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Tytuł :
Disruption of the interaction between TFIIAαβ and TFIIA recognition element inhibits RNA polymerase II gene transcription in a promoter context-dependent manner.
Autorzy :
Wang J; School of Materials and Metallurgy, Wuhan University of Science and Technology, Wuhan 430081, China; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China.
Shi K; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China.
Wu Z; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China.
Zhang C; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China.
Li Y; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China.
Deng H; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China.
Zhao S; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China. Electronic address: .
Deng W; College of Life Science and Health, Wuhan University of Science and Technology, Wuhan 430065, China. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Gene regulatory mechanisms [Biochim Biophys Acta Gene Regul Mech] 2020 Oct; Vol. 1863 (10), pp. 194611. Date of Electronic Publication: 2020 Jul 31.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Gene Expression Regulation*
Promoter Regions, Genetic*
Response Elements*
Transcriptional Activation*
RNA Polymerase II/*metabolism
Transcription Factor TFIIA/*metabolism
Transcription Factor TFIIB/*metabolism
Amino Acids ; Base Sequence ; Cell Line ; Humans ; Models, Molecular ; Mutation ; Nucleotide Motifs ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; Transcription Factor TFIIA/chemistry ; Transcription Factor TFIIA/genetics ; Transcription Factor TFIIB/chemistry ; Transcription Factor TFIIB/genetics
Czasopismo naukowe
Tytuł :
Structural variations in human ACE2 may influence its binding with SARS-CoV-2 spike protein.
Autorzy :
Hussain M; Bioinformatics and Molecular Medicine Research Group, Dow Research Institute of Biotechnology and Biomedical Sciences, Dow College of Biotechnology, Dow University of Health Sciences, Karachi, Pakistan.
Jabeen N; Department of Microbiology, University of Karachi, Karachi, Pakistan.
Raza F; Bioinformatics and Molecular Medicine Research Group, Dow Research Institute of Biotechnology and Biomedical Sciences, Dow College of Biotechnology, Dow University of Health Sciences, Karachi, Pakistan.
Shabbir S; Bioinformatics and Molecular Medicine Research Group, Dow Research Institute of Biotechnology and Biomedical Sciences, Dow College of Biotechnology, Dow University of Health Sciences, Karachi, Pakistan.; Department of Microbiology, University of Karachi, Karachi, Pakistan.
Baig AA; Bioinformatics and Molecular Medicine Research Group, Dow Research Institute of Biotechnology and Biomedical Sciences, Dow College of Biotechnology, Dow University of Health Sciences, Karachi, Pakistan.
Amanullah A; Bioinformatics and Molecular Medicine Research Group, Dow Research Institute of Biotechnology and Biomedical Sciences, Dow College of Biotechnology, Dow University of Health Sciences, Karachi, Pakistan.
Aziz B; Bioinformatics and Molecular Medicine Research Group, Dow Research Institute of Biotechnology and Biomedical Sciences, Dow College of Biotechnology, Dow University of Health Sciences, Karachi, Pakistan.
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Źródło :
Journal of medical virology [J Med Virol] 2020 Sep; Vol. 92 (9), pp. 1580-1586. Date of Electronic Publication: 2020 Apr 15.
Typ publikacji :
Journal Article
MeSH Terms :
Binding Sites*
Models, Molecular*
Angiotensin-Converting Enzyme 2/*chemistry
Spike Glycoprotein, Coronavirus/*chemistry
Alleles ; Amino Acid Sequence ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/metabolism ; Genetic Variation ; Humans ; Protein Binding ; Protein Conformation ; Receptors, Virus/chemistry ; Receptors, Virus/metabolism ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
A kinetic mechanism for enhanced selectivity of membrane transport.
Autorzy :
Bisignano P; Cardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California, United States of America.
Lee MA; Cardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California, United States of America.
George A; Department of Biomedical Engineering, Oregon Health and Science University, Portland, Oregon, United States of America.
Zuckerman DM; Department of Biomedical Engineering, Oregon Health and Science University, Portland, Oregon, United States of America.
