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Tytuł:
Cannabidiol binding and negative allosteric modulation at the cannabinoid type 1 receptor in the presence of delta-9-tetrahydrocannabinol: An In Silico study.
Autorzy:
Chung H; Pharmacy Department, Faculty of Chemistry, Pontificia Universidad Católica de Chile, Santiago, Chile.
Fierro A; Organic Chemistry Department, Faculty of Chemistry, Pontificia Universidad Católica de Chile, Santiago, Chile.
Pessoa-Mahana CD; Pharmacy Department, Faculty of Chemistry, Pontificia Universidad Católica de Chile, Santiago, Chile.
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Źródło:
PloS one [PLoS One] 2019 Jul 23; Vol. 14 (7), pp. e0220025. Date of Electronic Publication: 2019 Jul 23 (Print Publication: 2019).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Allosteric Site*
Molecular Docking Simulation*
Cannabidiol/*metabolism
Cannabinoid Receptor Agonists/*metabolism
Dronabinol/*metabolism
Receptor, Cannabinoid, CB1/*chemistry
Allosteric Regulation ; Cannabidiol/chemistry ; Cannabinoid Receptor Agonists/chemistry ; Dronabinol/chemistry ; Humans ; Protein Binding ; Receptor, Cannabinoid, CB1/metabolism
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Allosteric binding sites in Rab11 for potential drug candidates.
Autorzy:
Kumar AP; Department of Chemistry, College of Arts and Sciences, Khalifa University of Science and Technology, Abu Dhabi, United Arab Emirates.
Lukman S; Department of Chemistry, College of Arts and Sciences, Khalifa University of Science and Technology, Abu Dhabi, United Arab Emirates.
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Źródło:
PloS one [PLoS One] 2018 Jun 06; Vol. 13 (6), pp. e0198632. Date of Electronic Publication: 2018 Jun 06 (Print Publication: 2018).
Typ publikacji:
Journal Article
MeSH Terms:
Allosteric Regulation*
Allosteric Site*
Molecular Docking Simulation*
rab GTP-Binding Proteins/*chemistry
Crystallography, X-Ray ; Guanosine Diphosphate/chemistry ; Guanosine Triphosphate/chemistry ; Ligands ; Protein Binding ; Protein Structure, Tertiary
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
LRRK2 dynamics analysis identifies allosteric control of the crosstalk between its catalytic domains.
Autorzy:
Weng JH; Department of Pharmacology, University of California, San Diego, California, United States of America.
Aoto PC; Department of Pharmacology, University of California, San Diego, California, United States of America.
Lorenz R; Department of Biochemistry, University of Kassel, Kassel, Germany.
Wu J; Department of Pharmacology, University of California, San Diego, California, United States of America.
Schmidt SH; Department of Biochemistry, University of Kassel, Kassel, Germany.
Manschwetus JT; Department of Biochemistry, University of Kassel, Kassel, Germany.
Kaila-Sharma P; Department of Pharmacology, University of California, San Diego, California, United States of America.
Silletti S; Department of Chemistry and Biochemistry, University of California, San Diego, California, United States of America.
Mathea S; Institute for Pharmaceutical Chemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.
Chatterjee D; Institute for Pharmaceutical Chemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.
Knapp S; Institute for Pharmaceutical Chemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.
Herberg FW; Department of Biochemistry, University of Kassel, Kassel, Germany.
Taylor SS; Department of Pharmacology, University of California, San Diego, California, United States of America.
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Źródło:
PLoS biology [PLoS Biol] 2022 Feb 22; Vol. 20 (2), pp. e3001427. Date of Electronic Publication: 2022 Feb 22 (Print Publication: 2022).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms:
Catalytic Domain*
Molecular Dynamics Simulation*
Protein Conformation*
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/*chemistry
Allosteric Regulation ; Allosteric Site ; Deuterium Exchange Measurement/methods ; Humans ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/genetics ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/metabolism ; Mass Spectrometry/methods ; Mutation ; Protein Binding
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Known allosteric proteins have central roles in genetic disease.
