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Tytuł :
Systematic Engineering of Optimized Autonomous Heavy-Chain Variable Domains.
Autorzy :
Nilvebrant J; Banting and Best Department of Medical Research and Department of Molecular Genetics, The Donnelly Centre, University of Toronto, Toronto, Ontario M5S 3E1, Canada.
Ereño-Orbea J; Program in Molecular Medicine, The Hospital for Sick Children Research Institute and Departments of Biochemistry and Immunology, University of Toronto, Toronto, Ontario, Canada.
Gorelik M; Banting and Best Department of Medical Research and Department of Molecular Genetics, The Donnelly Centre, University of Toronto, Toronto, Ontario M5S 3E1, Canada.
Julian MC; Isermann Department of Chemical & Biological Engineering, Center for Biotechnology & Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Tessier PM; Isermann Department of Chemical & Biological Engineering, Center for Biotechnology & Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA; Departments of Chemical Engineering, Pharmaceutical Sciences, and Biomedical Engineering, Biointerfaces Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Julien JP; Program in Molecular Medicine, The Hospital for Sick Children Research Institute and Departments of Biochemistry and Immunology, University of Toronto, Toronto, Ontario, Canada.
Sidhu SS; Banting and Best Department of Medical Research and Department of Molecular Genetics, The Donnelly Centre, University of Toronto, Toronto, Ontario M5S 3E1, Canada. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Oct 15; Vol. 433 (21), pp. 167241. Date of Electronic Publication: 2021 Sep 09.
Typ publikacji :
Journal Article
MeSH Terms :
Binding Sites, Antibody*
Peptide Library*
Aspartic Acid/*chemistry
Complementarity Determining Regions/*chemistry
Immunoglobulin Heavy Chains/*chemistry
Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; Cloning, Molecular ; Complementarity Determining Regions/genetics ; Complementarity Determining Regions/metabolism ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Humans ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Heavy Chains/metabolism ; Kinetics ; Models, Molecular ; Protein Aggregates ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Interaction Domains and Motifs ; Receptor, EphA1/genetics ; Receptor, EphA1/immunology ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
Czasopismo naukowe
Tytuł :
Rational Engraftment of Quaternary-Interactive Acidic Loops for Anti-HIV-1 Antibody Improvement.
Autorzy :
Liu Q; Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, USA .
Zhang P; Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, USA.
Miao H; Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, USA.
Lin Y; Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, USA.
Kwon YD; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, USA.
Kwong PD; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, USA.
Rikhtegaran-Tehrani Z; Division of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA.; Division of Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Seaman MS; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA.
DeVico AL; Division of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Sajadi MM; Division of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA.; Division of Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA.; Department of Medicine, Baltimore VA Medical Center, Baltimore, Maryland, USA.
Lusso P; Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, USA .
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Źródło :
Journal of virology [J Virol] 2021 May 24; Vol. 95 (12). Date of Electronic Publication: 2021 May 24 (Print Publication: 2021).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Binding Sites, Antibody*/immunology
Protein Engineering*
Broadly Neutralizing Antibodies/*immunology
CD4 Antigens/*metabolism
HIV Antibodies/*immunology
HIV Envelope Protein gp120/*chemistry
HIV Envelope Protein gp120/*immunology
HIV-1/*immunology
Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/therapeutic use ; Binding Sites ; Broadly Neutralizing Antibodies/chemistry ; Broadly Neutralizing Antibodies/genetics ; Broadly Neutralizing Antibodies/therapeutic use ; CD4 Antigens/chemistry ; Epitopes/chemistry ; Epitopes/immunology ; HIV Antibodies/chemistry ; HIV Antibodies/genetics ; HIV Antibodies/therapeutic use ; HIV Envelope Protein gp120/metabolism ; HIV Infections/prevention & control ; HIV Infections/therapy ; Humans ; Models, Molecular ; Mutation ; Protein Binding ; Protein Multimerization ; Protein Subunits/chemistry
Czasopismo naukowe
Tytuł :
Construction of Optimal SERS Hotspots Based on Capturing the Spike Receptor-Binding Domain (RBD) of SARS-CoV-2 for Highly Sensitive and Specific Detection by a Fish Model.
