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Wyszukujesz frazę ""Ion Channel Gating"" wg kryterium: Temat


Tytuł :
Structural basis for pH gating of the two-pore domain K channel TASK2.
Autorzy :
Li B; Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA, USA.; Helen Wills Neuroscience Institute, University of California Berkeley, Berkeley, CA, USA.; California Institute for Quantitative Biology (QB3), University of California Berkeley, Berkeley, CA, USA.
Rietmeijer RA; Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA, USA.; Helen Wills Neuroscience Institute, University of California Berkeley, Berkeley, CA, USA.; California Institute for Quantitative Biology (QB3), University of California Berkeley, Berkeley, CA, USA.; Biophysics Graduate Group, University of California Berkeley, Berkeley, CA, USA.
Brohawn SG; Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA, USA. .; Helen Wills Neuroscience Institute, University of California Berkeley, Berkeley, CA, USA. .; California Institute for Quantitative Biology (QB3), University of California Berkeley, Berkeley, CA, USA. .
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Źródło :
Nature [Nature] 2020 Oct; Vol. 586 (7829), pp. 457-462. Date of Electronic Publication: 2020 Sep 30.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Cryoelectron Microscopy*
Ion Channel Gating*
Potassium/*metabolism
Potassium Channels, Tandem Pore Domain/*chemistry
Potassium Channels, Tandem Pore Domain/*ultrastructure
Animals ; Hydrogen-Ion Concentration ; Mice ; Models, Molecular ; Potassium Channels, Tandem Pore Domain/metabolism ; Protein Domains ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing.
Autorzy :
Kim M; School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.; The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University, Tempe, AZ, 85287, USA.
Sisco NJ; School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.; The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University, Tempe, AZ, 85287, USA.
Hilton JK; School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.; The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University, Tempe, AZ, 85287, USA.
Montano CM; The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University, Tempe, AZ, 85287, USA.
Castro MA; School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.
Cherry BR; The Magnetic Resonance Research Center, Arizona State University, Tempe, AZ, 85287, USA.
Levitus M; School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.; The Biodesign Institute Center for Single Molecule Biophysics, Arizona State University, Tempe, AZ, 85287, USA.
Van Horn WD; School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA. .; The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University, Tempe, AZ, 85287, USA. .
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Źródło :
Nature communications [Nat Commun] 2020 Aug 20; Vol. 11 (1), pp. 4169. Date of Electronic Publication: 2020 Aug 20.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Hot Temperature*
Ion Channel Gating/*physiology
TRPV Cation Channels/*metabolism
Thermosensing/*physiology
Binding Sites/genetics ; Capsaicin/chemistry ; Capsaicin/metabolism ; Circular Dichroism ; Humans ; Ion Channel Gating/genetics ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Protein Binding ; Protein Domains ; TRPV Cation Channels/chemistry ; TRPV Cation Channels/genetics ; Thermosensing/genetics
Czasopismo naukowe
Tytuł :
Flow and shortcuts along the Shaker Kv channel slow inactivation gating cycle.
Autorzy :
Nirenberg VA; Department of Life Sciences and the Zlotowski Center for Neurosciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Yifrach O; Department of Life Sciences and the Zlotowski Center for Neurosciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
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Źródło :
The Journal of general physiology [J Gen Physiol] 2020 Aug 03; Vol. 152 (8).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't; Comment
MeSH Terms :
Ion Channel Gating*
Shaker Superfamily of Potassium Channels*/metabolism
Czasopismo naukowe
Tytuł :
Structures of human pannexin 1 reveal ion pathways and mechanism of gating.
Autorzy :
Ruan Z; Van Andel Institute, Grand Rapids, MI, USA.
Orozco IJ; Van Andel Institute, Grand Rapids, MI, USA.
Du J; Van Andel Institute, Grand Rapids, MI, USA. .
Lü W; Van Andel Institute, Grand Rapids, MI, USA. .
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Źródło :
Nature [Nature] 2020 Aug; Vol. 584 (7822), pp. 646-651. Date of Electronic Publication: 2020 Jun 03.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Cryoelectron Microscopy*
Ion Channel Gating*/drug effects
Patch-Clamp Techniques*
Connexins/*chemistry
Connexins/*metabolism
Nerve Tissue Proteins/*chemistry
Nerve Tissue Proteins/*metabolism
Adenosine Triphosphate/metabolism ; Animals ; Apoproteins/chemistry ; Apoproteins/metabolism ; Apoproteins/ultrastructure ; Apoptosis ; Binding Sites/drug effects ; Carbenoxolone/chemistry ; Carbenoxolone/metabolism ; Carbenoxolone/pharmacology ; Caspase 7/metabolism ; Cell Line ; Connexins/ultrastructure ; Gap Junctions ; Glycosylation ; Humans ; Models, Molecular ; Mutation ; Nerve Tissue Proteins/ultrastructure ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Sf9 Cells
Czasopismo naukowe
Tytuł :
Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs.
