
González-Nilo FD; Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso, Chile, 2340000.; Center for Bioinformatics and Integrative Biology, Facultad de Ciencias de la Vida, Universidad Andrés Bello, Santiago, Chile, 8370146.
Latorre R; Centro Interdisciplinario de Neurociencia de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Valparaíso, Chile, 2340000; .
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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 Aug 18; Vol. 117 (33), pp. 20298-20304. Date of Electronic Publication: 2020 Aug 03.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Protein Domains*
Protein Folding*
TRPM Cation Channels/*chemistry
Animals ; Cold Temperature ; Cryoelectron Microscopy ; Humans ; Ion Channel Gating ; Models, Molecular ; Mutagenesis, Site-Directed ; Mutation ; Oocytes ; Protein Conformation ; TRPM Cation Channels/metabolism ; Thermodynamics ; Xenopus laevis
Czasopismo naukowe
Tytuł :
TNPO3-Mediated Nuclear Entry of the Rous Sarcoma Virus Gag Protein Is Independent of the Cargo-Binding Domain.
Autorzy :
Rice BL; Division of Infectious Diseases and Epidemiology, Department of Medicine, Penn State College of Medicine, Hershey, Pennsylvania, USA.
Stake MS; Division of Infectious Diseases and Epidemiology, Department of Medicine, Penn State College of Medicine, Hershey, Pennsylvania, USA.
Parent LJ; Division of Infectious Diseases and Epidemiology, Department of Medicine, Penn State College of Medicine, Hershey, Pennsylvania, USA .; Department of Microbiology and Immunology, Penn State College of Medicine, Hershey, Pennsylvania, USA.
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Źródło :
Journal of virology [J Virol] 2020 Aug 17; Vol. 94 (17). Date of Electronic Publication: 2020 Aug 17 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Virus Internalization*
Gene Products, gag/*metabolism
Rous sarcoma virus/*physiology
beta Karyopherins/*metabolism
Active Transport, Cell Nucleus ; Cell Nucleus ; Gene Products, gag/genetics ; Karyopherins/metabolism ; Nuclear Localization Signals/metabolism ; Nucleocapsid/metabolism ; Protein Transport ; Saccharomyces cerevisiae ; Virus Assembly ; alpha Karyopherins/metabolism ; beta Karyopherins/genetics
Czasopismo naukowe
Tytuł :
The molecular basis of selective DNA binding by the BRG1 AT-hook and bromodomain.
Autorzy :
Sanchez JC; Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States.
Zhang L; Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States; Integrated DNA Technologies IDT, Coralville, IA 52241, United States.
Evoli S; Department of Physics and The Center for Molecular Study of Condensed Soft Matter, Illinois Institute of Technology, Chicago, IL, United States.
Schnicker NJ; Protein & Crystallography Facility, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States.
Nunez-Hernandez M; Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States.
Yu L; Department of Biochemistry, Carver College of Medicine NMR Core Facility, University of Iowa, Iowa City, IA 52242, United States; The Iowa City Veterans Affairs Medical Center, Iowa City, IA 52242, United States.
Wereszczynski J; Department of Physics and The Center for Molecular Study of Condensed Soft Matter, Illinois Institute of Technology, Chicago, IL, United States. Electronic address: .
Pufall MA; Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States. Electronic address: .
Musselman CA; Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States; Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, United States. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Gene regulatory mechanisms [Biochim Biophys Acta Gene Regul Mech] 2020 Aug; Vol. 1863 (8), pp. 194566. Date of Electronic Publication: 2020 May 03.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Protein Domains*
DNA/*metabolism
DNA Helicases/*metabolism
Nuclear Proteins/*metabolism
Transcription Factors/*metabolism
Base Pairing ; Chromatin ; Chromatin Assembly and Disassembly ; DNA Helicases/chemistry ; DNA Helicases/genetics ; Gene Expression Regulation ; Histones/metabolism ; Humans ; Molecular Dynamics Simulation ; Mutation ; Neoplasms/genetics ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Protein Conformation ; Transcription Factors/chemistry ; Transcription Factors/genetics
Czasopismo naukowe
Tytuł :
A combined activation mechanism for the glucagon receptor.