Grabe M; Cardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California, United States of America.
Rosenberg JM; Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.
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Źródło :
PLoS computational biology [PLoS Comput Biol] 2020 Jul 02; Vol. 16 (7), pp. e1007789. Date of Electronic Publication: 2020 Jul 02 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Binding Sites*
Membrane Transport Proteins*/chemistry
Membrane Transport Proteins*/metabolism
Models, Biological*
Biological Transport/*physiology
Protein Binding/*physiology
Computational Biology ; Humans ; Kinetics ; Molecular Dynamics Simulation ; Sodium-Glucose Transporter 1 ; Substrate Specificity
Czasopismo naukowe
Tytuł :
Discovery of a new sialic acid binding region that regulates Siglec-7.
Autorzy :
Yamakawa N; Biocience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan.; Department of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan.; Université de Lille, CNRS, UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle, Lille, 59000, France.
Yasuda Y; Biocience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan.; Department of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Yoshimura A; Biocience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan.; Department of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Goshima A; Biocience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan.; Department of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Crocker PR; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK.
Vergoten G; Université de Lille, CNRS, UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle, Lille, 59000, France.
Nishiura Y; Department of Chemical Science and Engineering, School of Materials and Chemical Technology, Tokyo Institute of Technology, 2-12-1-H-101, Ookayama, Meguro, Tokyo, 152-8552, Japan.
Takahashi T; Department of pharmacy, Yokohama University of Pharmacy, 601, Matana-cho, Totsuka-ku, Yokohama, Kanagawa, 245-0066, Japan.
Hanashima S; Structural Glycobiology Team, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.; Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka, 560-0043, Japan.
Matsumoto K; Structural Glycobiology Team, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Yamaguchi Y; Structural Glycobiology Team, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.; Faculty of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aobaku, Sendai, Miyagi, 981-8558, Japan.
Tanaka H; Department of Chemical Science and Engineering, School of Materials and Chemical Technology, Tokyo Institute of Technology, 2-12-1-H-101, Ookayama, Meguro, Tokyo, 152-8552, Japan.
Kitajima K; Biocience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan.; Department of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan.
Sato C; Biocience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan. .; Department of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan. .
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Źródło :
Scientific reports [Sci Rep] 2020 May 26; Vol. 10 (1), pp. 8647. Date of Electronic Publication: 2020 May 26.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Molecular Conformation*
Molecular Docking Simulation*
Antigens, Differentiation, Myelomonocytic/*metabolism
Binding Sites/*physiology
Lectins/*metabolism
Sialic Acids/*metabolism
Amino Acid Sequence ; Binding Sites/genetics ; Gangliosides/metabolism ; Glycoconjugates/metabolism ; Humans ; Killer Cells, Natural/immunology ; Monocytes/immunology ; Mutagenesis, Site-Directed ; Sialic Acid Binding Ig-like Lectin 3/metabolism
Czasopismo naukowe
Tytuł :
Sequence-based prediction of protein binding mode landscapes.
Autorzy :
Horvath A; MTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.; The John Curtin School of Medical Research, The Australian National University, Canberra, Australia.
Miskei M; MTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Ambrus V; MTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Vendruscolo M; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Fuxreiter M; MTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
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Źródło :
PLoS computational biology [PLoS Comput Biol] 2020 May 26; Vol. 16 (5), pp. e1007864. Date of Electronic Publication: 2020 May 26 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Protein Binding*
Protein Processing, Post-Translational*
Proteins/*chemistry
Algorithms ; Computational Biology/methods ; Databases, Protein ; Eukaryotic Initiation Factor-2/chemistry ; Fuzzy Logic ; Humans ; Intrinsically Disordered Proteins/chemistry ; Probability ; Protein Domains ; Protein Folding ; ROC Curve ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae Proteins/chemistry ; Tumor Suppressor Protein p53/chemistry ; eIF-2 Kinase/chemistry
Czasopismo naukowe
Tytuł :
Restriction of S-adenosylmethionine conformational freedom by knotted protein binding sites.