Autorzy :
Kumar A; Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA.
Basak S; Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA.
Rao S; Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Gicheru Y; Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA.
Mayer ML; Division of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, 94025, USA.
Sansom MSP; Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Chakrapani S; Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA. .; Department of Neuroscience, School of Medicine, Case Western Reserve University, Cleveland, OH, 44106-4970, USA. .
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Źródło :
Nature communications [Nat Commun] 2020 Jul 27; Vol. 11 (1), pp. 3752. Date of Electronic Publication: 2020 Jul 27.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Ion Channel Gating*
Lipids/*chemistry
Nanoparticles/*chemistry
Receptors, Glycine/*metabolism
Zebrafish Proteins/*metabolism
Allosteric Regulation ; Animals ; Binding Sites ; Glycine/metabolism ; Molecular Dynamics Simulation ; Neurotransmitter Agents/metabolism ; Protein Conformation ; Receptors, Glycine/ultrastructure ; Xenopus ; Zebrafish Proteins/ultrastructure
Czasopismo naukowe
Tytuł :
Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance.
Autorzy :
Deng Z; Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.; Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, Saint Louis, MO, 63110, USA.
Maksaev G; Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.; Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, Saint Louis, MO, 63110, USA.
Schlegel AM; Department of Biology, Washington University in Saint Louis, Saint Louis, MO, 63130, USA.; NSF Center for Engineering Mechanobiology, Washington University in Saint Louis, Saint Louis, MO, 63130, USA.
Zhang J; Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.; Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, Saint Louis, MO, 63110, USA.
Rau M; Washington University Center for Cellular Imaging, Washington University School of Medicine, Saint Louis, MO, 63110, USA.
Fitzpatrick JAJ; Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.; Washington University Center for Cellular Imaging, Washington University School of Medicine, Saint Louis, MO, 63110, USA.; Department of Neuroscience, Washington University School of Medicine, Saint Louis, MO, 63110, USA.; Department of Biomedical Engineering, Washington University in Saint Louis, Saint Louis, MO, 63130, USA.
Haswell ES; Department of Biology, Washington University in Saint Louis, Saint Louis, MO, 63130, USA.; NSF Center for Engineering Mechanobiology, Washington University in Saint Louis, Saint Louis, MO, 63130, USA.
Yuan P; Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA. .; Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, Saint Louis, MO, 63110, USA. .
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Źródło :
Nature communications [Nat Commun] 2020 Jul 23; Vol. 11 (1), pp. 3690. Date of Electronic Publication: 2020 Jul 23.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Ion Channel Gating*
Mechanotransduction, Cellular*
Arabidopsis/*metabolism
Arabidopsis Proteins/*chemistry
Arabidopsis Proteins/*metabolism
Eukaryota/*metabolism
Arabidopsis Proteins/ultrastructure ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Ion Channels/chemistry ; Ion Channels/metabolism ; Models, Molecular ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Protein Domains ; Protein Structure, Secondary
Czasopismo naukowe
Tytuł :
Single-Molecule Localization of the Cardiac Voltage-Gated Sodium Channel Reveals Different Modes of Reorganization at Cardiomyocyte Membrane Domains.
Autorzy :
Vermij SH; Institute of Biochemistry and Molecular Medicine, University of Bern, Switzerland (S.H.V., J.-S.R., H.A.).
Rougier JS; Institute of Biochemistry and Molecular Medicine, University of Bern, Switzerland (S.H.V., J.-S.R., H.A.).
Agulló-Pascual E; Microscopy Core, Icahn School of Medicine at Mount Sinai, New York, NY (E.A.-P.).
Rothenberg E; Department of Biochemistry and Pharmacology (E.R.), New York University School of Medicine, NY.
Delmar M; Department of Cardiology (M.D.), New York University School of Medicine, NY.
Abriel H; Institute of Biochemistry and Molecular Medicine, University of Bern, Switzerland (S.H.V., J.-S.R., H.A.).
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Źródło :
Circulation. Arrhythmia and electrophysiology [Circ Arrhythm Electrophysiol] 2020 Jul; Vol. 13 (7), pp. e008241. Date of Electronic Publication: 2020 Jun 15.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Ion Channel Gating*
Single Molecule Imaging*
Cell Membrane/*metabolism
Myocytes, Cardiac/*metabolism
NAV1.5 Voltage-Gated Sodium Channel/*metabolism
Animals ; Cell Membrane/ultrastructure ; Computer Simulation ; Dystrophin/genetics ; Dystrophin/metabolism ; Membrane Potentials ; Mice, Inbred mdx ; Mice, Transgenic ; Models, Cardiovascular ; Myocytes, Cardiac/ultrastructure ; NAV1.5 Voltage-Gated Sodium Channel/genetics ; Protein Transport
Czasopismo naukowe
Tytuł :
Electromechanical coupling in the hyperpolarization-activated K channel KAT1.