Autorzy :
Mattedi G; Department of Chemistry, University College London, London WC1E 6BT, United Kingdom.
Acosta-Gutiérrez S; Department of Chemistry, University College London, London WC1E 6BT, United Kingdom.
Clark T; Computer-Chemistry Center, Department of Chemistry and Pharmacy, Friedrich-Alexander-University Erlangen-Nürnberg, Erlangen 91052, Germany.
Gervasio FL; Department of Chemistry, University College London, London WC1E 6BT, United Kingdom; .; Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.; Pharmaceutical Sciences, University of Geneva, Geneva CH-1211, Switzerland.
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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 Jul 07; Vol. 117 (27), pp. 15414-15422. Date of Electronic Publication: 2020 Jun 22.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
GTP-Binding Proteins/*metabolism
Receptors, Glucagon/*metabolism
Allosteric Regulation ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Drug Design ; Glucagon/analogs & derivatives ; Glucagon/metabolism ; Molecular Dynamics Simulation ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Dynamic rotation of the protruding domain enhances the infectivity of norovirus.
Autorzy :
Song C; National Institute for Physiological Sciences, Okazaki, Japan.
Takai-Todaka R; Laboratory of Viral Infection I, Department of Infection Control and Immunology, Ōmura Satoshi Memorial Institute & Graduate School of Infection Control Sciences, Kitasato University, Tokyo, Japan.
Miki M; DENKA Company Limited, Tokyo, Japan.
Haga K; Laboratory of Viral Infection I, Department of Infection Control and Immunology, Ōmura Satoshi Memorial Institute & Graduate School of Infection Control Sciences, Kitasato University, Tokyo, Japan.
Fujimoto A; Laboratory of Viral Infection I, Department of Infection Control and Immunology, Ōmura Satoshi Memorial Institute & Graduate School of Infection Control Sciences, Kitasato University, Tokyo, Japan.
Ishiyama R; Laboratory of Viral Infection I, Department of Infection Control and Immunology, Ōmura Satoshi Memorial Institute & Graduate School of Infection Control Sciences, Kitasato University, Tokyo, Japan.
Oikawa K; Laboratory of Viral Infection I, Department of Infection Control and Immunology, Ōmura Satoshi Memorial Institute & Graduate School of Infection Control Sciences, Kitasato University, Tokyo, Japan.
Yokoyama M; National Institute of Infectious Diseases, Tokyo, Japan.
Miyazaki N; Institute for Protein Research, Osaka University, Suita, Japan.; Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance, University of Tsukuba, Tsukuba, Japan.
Iwasaki K; Institute for Protein Research, Osaka University, Suita, Japan.; Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance, University of Tsukuba, Tsukuba, Japan.
Murakami K; National Institute of Infectious Diseases, Tokyo, Japan.
Katayama K; Laboratory of Viral Infection I, Department of Infection Control and Immunology, Ōmura Satoshi Memorial Institute & Graduate School of Infection Control Sciences, Kitasato University, Tokyo, Japan.; National Institute of Infectious Diseases, Tokyo, Japan.
Murata K; National Institute for Physiological Sciences, Okazaki, Japan.
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Źródło :
PLoS pathogens [PLoS Pathog] 2020 Jul 02; Vol. 16 (7), pp. e1008619. Date of Electronic Publication: 2020 Jul 02 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Capsid Proteins/*chemistry
Norovirus/*chemistry
Animals ; Cell Line ; Humans ; Mice
Czasopismo naukowe
Tytuł :
InteractomeSeq: a web server for the identification and profiling of domains and epitopes from phage display and next generation sequencing data.
Autorzy :
Puccio S; Laboratory of Translational Immunology, Humanitas Clinical and Research Center, IRCCS, Rozzano (Milan), 20089, Italy.
Grillo G; Institute for Biomedical Technologies, National Research Council, Bari 70100, Italy.