Autorzy :
Perlinska AP; College of Inter-Faculty Individual Studies in Mathematics and Natural Sciences, University of Warsaw, Warsaw, Poland.; Centre of New Technologies, University of Warsaw, Warsaw, Poland.
Stasiulewicz A; Centre of New Technologies, University of Warsaw, Warsaw, Poland.; Faculty of Pharmacy, Medical University of Warsaw, Warsaw, Poland.
Nawrocka EK; Centre of New Technologies, University of Warsaw, Warsaw, Poland.; Faculty of Chemistry, University of Warsaw, Warsaw, Poland.
Kazimierczuk K; Centre of New Technologies, University of Warsaw, Warsaw, Poland.
Setny P; Centre of New Technologies, University of Warsaw, Warsaw, Poland.
Sulkowska JI; Centre of New Technologies, University of Warsaw, Warsaw, Poland.; Faculty of Chemistry, University of Warsaw, Warsaw, Poland.
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Źródło :
PLoS computational biology [PLoS Comput Biol] 2020 May 26; Vol. 16 (5), pp. e1007904. Date of Electronic Publication: 2020 May 26 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Methionine Adenosyltransferase/*chemistry
S-Adenosylmethionine/*chemistry
Adenine/chemistry ; Amino Acid Motifs ; Computational Biology/methods ; Computer Simulation ; Databases, Protein ; Glycine/chemistry ; Magnetic Resonance Spectroscopy ; Molecular Dynamics Simulation ; Principal Component Analysis ; Protein Binding ; Protein Domains ; Protein Folding ; Solvents ; Temperature ; Water/chemistry ; tRNA Methyltransferases/chemistry
Czasopismo naukowe
Tytuł :
Cellular mRNA export factor UAP56 recognizes nucleic acid binding site of influenza virus NP protein.
Autorzy :
Morris AK; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Wang Z; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA; Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Ivey AL; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Xie Y; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Hill PS; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Schey KL; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA; Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Ren Y; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA. Electronic address: .
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Źródło :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2020 Apr 30; Vol. 525 (2), pp. 259-264. Date of Electronic Publication: 2020 Feb 19.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
DEAD-box RNA Helicases/*metabolism
RNA-Binding Proteins/*chemistry
Viral Core Proteins/*chemistry
Genome, Viral ; Host-Pathogen Interactions ; Humans ; Nucleocapsid Proteins ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Ribonucleoproteins/metabolism ; Viral Core Proteins/metabolism ; Virus Assembly ; Virus Replication
Czasopismo naukowe
Tytuł :
New Protocol for Predicting the Ligand-Binding Site and Mode Based on the 3D-RISM/KH Theory.
Autorzy :
Sugita M; Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, 1-1-1, Noji-higashi, Kusatsu, Shiga 525-8577, Japan.; Department of Computer Science, School of Computing, Tokyo Institute of Technology, W8-76, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan.
Hamano M; Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, 1-1-1, Noji-higashi, Kusatsu, Shiga 525-8577, Japan.
Kasahara K; Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, 1-1-1, Noji-higashi, Kusatsu, Shiga 525-8577, Japan.
Kikuchi T; Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, 1-1-1, Noji-higashi, Kusatsu, Shiga 525-8577, Japan.
Hirata F; Toyota Physical and Chemical Research Institute, 41-1, Yokomichi, Nagakute, Aichi 480-1192, Japan.
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Źródło :
Journal of chemical theory and computation [J Chem Theory Comput] 2020 Apr 14; Vol. 16 (4), pp. 2864-2876. Date of Electronic Publication: 2020 Mar 27.
Typ publikacji :
Journal Article
MeSH Terms :
Algorithms*
Binding Sites*
Crystallography, X-Ray ; Ligands ; Models, Molecular ; Proteins/chemistry
Czasopismo naukowe
Tytuł :
A computational approach yields selective inhibitors of human excitatory amino acid transporter 2 (EAAT2).
Autorzy :
Damm-Ganamet KL; Discovery Sciences, Janssen Research and Development, San Diego, California 92121 .