Autorzy:
Abrusán G; Cambridge Baker Systems Genomics Initiative, Department of Public Health and Primary Care, School of Medicine, University of Cambridge, Cambridge, United Kingdom.
Ascher DB; Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.; Structural Biology and Bioinformatics, Department of Biochemistry, Bio21 Institute, University of Melbourne, Melbourne, Australia.; Computational Biology and Clinical Informatics, Baker Heart and Diabetes Institute, Melbourne, Australia.
Inouye M; Cambridge Baker Systems Genomics Initiative, Department of Public Health and Primary Care, School of Medicine, University of Cambridge, Cambridge, United Kingdom.; Cambridge Baker Systems Genomics Initiative, Baker Heart and Diabetes Institute, Melbourne, Australia.; British Heart Foundation Cardiovascular Epidemiology Unit, Department of Public Health and Primary Care, University of Cambridge, Cambridge, United Kingdom.; British Heart Foundation Centre of Research Excellence, University of Cambridge, Cambridge, United Kingdom.; Health Data Research UK Cambridge, Wellcome Genome Campus and University of Cambridge, Cambridge, United Kingdom.; The Alan Turing Institute, London, United Kingdom.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2022 Feb 09; Vol. 18 (2), pp. e1009806. Date of Electronic Publication: 2022 Feb 09 (Print Publication: 2022).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Genome-Wide Association Study*
Proteins*/chemistry
Allosteric Regulation/genetics ; Allosteric Site ; Catalytic Domain
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Mapping major SARS-CoV-2 drug targets and assessment of druggability using computational fragment screening: Identification of an allosteric small-molecule binding site on the Nsp13 helicase.
Autorzy:
Freidel MR; Department of Pharmaceutical Sciences, College of Pharmacy, Thomas Jefferson University, Philadelphia, Pennsylvania, United States of America.
Armen RS; Department of Pharmaceutical Sciences, College of Pharmacy, Thomas Jefferson University, Philadelphia, Pennsylvania, United States of America.
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Źródło:
PloS one [PLoS One] 2021 Feb 17; Vol. 16 (2), pp. e0246181. Date of Electronic Publication: 2021 Feb 17 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms:
Antiviral Agents/*pharmacology
COVID-19/*virology
Coronavirus RNA-Dependent RNA Polymerase/*metabolism
Methyltransferases/*metabolism
RNA Helicases/*metabolism
SARS-CoV-2/*drug effects
Viral Nonstructural Proteins/*metabolism
Allosteric Site ; Binding Sites ; COVID-19/metabolism ; Computational Biology/methods ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/chemistry ; Coronavirus 3C Proteases/metabolism ; Coronavirus RNA-Dependent RNA Polymerase/antagonists & inhibitors ; Coronavirus RNA-Dependent RNA Polymerase/chemistry ; Humans ; Methyltransferases/antagonists & inhibitors ; Methyltransferases/chemistry ; Models, Molecular ; Molecular Targeted Therapy ; Protein Binding ; RNA Helicases/antagonists & inhibitors ; RNA Helicases/chemistry ; RNA-Dependent RNA Polymerase/metabolism ; SARS-CoV-2/metabolism ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/chemistry ; Virus Replication/drug effects ; COVID-19 Drug Treatment
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknieSzczegóły
Tytuł:
State-dependent protein-lipid interactions of a pentameric ligand-gated ion channel in a neuronal membrane.
Autorzy:
Dämgen MA; Structural Bioinformatics and Computational Biochemistry, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Biggin PC; Structural Bioinformatics and Computational Biochemistry, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2021 Feb 11; Vol. 17 (2), pp. e1007856. Date of Electronic Publication: 2021 Feb 11 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Models, Neurological*
Ligand-Gated Ion Channels/*metabolism
Neurons/*metabolism
Allosteric Site ; Animals ; Binding Sites ; Cholesterol/chemistry ; Cholesterol/metabolism ; Computational Biology ; Humans ; Ivermectin/chemistry ; Ivermectin/metabolism ; Ligand-Gated Ion Channels/chemistry ; Membrane Lipids/chemistry ; Membrane Lipids/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Molecular Dynamics Simulation ; Protein Binding ; Protein Domains ; Protein Structure, Quaternary ; Receptors, Glycine/chemistry ; Receptors, Glycine/metabolism
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Dynamic Allostery of the Catabolite Activator Protein Revealed by Interatomic Forces.