Consiglio A; Institute for Biomedical Technologies, National Research Council, Bari 70100, Italy.
Soluri MF; Department of Health Sciences & Center for TranslationalResearch on Autoimmune and Allergic Disease (CAAD), Università del Piemonte Orientale, Novara 28100, Italy.
Sblattero D; Department of Life Sciences, University of Trieste, Trieste 34100, Italy.
Cotella D; Department of Health Sciences & Center for TranslationalResearch on Autoimmune and Allergic Disease (CAAD), Università del Piemonte Orientale, Novara 28100, Italy.
Santoro C; Department of Health Sciences & Center for TranslationalResearch on Autoimmune and Allergic Disease (CAAD), Università del Piemonte Orientale, Novara 28100, Italy.
Liuni S; Institute for Biomedical Technologies, National Research Council, Bari 70100, Italy.
Bellis G; Institute for Biomedical Technologies, National Research Council, Segrate (Milan) 20090, Italy.
Lugli E; Laboratory of Translational Immunology, Humanitas Clinical and Research Center, IRCCS, Rozzano (Milan), 20089, Italy.; Humanitas Flow Cytometry Core, Humanitas Clinical and Research Center, IRCCS, Rozzano (Milan) 20089, Italy.
Peano C; Institute of Genetic and Biomedical Research, UoS Milan, National Research Council, Rozzano (Milan) 20089, Italy.; Genomic Unit, Humanitas Clinical and Research Center, IRCCS,Rozzano (Milan) 20089, Italy.
Licciulli F; Institute for Biomedical Technologies, National Research Council, Bari 70100, Italy.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2020 Jul 02; Vol. 48 (W1), pp. W200-W207.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Cell Surface Display Techniques*
Epitopes*
High-Throughput Nucleotide Sequencing*
Protein Domains*
Software*
Bacteriophages/genetics ; Internet
Czasopismo naukowe
Tytuł :
Domain-centric database to uncover structure of minimally characterized viral genomes.
Autorzy :
Bramley JC; Department of Genetics, Washington University School of Medicine, St Louis, MO, 63110, USA.
Yenkin AL; Department of Genetics, Washington University School of Medicine, St Louis, MO, 63110, USA.
Zaydman MA; Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, 63110, USA.
DiAntonio A; Department of Genetics, Washington University School of Medicine, St Louis, MO, 63110, USA.; Department of Developmental Biology, Washington University School of Medicine in St. Louis, St. Louis, 63110, MO, USA.
Milbrandt JD; Department of Genetics, Washington University School of Medicine, St Louis, MO, 63110, USA.; Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, 63110, USA.
Buchser WJ; Department of Genetics, Washington University School of Medicine, St Louis, MO, 63110, USA. .
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Źródło :
Scientific data [Sci Data] 2020 Jun 25; Vol. 7 (1), pp. 202. Date of Electronic Publication: 2020 Jun 25.
Typ publikacji :
Dataset; Journal Article
MeSH Terms :
Databases, Protein*
Genome, Viral*
Protein Domains*
Markov Chains
Czasopismo naukowe
Tytuł :
The geometric influence on the Cys2His2 zinc finger domain and functional plasticity.
Autorzy :
Mueller AL; Institute for Systems Genetics, NYU Langone Health, New York, NY 10016, USA.; Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA.
Corbi-Verge C; Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada.
Giganti DO; Institute for Systems Genetics, NYU Langone Health, New York, NY 10016, USA.; Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA.
Ichikawa DM; Institute for Systems Genetics, NYU Langone Health, New York, NY 10016, USA.; Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA.
Spencer JM; Institute for Systems Genetics, NYU Langone Health, New York, NY 10016, USA.; Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA.
MacRae M; Institute for Systems Genetics, NYU Langone Health, New York, NY 10016, USA.; Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA.
Garton M; Institute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, Ontario M5S 3G9, Canada.
Kim PM; Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada.; Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S3E1, Canada.; Department of Computer Science, University of Toronto, Toronto, Ontario M5S3E1, Canada.