Rives ML; Discovery Sciences, Janssen Research and Development, San Diego, California 92121.
Wickenden AD; Discovery Sciences, Janssen Research and Development, San Diego, California 92121.
McAllister HM; Discovery Sciences, Janssen Research and Development, San Diego, California 92121.
Mirzadegan T; Discovery Sciences, Janssen Research and Development, San Diego, California 92121.
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2020 Mar 27; Vol. 295 (13), pp. 4359-4366. Date of Electronic Publication: 2020 Feb 20.
Typ publikacji :
Journal Article
MeSH Terms :
Amino Acid Transport System X-AG/*antagonists & inhibitors
Binding Sites/*drug effects
Central Nervous System Diseases/*drug therapy
Excitatory Amino Acid Transporter 2/*antagonists & inhibitors
Amino Acid Transport System X-AG/chemistry ; Amino Acid Transport System X-AG/genetics ; Animals ; Binding Sites/genetics ; Biological Transport/drug effects ; Central Nervous System Diseases/genetics ; Central Nervous System Diseases/pathology ; Computational Biology ; Excitatory Amino Acid Transporter 2/chemistry ; Excitatory Amino Acid Transporter 2/genetics ; Humans ; Protein Binding/drug effects ; Synaptic Transmission/drug effects ; User-Computer Interface
Czasopismo naukowe
Tytuł :
Performance of virtual screening against GPCR homology models: Impact of template selection and treatment of binding site plasticity.
Autorzy :
Jaiteh M; Science for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.
Rodríguez-Espigares I; Research Programme on Biomedical Informatics (GRIB), Department of Experimental and Health Sciences of Pompeu Fabra University (UPF), Hospital del Mar Medical Research Institute (IMIM), Barcelona, Spain.
Selent J; Research Programme on Biomedical Informatics (GRIB), Department of Experimental and Health Sciences of Pompeu Fabra University (UPF), Hospital del Mar Medical Research Institute (IMIM), Barcelona, Spain.
Carlsson J; Science for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.
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Źródło :
PLoS computational biology [PLoS Comput Biol] 2020 Mar 13; Vol. 16 (3), pp. e1007680. Date of Electronic Publication: 2020 Mar 13 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Molecular Docking Simulation*
Receptors, G-Protein-Coupled*/chemistry
Receptors, G-Protein-Coupled*/genetics
Receptors, G-Protein-Coupled*/metabolism
Structural Homology, Protein*
Computational Biology/*methods
Crystallization ; Drug Design ; Humans ; Ligands ; Protein Binding
Czasopismo naukowe
Tytuł :
Structure and mechanism of monoclonal antibody binding to the junctional epitope of Plasmodium falciparum circumsporozoite protein.
Autorzy :
Oyen D; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
Torres JL; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
Aoto PC; Department of Pharmacology, University of California at San Diego, La Jolla, California, United States of America.
Flores-Garcia Y; Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, United States of America.
Binter Š; Kymab Ltd., The Bennet Building (B930), Babraham Research Campus, Cambridge, United Kingdom.
Pholcharee T; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
Carroll S; Atreca Inc., South San Francisco, California, United States of America.
Reponen S; Atreca Inc., South San Francisco, California, United States of America.
Wash R; Kymab Ltd., The Bennet Building (B930), Babraham Research Campus, Cambridge, United Kingdom.
Liang Q; Kymab Ltd., The Bennet Building (B930), Babraham Research Campus, Cambridge, United Kingdom.
Lemiale F; PATH's Malaria Vaccine Initiative, PATH Center for Vaccine Innovation and Access, Washington, United States of America.
Locke E; PATH's Malaria Vaccine Initiative, PATH Center for Vaccine Innovation and Access, Washington, United States of America.
Bradley A; Kymab Ltd., The Bennet Building (B930), Babraham Research Campus, Cambridge, United Kingdom.; Wellcome Trust Sanger Institute, Hinxton, Cambridge, United Kingdom.