Autorzy:
Louet M; Heidelberg Institutes for Theoretical Studies gGmbH, Heidelberg, Germany.
Seifert C; Heidelberg Institutes for Theoretical Studies gGmbH, Heidelberg, Germany.
Hensen U; Eidgenössische Technische Hochschule Zürich, Department of Biosystem Science and Engineering, Basel, Switzerland.
Gräter F; Heidelberg Institutes for Theoretical Studies gGmbH, Heidelberg, Germany; CAS-MPG Partner Institute and Key Laboratory for Computational Biology, Shanghai, China.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2015 Aug 05; Vol. 11 (8), pp. e1004358. Date of Electronic Publication: 2015 Aug 05 (Print Publication: 2015).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Allosteric Site*
Cyclic AMP Receptor Protein/*chemistry
Cyclic AMP Receptor Protein/*metabolism
Entropy ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Molecular Dynamics Simulation ; Nuclear Magnetic Resonance, Biomolecular ; Principal Component Analysis ; Protein Binding
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknieSzczegóły
Tytuł:
The structural basis of ATP as an allosteric modulator.
Autorzy:
Lu S; Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai JiaoTong University, School of Medicine, Shanghai, China.
Huang W; Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai JiaoTong University, School of Medicine, Shanghai, China.
Wang Q; Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai JiaoTong University, School of Medicine, Shanghai, China.
Shen Q; Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai JiaoTong University, School of Medicine, Shanghai, China.
Li S; Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai JiaoTong University, School of Medicine, Shanghai, China.
Nussinov R; Cancer and Inflammation Program, Leidos Biomedical Research, Inc., Frederick National Laboratory, National Cancer Institute, Frederick, Maryland, United States of America; Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Sackler Institute of Molecular Medicine, Tel Aviv University, Tel Aviv, Israel.
Zhang J; Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai JiaoTong University, School of Medicine, Shanghai, China; Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2014 Sep 11; Vol. 10 (9), pp. e1003831. Date of Electronic Publication: 2014 Sep 11 (Print Publication: 2014).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't
MeSH Terms:
Allosteric Site*
Adenosine Triphosphate/*chemistry
Adenosine Triphosphate/*metabolism
Enzymes/*chemistry
Enzymes/*metabolism
Bacteria ; Fungi ; Humans ; Molecular Dynamics Simulation ; Proteins/chemistry ; Proteins/metabolism ; Signal Transduction ; Thermodynamics
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknieSzczegóły
Tytuł:
Direct coupling analysis of epistasis in allosteric materials.
Autorzy:
Bravi B; Institute of Physics, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Ravasio R; Institute of Physics, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Brito C; Instituto de Fìsica, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil.
Wyart M; Institute of Physics, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2020 Mar 02; Vol. 16 (3), pp. e1007630. Date of Electronic Publication: 2020 Mar 02 (Print Publication: 2020).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Allosteric Site/*genetics
Computational Biology/*methods
Epistasis, Genetic/*genetics
Allosteric Regulation/physiology ; Amino Acids/genetics ; Animals ; Catalytic Domain/physiology ; Computer Simulation ; Drug Design ; Humans ; Ligands ; Models, Molecular ; Models, Theoretical ; Protein Conformation ; Proteins/chemistry
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Long-range correlation in protein dynamics: Confirmation by structural data and normal mode analysis.
Autorzy:
Tang QY; Center for Complex Systems Biology, Universal Biology Institute, University of Tokyo, Tokyo, Japan.