Autorzy :
Huang G; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.; Cancer Hospital, Chinese Academy of Sciences, Hefei 230031, China.
Zhao H; High Magnetic Field Science Center, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.
Li P; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.
Liu J; High Magnetic Field Science Center, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.
Chen S; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.
Ge M; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.
Qin M; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.
Zhou G; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.
Wang Y; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.
Li S; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.
Cheng Y; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.
Huang Q; Multiscale Research Institute of Complex Systems, Fudan University, Shanghai 201203, China.
Wang J; High Magnetic Field Science Center, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.
Wang H; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.; Cancer Hospital, Chinese Academy of Sciences, Hefei 230031, China.
Yang L; Institute of Health and Medicine Technology, and Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.; University of Science and Technology of China, Hefei 230026, China.; Cancer Hospital, Chinese Academy of Sciences, Hefei 230031, China.
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Źródło :
Analytical chemistry [Anal Chem] 2021 Dec 07; Vol. 93 (48), pp. 16086-16095. Date of Electronic Publication: 2021 Nov 03.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Metal Nanoparticles*
Spike Glycoprotein, Coronavirus/*chemistry
COVID-19 ; Gold ; Humans ; SARS-CoV-2
Czasopismo naukowe
Tytuł :
A distributed residue network permits conformational binding specificity in a conserved family of actin remodelers.
Autorzy :
Hwang T; Department of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Parker SS; Department of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, United States.
Hill SM; Department of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, United States.
Ilunga MW; Department of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Grant RA; Department of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Mouneimne G; Department of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, United States.
Keating AE; Department of Biology, Massachusetts Institute of Technology, Cambridge, United States.; Department of Biological Engineering and Koch Institue for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, United States.
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Źródło :
ELife [Elife] 2021 Dec 02; Vol. 10. Date of Electronic Publication: 2021 Dec 02.
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*
Actins/*metabolism
Cell Adhesion Molecules/*metabolism
Eye Proteins/*metabolism
Microfilament Proteins/*metabolism
Phosphoproteins/*metabolism
HEK293 Cells ; Humans ; MCF-7 Cells ; Molecular Conformation ; Protein Domains
Czasopismo naukowe
Tytuł :
Mapping Genome-wide Binding Sites of Prox1 in Mouse Cochlea Using the CUT&RUN Approach.
Autorzy :
Luo Z; Institute of Neuroscience, State Key Laboratory of Neuroscience, CAS Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences, Shanghai, 200031, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Zhang J; University of Chinese Academy of Sciences, Beijing, 100049, China.; State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China.
Qiao L; State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China.
Lu F; University of Chinese Academy of Sciences, Beijing, 100049, China. .; State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China. .
Liu Z; Institute of Neuroscience, State Key Laboratory of Neuroscience, CAS Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences, Shanghai, 200031, China. .; University of Chinese Academy of Sciences, Beijing, 100049, China. .; Shanghai Center for Brain Science and Brain-Inspired Intelligence Technology, Shanghai, 201210, China. .
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Źródło :
Neuroscience bulletin [Neurosci Bull] 2021 Dec; Vol. 37 (12), pp. 1703-1707. Date of Electronic Publication: 2021 Aug 05.
Typ publikacji :
Letter
MeSH Terms :
Binding Sites*
Cochlea*
Transcription Factors*
Homeodomain Proteins/*chemistry
Tumor Suppressor Proteins/*chemistry
Animals ; Mice
Opinia redakcyjna
Tytuł :
Photoactivatable ribonucleosides mark base-specific RNA-binding sites.
Autorzy :
Bae JW; Center for RNA Research, Institute for Basic Science, Seoul, 08826, Korea.; School of Biological Sciences, Seoul National University, Seoul, 08826, Korea.