Noyes MB; Institute for Systems Genetics, NYU Langone Health, New York, NY 10016, USA.; Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2020 Jun 19; Vol. 48 (11), pp. 6382-6402.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
Models, Molecular*
Protein Domains/*physiology
Zinc Fingers/*physiology
Amino Acid Sequence ; Animals ; Base Sequence ; DNA/chemical synthesis ; DNA/genetics ; DNA/metabolism ; Deep Learning ; Humans ; Hydrogen Bonding ; Protein Domains/genetics ; Reproducibility of Results ; Substrate Specificity/genetics ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Zinc Fingers/genetics
Czasopismo naukowe
Tytuł :
Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family.
Autorzy :
D'Abrosca G; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Paladino A; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.; SCITEC-CNR, via Mario Bianco 9, 20131, Milano, Italy.
Baglivo I; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Russo L; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Sassano M; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Grazioso R; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Iacovino R; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Pirone L; Institute of Biostructures and Bioimaging - CNR, Via Mezzocannone 16, 80134, Naples, Italy.
Pedone EM; Institute of Biostructures and Bioimaging - CNR, Via Mezzocannone 16, 80134, Naples, Italy.
Pedone PV; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Isernia C; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Fattorusso R; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy.
Malgieri G; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania 'Luigi Vanvitelli', via Vivaldi, 43, 81100, Caserta, Italy. .
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Źródło :
Scientific reports [Sci Rep] 2020 Jun 09; Vol. 10 (1), pp. 9283. Date of Electronic Publication: 2020 Jun 09.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Agrobacterium tumefaciens/*metabolism
DNA-Binding Proteins/*genetics
Protein Structure, Secondary/*genetics
Zinc Fingers/*genetics
Agrobacterium tumefaciens/genetics ; Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; DNA-Binding Proteins/metabolism ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular
Czasopismo naukowe
Tytuł :
A supramolecular system that strictly follows the binding mechanism of conformational selection.
Autorzy :
Yang LP; Shenzhen Grubbs Institute, Department of Chemistry, Guangdong Provincial Key Laboratory of Catalysis and Academy for Advanced Interdisciplinary Studies, Southern University of Science and Technology, Xueyuan Blvd 1088, Shenzhen, 518055, China.
Zhang L; Shenzhen Grubbs Institute, Department of Chemistry, Guangdong Provincial Key Laboratory of Catalysis and Academy for Advanced Interdisciplinary Studies, Southern University of Science and Technology, Xueyuan Blvd 1088, Shenzhen, 518055, China.
Quan M; Shenzhen Grubbs Institute, Department of Chemistry, Guangdong Provincial Key Laboratory of Catalysis and Academy for Advanced Interdisciplinary Studies, Southern University of Science and Technology, Xueyuan Blvd 1088, Shenzhen, 518055, China.
Ward JS; Department of Chemistry, University of Jyvaskyla, P.O. Box 35, FI-40014, Jyväskylä, Finland.
Ma YL; Shenzhen Grubbs Institute, Department of Chemistry, Guangdong Provincial Key Laboratory of Catalysis and Academy for Advanced Interdisciplinary Studies, Southern University of Science and Technology, Xueyuan Blvd 1088, Shenzhen, 518055, China.
Zhou H; Shenzhen Grubbs Institute, Department of Chemistry, Guangdong Provincial Key Laboratory of Catalysis and Academy for Advanced Interdisciplinary Studies, Southern University of Science and Technology, Xueyuan Blvd 1088, Shenzhen, 518055, China.
Rissanen K; Department of Chemistry, University of Jyvaskyla, P.O. Box 35, FI-40014, Jyväskylä, Finland.
Jiang W; Shenzhen Grubbs Institute, Department of Chemistry, Guangdong Provincial Key Laboratory of Catalysis and Academy for Advanced Interdisciplinary Studies, Southern University of Science and Technology, Xueyuan Blvd 1088, Shenzhen, 518055, China. .