Kaneko K; Center for Complex Systems Biology, Universal Biology Institute, University of Tokyo, Tokyo, Japan.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2020 Feb 13; Vol. 16 (2), pp. e1007670. Date of Electronic Publication: 2020 Feb 13 (Print Publication: 2020).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Conformation*
Computational Biology/*methods
Proteins/*chemistry
Algorithms ; Allosteric Site ; Catalysis ; Computer Simulation ; Crystallography, X-Ray ; Databases, Protein ; Elasticity ; Fractals ; HSP90 Heat-Shock Proteins/chemistry ; Humans ; Imaging, Three-Dimensional ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Normal Distribution ; Protein Interaction Mapping ; Structure-Activity Relationship
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Structural analysis of the manganese transport regulator MntR from Bacillus halodurans in apo and manganese bound forms.
Autorzy:
Lee MY; Department of Life Science, Dongguk University-Seoul, Ilsandong-gu, Goyang-si, Gyeonggi-do, Republic of Korea.
Lee DW; Department of Life Science, Dongguk University-Seoul, Ilsandong-gu, Goyang-si, Gyeonggi-do, Republic of Korea.
Joo HK; Department of Life Science, Dongguk University-Seoul, Ilsandong-gu, Goyang-si, Gyeonggi-do, Republic of Korea.
Jeong KH; Department of Life Science, Dongguk University-Seoul, Ilsandong-gu, Goyang-si, Gyeonggi-do, Republic of Korea.
Lee JY; Department of Life Science, Dongguk University-Seoul, Ilsandong-gu, Goyang-si, Gyeonggi-do, Republic of Korea.
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Źródło:
PloS one [PLoS One] 2019 Nov 18; Vol. 14 (11), pp. e0224689. Date of Electronic Publication: 2019 Nov 18 (Print Publication: 2019).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Bacillus/*ultrastructure
Bacterial Proteins/*ultrastructure
Manganese/*metabolism
Repressor Proteins/*ultrastructure
Allosteric Site ; Amino Acid Sequence ; Bacillus/metabolism ; Bacterial Proteins/isolation & purification ; Bacterial Proteins/metabolism ; Crystallography, X-Ray ; Models, Molecular ; Protein Domains ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Recombinant Proteins/ultrastructure ; Repressor Proteins/isolation & purification ; Repressor Proteins/metabolism ; Sequence Alignment
SCR Organism:
Bacillus halodurans
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Identification of a potential allosteric site of Golgi α-mannosidase II using computer-aided drug design.
Autorzy:
Irsheid L; Institute of Pharmacy and Biochemistry, University of Mainz, Mainz, Germany.
Wehler T; Institute of Pharmacy and Biochemistry, University of Mainz, Mainz, Germany.; Department of Biomedicine, University of Bergen, Bergen, Norway.
Borek C; Institute of Pharmacy and Biochemistry, University of Mainz, Mainz, Germany.
Kiefer W; Institute of Pharmacy and Biochemistry, University of Mainz, Mainz, Germany.
Brenk R; Department of Biomedicine, University of Bergen, Bergen, Norway.
Ortiz-Soto ME; Institute of Organic Chemistry, University of Würzburg, Würzburg, Germany.
Seibel J; Institute of Organic Chemistry, University of Würzburg, Würzburg, Germany.
Schirmeister T; Institute of Pharmacy and Biochemistry, University of Mainz, Mainz, Germany.
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Źródło:
PloS one [PLoS One] 2019 May 08; Vol. 14 (5), pp. e0216132. Date of Electronic Publication: 2019 May 08 (Print Publication: 2019).
Typ publikacji:
Journal Article
MeSH Terms:
Drug Design*
Golgi Apparatus/*enzymology
alpha-Mannosidase/*ultrastructure
Allosteric Site ; Animals ; Binding Sites ; Cloning, Molecular ; Drosophila melanogaster/enzymology ; Molecular Docking Simulation ; Protein Structure, Quaternary ; Recombinant Proteins
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Identifying cytochrome p450 functional networks and their allosteric regulatory elements.
Autorzy:
Liu J; Department of Defense Biotechnology High Performance Computing Software Applications Institute, Telemedicine and Advanced Technology Research Center, United States Army Medical Research and Materiel Command, Fort Detrick, Maryland, United States of America.
Tawa GJ
Wallqvist A
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Źródło:
PloS one [PLoS One] 2013 Dec 03; Vol. 8 (12), pp. e81980. Date of Electronic Publication: 2013 Dec 03 (Print Publication: 2013).