Kim S; Seer Inc., Redwood City, CA, 94065, USA.
Kim VN; Center for RNA Research, Institute for Basic Science, Seoul, 08826, Korea. .; School of Biological Sciences, Seoul National University, Seoul, 08826, Korea. .
Kim JS; Center for RNA Research, Institute for Basic Science, Seoul, 08826, Korea. .; School of Biological Sciences, Seoul National University, Seoul, 08826, Korea. .
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Źródło :
Nature communications [Nat Commun] 2021 Oct 15; Vol. 12 (1), pp. 6026. Date of Electronic Publication: 2021 Oct 15.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
RNA/*metabolism
RNA-Binding Proteins/*metabolism
Ribonucleosides/*metabolism
Amino Acids/metabolism ; HeLa Cells ; Humans ; Protein Interaction Domains and Motifs ; Proteomics ; Tandem Mass Spectrometry ; Thiouridine/metabolism
Czasopismo naukowe
Tytuł :
Autoencoder-based detection of the residues involved in G protein-coupled receptor signaling.
Autorzy :
Tsuchiya Y; Artificial Intelligence Research Center, National Institute of Advanced Industrial Science and Technology, 2-4-7 Aomi, Koto-ku, Tokyo, 135-0064, Japan. .
Taneishi K; Center for Advanced Photonics, RIKEN, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Yonezawa Y; High Pressure Protein Research Center, Institute of Advanced Technology, Kindai University, 930 Nishimitani, Kinokawa, Wakayama, 649-6493, Japan.
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Źródło :
Scientific reports [Sci Rep] 2021 Oct 06; Vol. 11 (1), pp. 19867. Date of Electronic Publication: 2021 Oct 06.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Amino Acid Motifs*
Binding Sites*
Models, Molecular*
Protein Interaction Domains and Motifs*
Quantitative Structure-Activity Relationship*
Computational Biology/*methods
Receptors, G-Protein-Coupled/*chemistry
Humans ; Ligands ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; Receptors, G-Protein-Coupled/metabolism
Czasopismo naukowe
Tytuł :
Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability.
Autorzy :
Verma J; School of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. Electronic address: .
Subbarao N; School of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. Electronic address: .
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Źródło :
Virology [Virology] 2021 Sep; Vol. 561, pp. 107-116. Date of Electronic Publication: 2021 Jun 28.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Mutation*
Protein Interaction Domains and Motifs*
Angiotensin-Converting Enzyme 2/*chemistry
SARS-CoV-2/*genetics
Spike Glycoprotein, Coronavirus/*chemistry
Spike Glycoprotein, Coronavirus/*genetics
Amino Acids ; Angiotensin-Converting Enzyme 2/metabolism ; COVID-19/metabolism ; COVID-19/virology ; Humans ; Hydrogen Bonding ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Germline-Dependent Antibody Paratope States and Pairing Specific V H -V L Interface Dynamics.
Autorzy :
Fernández-Quintero ML; Department of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innsbruck, Austria.
Kroell KB; Department of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innsbruck, Austria.
Bacher LM; Department of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innsbruck, Austria.
Loeffler JR; Department of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innsbruck, Austria.
Quoika PK; Department of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innsbruck, Austria.
Georges G; Roche Pharma Research and Early Development, Large Molecule Research, Roche Innovation Center Munich, Penzberg, Germany.
Bujotzek A; Roche Pharma Research and Early Development, Large Molecule Research, Roche Innovation Center Munich, Penzberg, Germany.
Kettenberger H; Roche Pharma Research and Early Development, Large Molecule Research, Roche Innovation Center Munich, Penzberg, Germany.
Liedl KR; Department of General, Inorganic and Theoretical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innsbruck, Austria.