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Źródło :
Nature communications [Nat Commun] 2020 Jun 02; Vol. 11 (1), pp. 2740. Date of Electronic Publication: 2020 Jun 02.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Biophysical Phenomena*
Protein Domains*
Proteins/*metabolism
Heterocyclic Compounds/chemistry ; Heterocyclic Compounds/metabolism ; Kinetics ; Ligands ; Models, Molecular ; Models, Theoretical ; Protein Binding ; Protein Conformation ; Proteins/chemistry ; Thermodynamics
Czasopismo naukowe
Tytuł :
Solution structure of the cytoplasmic domain of NhaP2 a K antiporter from Vibrio cholera.
Autorzy :
Orriss GL; University of Manitoba, Department of Chemistry, 144 Dysart Road, Winnipeg, Manitoba R3T 2N2, Canada.
To V; University of Manitoba, Department of Chemistry, 144 Dysart Road, Winnipeg, Manitoba R3T 2N2, Canada.
Moya-Torres A; University of Manitoba, Department of Chemistry, 144 Dysart Road, Winnipeg, Manitoba R3T 2N2, Canada.
Seabrook G; The OCI/UHN High Field NMR Facility, MaRS Toronto Medical Discovery Tower, 101 College Street, Toronto, Ontario M5C 1L7, Canada.
O'Neil J; University of Manitoba, Department of Chemistry, 144 Dysart Road, Winnipeg, Manitoba R3T 2N2, Canada.
Stetefeld J; University of Manitoba, Department of Chemistry, 144 Dysart Road, Winnipeg, Manitoba R3T 2N2, Canada. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2020 Jun 01; Vol. 1862 (6), pp. 183225. Date of Electronic Publication: 2020 Feb 29.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Bacterial Proteins/*chemistry
Potassium-Hydrogen Antiporters/*chemistry
Vibrio cholerae/*chemistry
Adenosine Triphosphate/metabolism ; Antiporters/chemistry ; Antiporters/metabolism ; Bacterial Proteins/metabolism ; Binding Sites ; Cytoplasm/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Potassium-Hydrogen Antiporters/metabolism ; Protein Conformation
Czasopismo naukowe
Tytuł :
Structure of HIRAN domain of human HLTF bound to duplex DNA provides structural basis for DNA unwinding to initiate replication fork regression.
Autorzy :
Hishiki A; School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8002, Japan.
Sato M; Graduate School of Medical Life Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Hashimoto H; School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8002, Japan.
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Źródło :
Journal of biochemistry [J Biochem] 2020 Jun 01; Vol. 167 (6), pp. 597-602.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Domains*
DNA/*metabolism
DNA Replication/*physiology
DNA-Binding Proteins/*chemistry
Transcription Factors/*chemistry
Crystallization ; DNA Damage ; DNA Helicases/metabolism ; Humans ; Protein Binding ; Protein Conformation ; X-Ray Diffraction
Czasopismo naukowe
Tytuł :
N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity.
Autorzy :
Bouwman KM; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Habraeken N; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Laconi A; Present address: Department of Comparative Biomedicine and Food Science, University of Padua, Legnaro (PD), Italy.; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Berends AJ; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Groenewoud L; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Alders M; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Kemp V; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Verheije MH; Division of Pathology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
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Źródło :
The Journal of general virology [J Gen Virol] 2020 Jun; Vol. 101 (6), pp. 599-608.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Coronavirus Infections/*immunology
Host Specificity/*immunology
Infectious bronchitis virus/*chemistry
Receptors, Virus/*immunology
Spike Glycoprotein, Coronavirus/*chemistry
Animals ; Cell Line ; Chick Embryo ; Coronavirus Infections/virology ; Glycosylation ; Infectious bronchitis virus/immunology ; Kidney/cytology ; Kidney/embryology ; Protein Binding ; Receptors, Cell Surface/metabolism ; Receptors, Virus/metabolism ; Recombinant Proteins ; Spike Glycoprotein, Coronavirus/metabolism ; Viral Tropism/immunology ; Virus Attachment ; Virus Replication
Czasopismo naukowe

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