Typ publikacji:
Journal Article
MeSH Terms:
Allosteric Site*
Molecular Dynamics Simulation*
Computational Biology/*methods
Cytochrome P-450 Enzyme System/*chemistry
Cytochrome P-450 Enzyme System/*metabolism
Benzoflavones/metabolism ; Benzoflavones/pharmacology ; Biocatalysis ; Cell Membrane/metabolism ; Cytochrome P-450 Enzyme System/genetics ; Evolution, Molecular ; Heme/metabolism ; Mutation ; Oxazines/metabolism ; Protein Conformation ; Temperature
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknieSzczegóły
Tytuł:
In vitro pharmacological characterization of RXFP3 allosterism: an example of probe dependency.
Autorzy:
Alvarez-Jaimes L; Janssen Pharmaceutical Companies of Johnson & Johnson, San Diego, California, United States of America.
Sutton SW
Nepomuceno D
Motley ST
Cik M
Stocking E
Shoblock J
Bonaventure P
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Źródło:
PloS one [PLoS One] 2012; Vol. 7 (2), pp. e30792. Date of Electronic Publication: 2012 Feb 07.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Allosteric Site*
Receptors, G-Protein-Coupled/*metabolism
Allosteric Regulation ; Calcium Signaling ; Cell Line ; Cyclic AMP/metabolism ; Humans ; Molecular Probes ; Receptors, G-Protein-Coupled/chemistry ; Relaxin
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknieSzczegóły
Tytuł:
Identification of the allosteric regulatory site of insulysin.
Autorzy:
Noinaj N; Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, Kentucky, United States of America.
Bhasin SK
Song ES
Scoggin KE
Juliano MA
Juliano L
Hersh LB
Rodgers DW
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Źródło:
PloS one [PLoS One] 2011; Vol. 6 (6), pp. e20864. Date of Electronic Publication: 2011 Jun 24.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms:
Allosteric Site*
Insulysin/*chemistry
Insulysin/*metabolism
Adenosine Triphosphate/analogs & derivatives ; Adenosine Triphosphate/metabolism ; Allosteric Regulation ; Animals ; Crystallography, X-Ray ; Kinetics ; Ligands ; Mass Spectrometry ; Models, Molecular ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Mutation/genetics ; Protein Binding ; Protein Multimerization ; Protein Structure, Secondary ; Rats ; Spectrometry, Fluorescence
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknieSzczegóły
Tytuł:
Identification of a negative allosteric site on human α4β2 and α3β4 neuronal nicotinic acetylcholine receptors.
Autorzy:
Pavlovicz RE; Biophysics Program, Ohio State University, Columbus, Ohio, United States of America.
Henderson BJ
Bonnell AB
Boyd RT
McKay DB
Li C
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Źródło:
PloS one [PLoS One] 2011; Vol. 6 (9), pp. e24949. Date of Electronic Publication: 2011 Sep 15.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms:
Allosteric Site*
Receptors, Nicotinic/*metabolism
Calcium/metabolism ; Cells, Cultured ; Humans ; Kidney/cytology ; Kidney/metabolism ; Models, Molecular ; Mutagenesis, Site-Directed ; Mutation/genetics ; Nicotinic Agonists/metabolism ; Nicotinic Antagonists/metabolism ; Protein Conformation ; Receptors, Nicotinic/chemistry ; Receptors, Nicotinic/genetics ; Structure-Activity Relationship
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknieSzczegóły
Tytuł:
A DNA aptamer reveals an allosteric site for inhibition in metallo-β-lactamases.
Autorzy:
Khan NH; Department of Chemistry & Biochemistry, Texas Tech University, Lubbock, Texas, United States of America.
Bui AA; Department of Chemistry & Biochemistry, Texas Tech University, Lubbock, Texas, United States of America.
Xiao Y; Department of Chemistry & Biochemistry, Texas Tech University, Lubbock, Texas, United States of America.
Sutton RB; Department of Cell Physiology & Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, Texas, United States of America.
Shaw RW; Department of Chemistry & Biochemistry, Texas Tech University, Lubbock, Texas, United States of America.