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Źródło :
Frontiers in immunology [Front Immunol] 2021 Aug 10; Vol. 12, pp. 675655. Date of Electronic Publication: 2021 Aug 10 (Print Publication: 2021).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites, Antibody*
Molecular Dynamics Simulation*
Germ Cells/*immunology
Complementarity Determining Regions/chemistry ; Humans ; Immunoglobulin Heavy Chains/chemistry ; Immunoglobulin Light Chains/chemistry ; Immunoglobulin Variable Region/chemistry ; Protein Conformation
Czasopismo naukowe
Tytuł :
The Crystal Structure of the Ca -ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation.
Autorzy :
Hansen SB; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Dyla M; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Neumann C; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Quistgaard EMH; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Andersen JL; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark.
Kjaergaard M; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark; Aarhus Institute of Advanced Studies (AIAS), Denmark; The Danish National Research Foundation Center for Proteins in Memory (PROMEMO), Denmark.
Nissen P; Department of Molecular Biology and Genetics, Aarhus University, Denmark; The Danish Research Institute for Translational Neuroscience (DANDRITE), Nordic EMBL Partnership for Molecular Medicine, Denmark; The Danish National Research Foundation Center for Proteins in Memory (PROMEMO), Denmark. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Aug 06; Vol. 433 (16), pp. 167015. Date of Electronic Publication: 2021 Apr 30.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Models, Molecular*
Protein Binding*
Protein Conformation*
Structure-Activity Relationship*
Listeria monocytogenes/*enzymology
Sarcoplasmic Reticulum Calcium-Transporting ATPases/*chemistry
Sarcoplasmic Reticulum Calcium-Transporting ATPases/*metabolism
Calcium/chemistry ; Calcium/metabolism ; Crystallography, X-Ray ; Phosphorylation
Czasopismo naukowe
Tytuł :
Cas4-Cas1 Is a Protospacer Adjacent Motif-Processing Factor Mediating Half-Site Spacer Integration During CRISPR Adaptation.
Autorzy :
Kieper SN; Department of Bionanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.; Kavli Institute of Nanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.
Almendros C; Department of Bionanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.; Kavli Institute of Nanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.
Haagsma AC; Department of Bionanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.; Kavli Institute of Nanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.
Barendregt A; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Utrecht, Netherlands; and Utrecht, Netherlands.; Netherlands Proteomics Center, Utrecht, Netherlands.
Heck AJR; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Utrecht, Netherlands; and Utrecht, Netherlands.; Netherlands Proteomics Center, Utrecht, Netherlands.
Brouns SJJ; Department of Bionanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.; Kavli Institute of Nanoscience, Delft University of Technology, Delft, Netherlands; Utrecht, Netherlands.
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Źródło :
The CRISPR journal [CRISPR J] 2021 Aug; Vol. 4 (4), pp. 536-548.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
CRISPR-Cas Systems*
Gene Editing*/methods
Nucleotide Motifs*
CRISPR-Associated Proteins/*metabolism
CRISPR-Associated Proteins/chemistry ; CRISPR-Associated Proteins/genetics ; DNA, Bacterial ; Gene Order ; Multiprotein Complexes ; Plasmids/chemistry ; Plasmids/genetics ; Protein Binding ; Protein Multimerization
Czasopismo naukowe
Tytuł :
Regulatory SNPs: Altered Transcription Factor Binding Sites Implicated in Complex Traits and Diseases.
Autorzy :
Degtyareva AO; Department of Molecular Genetic, Institute of Cytology and Genetics, 630090 Novosibirsk, Russia.
Antontseva EV; Department of Molecular Genetic, Institute of Cytology and Genetics, 630090 Novosibirsk, Russia.
Merkulova TI; Department of Molecular Genetic, Institute of Cytology and Genetics, 630090 Novosibirsk, Russia.; Department of Natural Sciences, Novosibirsk State University, 630090 Novosibirsk, Russia.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Jun 16; Vol. 22 (12). Date of Electronic Publication: 2021 Jun 16.