King CR; PATH's Malaria Vaccine Initiative, PATH Center for Vaccine Innovation and Access, Washington, United States of America.
Emerling D; Atreca Inc., South San Francisco, California, United States of America.
Kellam P; Kymab Ltd., The Bennet Building (B930), Babraham Research Campus, Cambridge, United Kingdom.; Department of Infectious Diseases, Faculty of Medicine, Imperial College London, London, United Kingdom.
Zavala F; Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, United States of America.
Ward AB; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
Wilson IA; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, United States of America.
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Źródło :
PLoS pathogens [PLoS Pathog] 2020 Mar 09; Vol. 16 (3), pp. e1008373. Date of Electronic Publication: 2020 Mar 09 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites, Antibody*
Antibodies, Monoclonal, Murine-Derived/*chemistry
Antibodies, Protozoan/*chemistry
Epitopes/*chemistry
Plasmodium falciparum/*chemistry
Protozoan Proteins/*chemistry
Animals ; Antibodies, Monoclonal, Murine-Derived/immunology ; Antibodies, Protozoan/immunology ; Epitopes/immunology ; Female ; Male ; Mice ; Mice, Transgenic ; Plasmodium falciparum/immunology ; Protozoan Proteins/immunology ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Construction of a circularly connected VHH bispecific antibody (cyclobody) for the desirable positioning of antigen-binding sites.
Autorzy :
Hemmi S; Graduate School of Science and Engineering, Yamagata University, 4-3-16 Jyonan, Yonezawa, Yamagata, 992-8510, Japan.
Asano R; Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo, 183-8538, Japan.
Kimura K; Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo, 183-8538, Japan.
Umetsu M; Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, 6-6-11-606 Aoba-yama, Aramaki, Aoba-ku, Sendai, Miyagi, 980-8579, Japan.
Nakanishi T; Department of Applied Chemistry and Bioengineering, Graduate School of Engineering, Osaka City University, Sugimoto 3-3-138, Sumiyoshi-ku, Osaka, 558-8585, Japan.
Kumagai I; Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo, 183-8538, Japan.
Makabe K; Graduate School of Science and Engineering, Yamagata University, 4-3-16 Jyonan, Yonezawa, Yamagata, 992-8510, Japan. Electronic address: .
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Źródło :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2020 Feb 26; Vol. 523 (1), pp. 72-77. Date of Electronic Publication: 2019 Dec 09.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites, Antibody*
Antibodies, Bispecific/*chemistry
Antibodies, Bispecific/*immunology
Receptors, Antigen/*chemistry
Receptors, Antigen/*immunology
Cell Line ; Cell Proliferation ; Cell Survival ; Humans ; Proteolysis
Czasopismo naukowe
Tytuł :
Multiple lipid binding sites determine the affinity of PH domains for phosphoinositide-containing membranes.
Autorzy :
Yamamoto E; Department of System Design Engineering, Keio University, Yokohama, Kanagawa 223-8522, Japan.
Domański J; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Naughton FB; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.; Department of Physics, Arizona State University, Tempe, AZ 85287-1504, USA.
Best RB; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Kalli AC; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.; Leeds Institute of Cardiovascular and Metabolic Medicine and Astbury Center for Structural Molecular Biology, University of Leeds, Leeds, UK.
Stansfeld PJ; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Sansom MSP; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
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Źródło :
Science advances [Sci Adv] 2020 Feb 19; Vol. 6 (8), pp. eaay5736. Date of Electronic Publication: 2020 Feb 19 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Pleckstrin Homology Domains*
Cell Membrane/*chemistry
Lipids/*chemistry
Phosphatidylinositols/*chemistry
Algorithms ; Cell Membrane/metabolism ; Membrane Lipids/chemistry ; Membrane Lipids/metabolism ; Models, Theoretical ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Receptors, Cytoplasmic and Nuclear/chemistry ; Receptors, Cytoplasmic and Nuclear/metabolism
Czasopismo naukowe
Tytuł :
Chemical structure of semiochemicals and key binding sites together determine the olfactory functional modes of odorant-binding protein 2 in Eastern honey bee, Apis cerana.