Wylie BJ; Department of Chemistry & Biochemistry, Texas Tech University, Lubbock, Texas, United States of America.
Latham MP; Department of Chemistry & Biochemistry, Texas Tech University, Lubbock, Texas, United States of America.
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Źródło:
PloS one [PLoS One] 2019 Apr 22; Vol. 14 (4), pp. e0214440. Date of Electronic Publication: 2019 Apr 22 (Print Publication: 2019).
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:
Anti-Bacterial Agents/*pharmacology
Aptamers, Nucleotide/*chemistry
beta-Lactamase Inhibitors/*pharmacology
beta-Lactamases/*metabolism
Allosteric Site ; Bacillus cereus/drug effects ; Bacillus cereus/enzymology ; Catalysis ; Catalytic Domain ; Crystallography, X-Ray ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular Docking Simulation ; Mutagenesis, Site-Directed ; Protein Binding ; Substrate Specificity ; beta-Lactamases/genetics
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Analysis of equilibrium binding of an orthosteric tracer and two allosteric modulators.
Autorzy:
Jakubík J; Department of Neurochemistry, Institute of Physiology CAS, Prague, Czech Republic.
Randáková A; Department of Neurochemistry, Institute of Physiology CAS, Prague, Czech Republic.
El-Fakahany EE; Department of Experimental and Clinical Pharmacology, University of Minnesota College of Pharmacy, Minneapolis, MN, United States of America.
Doležal V; Department of Neurochemistry, Institute of Physiology CAS, Prague, Czech Republic.
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Źródło:
PloS one [PLoS One] 2019 Mar 27; Vol. 14 (3), pp. e0214255. Date of Electronic Publication: 2019 Mar 27 (Print Publication: 2019).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Models, Chemical*
Allosteric Regulation ; Allosteric Site ; Kinetics ; Ligands
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Allosteric mechanism of the circadian protein Vivid resolved through Markov state model and machine learning analysis.
Autorzy:
Zhou H; Department of Chemistry, Center for Scientific Computation, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, Texas, United States of America.
Dong Z; Department of Chemistry, Center for Scientific Computation, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, Texas, United States of America.
Verkhivker G; Graduate Program in Computational and Data Sciences, Schmid College of Science and Technology, Chapman University, Orange, California, United States of America.; Chapman University School of Pharmacy, Irvine, California, United States of America.
Zoltowski BD; Department of Chemistry, Center for Scientific Computation, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, Texas, United States of America.
Tao P; Department of Chemistry, Center for Scientific Computation, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, Texas, United States of America.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2019 Feb 19; Vol. 15 (2), pp. e1006801. Date of Electronic Publication: 2019 Feb 19 (Print Publication: 2019).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms:
Allosteric Regulation/*physiology
Computational Biology/*methods
Fungal Proteins/*chemistry
Fungal Proteins/*metabolism
Allosteric Site ; Fungal Proteins/genetics ; Machine Learning ; Markov Chains ; Molecular Dynamics Simulation ; Optogenetics ; Protein Conformation
Czasopismo naukowe
Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
Tytuł:
Reversing allosteric communication: From detecting allosteric sites to inducing and tuning targeted allosteric response.
Autorzy:
Tee WV; Bioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), Matrix, Singapore.; Department of Biological Sciences (DBS), National University of Singapore (NUS), Singapore.
Guarnera E; Bioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), Matrix, Singapore.
Berezovsky IN; Bioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), Matrix, Singapore.; Department of Biological Sciences (DBS), National University of Singapore (NUS), Singapore.
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Źródło:
PLoS computational biology [PLoS Comput Biol] 2018 Jun 18; Vol. 14 (6), pp. e1006228. Date of Electronic Publication: 2018 Jun 18 (Print Publication: 2018).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Allosteric Regulation/*physiology
Allosteric Site/*physiology
Protein Binding/*physiology
Binding Sites/physiology ; Ligands ; Models, Molecular ; Protein Conformation ; Proteins/chemistry ; Signal Transduction ; Structure-Activity Relationship
Czasopismo naukowe
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