Typ publikacji :
Journal Article; Review
MeSH Terms :
Binding Sites*
Disease Susceptibility*
Gene Expression Regulation*
Multifactorial Inheritance*
Polymorphism, Single Nucleotide*
Transcription Factors/*metabolism
Alleles ; Genetic Predisposition to Disease ; Genome, Human ; Genome-Wide Association Study ; Genomics/methods ; Humans ; Quantitative Trait Loci ; Telomerase/genetics
Czasopismo naukowe
Tytuł :
Heterogeneous nuclear ribonucleoprotein E1 binds polycytosine DNA and monitors genome integrity.
Autorzy :
Mohanty BK; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Karam JA; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Howley BV; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Dalton AC; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Grelet S; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.; Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, USA.
Dincman T; Division of Hematology and Oncology, Department of Medicine, Medical University of South Carolina, Charleston, SC, USA.
Streitfeld WS; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Yoon JH; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Balakrishnan L; Department of Biology, School of Science, Indiana University Purdue University Indianapolis, Indianapolis, IN, USA.
Chazin WJ; Departments of Biochemistry and Chemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN, USA.
Long DT; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Howe PH; Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA .; Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, USA.
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Źródło :
Life science alliance [Life Sci Alliance] 2021 Jul 16; Vol. 4 (9). Date of Electronic Publication: 2021 Jul 16 (Print Publication: 2021).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Genomic Instability*
Poly C*/chemistry
DNA/*metabolism
DNA-Binding Proteins/*metabolism
RNA-Binding Proteins/*metabolism
Animals ; Base Sequence ; DNA/chemistry ; DNA/genetics ; DNA Damage/drug effects ; DNA Damage/radiation effects ; Humans ; Mice ; Models, Biological ; Mutation ; Mutation Rate ; Nucleic Acid Conformation ; Nucleotide Motifs ; Protein Binding ; Signal Transduction
Czasopismo naukowe
Tytuł :
An anti-HER2 nanobody binds to its antigen HER2 via two independent paratopes.
Autorzy :
Ubbiali D; Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle, Germany.
Orlando M; Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milano, Italy; Department of Biotechnology and Life Sciences, University of Insubria, Via J. H. Dunant 3, 21100 Varese, Italy.
Kovačič M; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, 1001 Ljubljana, Slovenia.
Iacobucci C; Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle, Germany.
Semrau MS; Structural Biology Lab, Elettra Sincrotrone Trieste S.C.p.A., 34149, Basovizza, Trieste, Italy; CIBIO, Centre for Integrative Biology, University of Trento, via Sommarive 9, Povo 38123, Italy.
Bajc G; Department of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia.
Fortuna S; Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy.
Ilc G; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, 1001 Ljubljana, Slovenia.
Medagli B; Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy.
Oloketuyi S; Lab of Environmental and Life Sciences, University of Nova Gorica, Vipavska cesta 13, 5000 Rožna Dolina, Nova Gorica, Slovenia.
Storici P; Structural Biology Lab, Elettra Sincrotrone Trieste S.C.p.A., 34149, Basovizza, Trieste, Italy.
Sinz A; Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle, Germany.
Grandori R; Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milano, Italy.
de Marco A; Lab of Environmental and Life Sciences, University of Nova Gorica, Vipavska cesta 13, 5000 Rožna Dolina, Nova Gorica, Slovenia. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2021 Jul 01; Vol. 182, pp. 502-511. Date of Electronic Publication: 2021 Apr 14.
Typ publikacji :
Journal Article
MeSH Terms :
Binding Sites, Antibody*
Receptor, ErbB-2/*chemistry
Single-Chain Antibodies/*chemistry
Humans ; Molecular Docking Simulation ; Mutation ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/immunology ; Protein Binding ; Receptor, ErbB-2/immunology ; Single-Chain Antibodies/genetics ; Single-Chain Antibodies/immunology
Czasopismo naukowe
Tytuł :
Mutagenic Analysis of the Putative ABCC6 Substrate-Binding Cavity Using a New Homology Model.