Autorzy :
Li HL; College of Life Sciences, China Jiliang University, Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, Hangzhou 310018, China. Electronic address: .
Song XM; College of Life Sciences, China Jiliang University, Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, Hangzhou 310018, China.
Wu F; College of Life Sciences, China Jiliang University, Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, Hangzhou 310018, China.
Qiu YL; College of Life Sciences, China Jiliang University, Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, Hangzhou 310018, China.
Fu XB; College of Life Sciences, China Jiliang University, Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, Hangzhou 310018, China.
Zhang LY; College of Life Sciences, China Jiliang University, Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, Hangzhou 310018, China; College of Life Science, Shangrao Normal University, Shangrao 334001, China.
Tan J; College of Life Sciences, China Jiliang University, Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, Hangzhou 310018, China.
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2020 Feb 15; Vol. 145, pp. 876-884. Date of Electronic Publication: 2019 Nov 22.
Typ publikacji :
Journal Article
MeSH Terms :
Bees*/physiology
Binding Sites*
Molecular Docking Simulation*
Molecular Dynamics Simulation*
Pheromones/*chemistry
Receptors, Odorant/*chemistry
Amino Acid Sequence ; Animals ; Fluorescent Antibody Technique ; Ligands ; Mutation ; Odorants ; Olfactory Perception ; Pheromones/metabolism ; Protein Binding ; Receptors, Odorant/genetics ; Receptors, Odorant/metabolism ; Recombinant Proteins ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites.
Autorzy :
Eisenhaber, Birgit (AUTHOR)
Sinha, Swati (AUTHOR)
Jadalanki, Chaitanya K. (AUTHOR)
Shitov, Vladimir A. (AUTHOR)
Tan, Qiao Wen (AUTHOR)
Sirota, Fernanda L. (AUTHOR)
Eisenhaber, Frank (AUTHOR)
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Źródło :
Biology Direct. 1/12/2021, Vol. 16 Issue 1, p1-18. 18p.
Czasopismo naukowe
Tytuł :
Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2.
Autorzy :
Bracken CJ; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Lim SA; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Solomon P; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Rettko NJ; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Nguyen DP; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.; Lyell Immunopharma Inc., Seattle, WA, USA.
Zha BS; Department of Pulmonary, Critical Care, Allergy and Sleep Medicine, University of California San Francisco, San Francisco, CA, USA.
Schaefer K; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Byrnes JR; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Zhou J; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Lui I; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Liu J; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.; Merck & Co., South San Francisco, CA, USA.
Pance K; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Zhou XX; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Leung KK; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA.
Wells JA; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA. .; Department of Cellular & Molecular Pharmacology, University of California San Francisco, San Francisco, CA, USA. .; Chan Zuckerberg Biohub, San Francisco, CA, USA. .
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Corporate Authors :
QCRG Structural Biology Consortium
Źródło :
Nature chemical biology [Nat Chem Biol] 2021 Jan; Vol. 17 (1), pp. 113-121. Date of Electronic Publication: 2020 Oct 20.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Angiotensin-Converting Enzyme 2/*chemistry
Antibodies, Neutralizing/*chemistry
Antibodies, Viral/*chemistry
Single-Chain Antibodies/*chemistry
Spike Glycoprotein, Coronavirus/*chemistry
Angiotensin-Converting Enzyme 2/antagonists & inhibitors ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/immunology ; Animals ; Antibodies, Neutralizing/genetics ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/genetics ; Antibodies, Viral/immunology ; Binding Sites, Antibody/genetics ; Binding Sites, Antibody/immunology ; Chlorocebus aethiops ; Cryoelectron Microscopy ; HEK293 Cells ; Humans ; Models, Molecular ; Peptide Library ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; SARS-CoV-2 ; Single-Chain Antibodies/genetics ; Single-Chain Antibodies/immunology ; Spike Glycoprotein, Coronavirus/antagonists & inhibitors ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Vero Cells
Czasopismo naukowe

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