Autorzy :
Szeri F; Department of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.; Research Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.
Corradi V; Department of Biological Sciences and Centre for Molecular Simulation, University of Calgary, Calgary, AB T2N 1N4, Canada.
Niaziorimi F; Department of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Donnelly S; Department of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Conseil G; Department of Pathology and Molecular Medicine, Queen's University, Kingston, ON K7L 3N6, Canada.
Cole SPC; Department of Pathology and Molecular Medicine, Queen's University, Kingston, ON K7L 3N6, Canada.
Tieleman DP; Department of Biological Sciences and Centre for Molecular Simulation, University of Calgary, Calgary, AB T2N 1N4, Canada.
van de Wetering K; Department of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Jun 27; Vol. 22 (13). Date of Electronic Publication: 2021 Jun 27.
Typ publikacji :
Journal Article
MeSH Terms :
Binding Sites*
Models, Molecular*
Mutation*
Multidrug Resistance-Associated Proteins/*chemistry
Multidrug Resistance-Associated Proteins/*genetics
Adenosine Triphosphate/chemistry ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Amino Acids/chemistry ; Animals ; Ligands ; Molecular Conformation ; Multidrug Resistance-Associated Proteins/metabolism ; Mutagenesis ; Protein Binding ; Protein Transport ; Rats ; Structure-Activity Relationship ; Substrate Specificity
Czasopismo naukowe
Tytuł :
' All That Glitters Is Not Gold ': High-Resolution Crystal Structures of Ligand-Protein Complexes Need Not Always Represent Confident Binding Poses.
Autorzy :
Chakraborti S; Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560012, Karnataka, India.
Hatti K; Wellcome Centre for Anti-Infectives Research, Drug Discovery Unit, School of Life Sciences, University of Dundee, Dow Street, Dundee DDI 5EH, UK.
Srinivasan N; Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560012, Karnataka, India.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Jun 25; Vol. 22 (13). Date of Electronic Publication: 2021 Jun 25.
Typ publikacji :
Journal Article
MeSH Terms :
Binding Sites*
Ligands*
Models, Molecular*
Macromolecular Substances/*chemistry
Proteins/*chemistry
Crystallography, X-Ray ; Macromolecular Substances/metabolism ; Molecular Conformation ; Protein Binding ; Proteins/metabolism
Czasopismo naukowe
Tytuł :
High-resolution asymmetric structure of a Fab-virus complex reveals overlap with the receptor binding site.
Autorzy :
Goetschius DJ; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802.
Hartmann SR; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802.
Organtini LJ; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802.
Callaway H; Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.
Huang K; Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.
Bator CM; Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA 16802.
Ashley RE; Department of Medicine, Penn State University College of Medicine, The Pennsylvania State University, Hershey, PA 17033.
Makhov AM; Department of Structural Biology, University of Pittsburgh School of Medicine, University of Pittsburgh, Pittsburgh, PA 15260.
Conway JF; Department of Structural Biology, University of Pittsburgh School of Medicine, University of Pittsburgh, Pittsburgh, PA 15260.
Parrish CR; Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.
Hafenstein SL; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802; .; Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA 16802.; Department of Medicine, Penn State University College of Medicine, The Pennsylvania State University, Hershey, PA 17033.
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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] 2021 Jun 08; Vol. 118 (23).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Antibodies, Viral/*chemistry
Capsid/*metabolism
Immunoglobulin Fab Fragments/*chemistry
Parvovirus, Canine/*physiology
Protein Binding/*physiology
Animals ; Antibodies, Viral/immunology ; Antigens/metabolism ; Cryoelectron Microscopy ; Dogs ; Epitopes/genetics ; Epitopes/immunology ; Mutation ; Protein Domains
Czasopismo naukowe
Tytuł :
High throughput screening identifies SOX2 as a super pioneer factor that inhibits DNA methylation maintenance at its binding sites.
Autorzy :
Vanzan L; Department of Genetic Medicine and Development, University of Geneva Medical School, Geneva, Switzerland.; Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
Soldati H; Department of Genetic Medicine and Development, University of Geneva Medical School, Geneva, Switzerland.
Ythier V; Department of Genetic Medicine and Development, University of Geneva Medical School, Geneva, Switzerland.; Diagnostic Department, Clinical Pathology Division, University Hospital of Geneva, Geneva, Switzerland.
Anand S; Department of Genetic Medicine and Development, University of Geneva Medical School, Geneva, Switzerland.; Department of Informatics, Systems and Communications (DISCo), University of Milano-Bicocca, Milan, Italy.
Braun SMG; Department of Genetic Medicine and Development, University of Geneva Medical School, Geneva, Switzerland.
Francis N; Institut de Recherches Cliniques de Montréal (IRCM) and Département de Biochimie et Médecine Moléculaire, Université de Montréal, Montréal, Canada.
Murr R; Department of Genetic Medicine and Development, University of Geneva Medical School, Geneva, Switzerland. .; Institute for Genetics and Genomics of Geneva (iGE3), University of Geneva, Geneva, Switzerland. .
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Źródło :
Nature communications [Nat Commun] 2021 Jun 07; Vol. 12 (1), pp. 3337. Date of Electronic Publication: 2021 Jun 07.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
DNA Methylation*
High-Throughput Screening Assays*
DNA/*metabolism
SOXB1 Transcription Factors/*genetics
SOXB1 Transcription Factors/*metabolism
Animals ; Chromatin ; DNA Demethylation ; DNA Replication ; Epigenomics ; Gene Expression ; Mice ; Nucleosomes ; Octamer Transcription Factor-3/metabolism ; Protein Binding ; RNA, Small Interfering/genetics ; Sf9 Cells ; Transcription Factors/metabolism
Czasopismo naukowe
Tytuł :
SARS-CoV-2 receptor binding domain fusion protein efficiently neutralizes virus infection.
Autorzy :
Chaouat AE; The Concern Foundation Laboratories at the Lautenberg Center for Immunology and Cancer Research, Institute for Medical Research Israel Canada (IMRIC), The Hebrew University Hadassah Medical School, Jerusalem, Israel.
Achdout H; Department of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona, Israel.
Kol I; The Concern Foundation Laboratories at the Lautenberg Center for Immunology and Cancer Research, Institute for Medical Research Israel Canada (IMRIC), The Hebrew University Hadassah Medical School, Jerusalem, Israel.
Berhani O; The Concern Foundation Laboratories at the Lautenberg Center for Immunology and Cancer Research, Institute for Medical Research Israel Canada (IMRIC), The Hebrew University Hadassah Medical School, Jerusalem, Israel.
Roi G; The Concern Foundation Laboratories at the Lautenberg Center for Immunology and Cancer Research, Institute for Medical Research Israel Canada (IMRIC), The Hebrew University Hadassah Medical School, Jerusalem, Israel.
Vitner EB; Department of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona, Israel.
Melamed S; Department of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona, Israel.
Politi B; Department of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona, Israel.
Zahavy E; Department of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness Ziona, Israel.
Brizic I; Center for Proteomics, Faculty of Medicine, University of Rijeka, Rijeka, Croatia.
Lenac Rovis T; Center for Proteomics, Faculty of Medicine, University of Rijeka, Rijeka, Croatia.
Alfi O; Lautenberg Center for General and Tumor Immunology, The Hebrew University Faculty of Medicine, Jerusalem, Israel.; Clinical Virology Unit, Hadassah Hebrew University Medical Center, Jerusalem, Israel.
Wolf D; Lautenberg Center for General and Tumor Immunology, The Hebrew University Faculty of Medicine, Jerusalem, Israel.; Clinical Virology Unit, Hadassah Hebrew University Medical Center, Jerusalem, Israel.
Jonjic S; Center for Proteomics, Faculty of Medicine, University of Rijeka, Rijeka, Croatia.
Israely T; Department of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona, Israel.
Mandelboim O; The Concern Foundation Laboratories at the Lautenberg Center for Immunology and Cancer Research, Institute for Medical Research Israel Canada (IMRIC), The Hebrew University Hadassah Medical School, Jerusalem, Israel.
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Źródło :
PLoS pathogens [PLoS Pathog] 2021 Dec 20; Vol. 17 (12), pp. e1010175. Date of Electronic Publication: 2021 Dec 20 (Print Publication: 2021).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Domains*
Angiotensin-Converting Enzyme 2/*antagonists & inhibitors
Immunoglobulin Fc Fragments/*metabolism
Immunoglobulin G/*metabolism
Recombinant Fusion Proteins/*metabolism
SARS-CoV-2/*metabolism
Angiotensin-Converting Enzyme 2/metabolism ; Animals ; Binding Sites ; Binding Sites, Antibody ; COVID-19/prevention & control ; Chlorocebus aethiops ; Female ; HEK293 Cells ; Humans ; Immunoglobulin Fc Fragments/therapeutic use ; Immunoglobulin G/therapeutic use ; Mice, Transgenic ; Neutralization Tests ; Protein Binding ; Recombinant Fusion Proteins/therapeutic use ; SARS-CoV-2/drug effects ; Vero Cells
Czasopismo naukowe
Tytuł :
Chromatin occupancy and target genes of the haematopoietic master transcription factor MYB.
Autorzy :
Lemma RB; Department of Biosciences, University of Oslo, Blindern, PO Box 1066, 0316, Oslo, Norway.; Centre for Molecular Medicine Norway (NCMM), Nordic EMBL Partnership, University of Oslo, 0318, Oslo, Norway.
Ledsaak M; Department of Biosciences, University of Oslo, Blindern, PO Box 1066, 0316, Oslo, Norway.; Institute of Basic Medical Sciences, Department of Molecular Medicine, University of Oslo, Blindern, PO Box 1112, 0317, Oslo, Norway.
Fuglerud BM; Department of Biosciences, University of Oslo, Blindern, PO Box 1066, 0316, Oslo, Norway.; Terry Fox Laboratory, BC Cancer, Vancouver, BC, V5Z 1L3, Canada.; Department of Medical Genetics, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada.
Sandve GK; Department of Informatics, University of Oslo, Blindern, PO Box 1080, 0371, Oslo, Norway.
Eskeland R; Department of Biosciences, University of Oslo, Blindern, PO Box 1066, 0316, Oslo, Norway.; Institute of Basic Medical Sciences, Department of Molecular Medicine, University of Oslo, Blindern, PO Box 1112, 0317, Oslo, Norway.; Centre for Cancer Cell Reprogramming, Institute of Clinical Medicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Gabrielsen OS; Department of Biosciences, University of Oslo, Blindern, PO Box 1066, 0316, Oslo, Norway. .
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Źródło :
Scientific reports [Sci Rep] 2021 Apr 26; Vol. 11 (1), pp. 9008. Date of Electronic Publication: 2021 Apr 26.
Typ publikacji :
Journal Article
MeSH Terms :
Binding Sites*
Gene Expression Regulation*
Chromatin/*genetics
Chromatin/*metabolism
Hematopoiesis/*genetics
Proto-Oncogene Proteins c-myb/*metabolism
Cell Differentiation/genetics ; Chromatin Assembly and Disassembly ; Chromatin Immunoprecipitation ; Computational Biology/methods ; Databases, Genetic ; Epigenesis, Genetic ; Epigenomics/methods ; Gene Expression Profiling ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/metabolism ; Humans ; K562 Cells ; Models, Biological ; Nucleotide Motifs ; Promoter Regions, Genetic ; Protein Binding ; Transcriptome
Czasopismo naukowe

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