Autorzy :
Clark MD; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.
Contreras GF; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.
Shen R; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA.
Perozo E; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA. .
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Źródło :
Nature [Nature] 2020 Jul; Vol. 583 (7814), pp. 145-149. Date of Electronic Publication: 2020 May 27.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Arabidopsis*/chemistry
Arabidopsis*/ultrastructure
Cryoelectron Microscopy*
Ion Channel Gating*
Arabidopsis Proteins/*chemistry
Arabidopsis Proteins/*metabolism
Potassium Channels, Inwardly Rectifying/*chemistry
Potassium Channels, Inwardly Rectifying/*metabolism
Allosteric Regulation ; Arabidopsis Proteins/ultrastructure ; Binding Sites ; Lipids ; Models, Molecular ; Potassium Channels, Inwardly Rectifying/ultrastructure ; Protein Conformation
Czasopismo naukowe
Tytuł :
Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations.
Autorzy :
Geragotelis AD; Department of Chemistry, University of California, Irvine, CA 92697.
Wood ML; Department of Chemistry, University of California, Irvine, CA 92697.
Göddeke H; Theoretical Chemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, D-44780 Bochum, Germany.
Hong L; Department of Physiology and Biophysics, University of California, Irvine, CA 92697.
Webster PD; Department of Physiology and Biophysics, University of California, Irvine, CA 92697.; Chao Family Comprehensive Cancer Center, University of California, Irvine, CA 92697.
Wong EK; Department of Chemistry, University of California, Irvine, CA 92697.
Freites JA; Department of Chemistry, University of California, Irvine, CA 92697.
Tombola F; Department of Physiology and Biophysics, University of California, Irvine, CA 92697.; Chao Family Comprehensive Cancer Center, University of California, Irvine, CA 92697.
Tobias DJ; Department of Chemistry, University of California, Irvine, CA 92697; .
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Jun 16; Vol. 117 (24), pp. 13490-13498. Date of Electronic Publication: 2020 May 27.
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 :
Ion Channel Gating*
Ion Channels/*chemistry
Ion Channels/*metabolism
Crystallography, X-Ray ; Guanidines/metabolism ; Humans ; Hydrogen Bonding ; Ion Channels/genetics ; Membrane Potentials ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Mutation ; Protein Conformation ; Protons
Czasopismo naukowe
Tytuł :
Desensitization of NMDA channels requires ligand binding to both GluN1 and GluN2 subunits to constrict the pore beside the activation gate.
Autorzy :
Chen YS; Department of Physiology, National Taiwan University College of Medicine, Taipei, Taiwan.
Tu YC; Department of Physiology, National Taiwan University College of Medicine, Taipei, Taiwan.
Lai YC; Department of Biomedical Sciences, College of Medicine, Chang Gung University, Tao-Yuan, Taiwan.
Liu E; Department of Physiology, National Taiwan University College of Medicine, Taipei, Taiwan.
Yang YC; Department of Biomedical Sciences, College of Medicine, Chang Gung University, Tao-Yuan, Taiwan.; Graduate Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Tao-Yuan, Taiwan.; Neuroscience Research Center, Chang Gung Memorial Hospital, Linkou Medical Center, Tao-Yuan, Taiwan.
Kuo CC; Department of Physiology, National Taiwan University College of Medicine, Taipei, Taiwan.; Department of Neurology, National Taiwan University Hospital, Taipei, Taiwan.
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Źródło :
Journal of neurochemistry [J Neurochem] 2020 Jun; Vol. 153 (5), pp. 549-566. Date of Electronic Publication: 2019 Dec 26.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Glutamic Acid/*metabolism
Glycine/*metabolism
Ion Channel Gating/*physiology
Nerve Tissue Proteins/*metabolism
Receptors, N-Methyl-D-Aspartate/*metabolism
Animals ; Dose-Response Relationship, Drug ; Excitatory Amino Acid Agonists/metabolism ; Excitatory Amino Acid Agonists/pharmacology ; Excitatory Amino Acid Antagonists/metabolism ; Excitatory Amino Acid Antagonists/pharmacology ; Female ; Glutamic Acid/pharmacology ; Glycine/pharmacology ; Ion Channel Gating/drug effects ; Ligands ; Nerve Tissue Proteins/agonists ; Nerve Tissue Proteins/antagonists & inhibitors ; Protein Binding/drug effects ; Protein Binding/physiology ; Rats ; Receptors, N-Methyl-D-Aspartate/agonists ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors ; Receptors, N-Methyl-D-Aspartate/genetics ; Xenopus laevis
Czasopismo naukowe
Tytuł :
How goblet cells respond to dry eye: adaptive and pathological roles of voltage-gated calcium channels and P2X 7 purinoceptors.
Autorzy :
Puro DG; Department of Ophthalmology and Visual Sciences, University of Michigan, Ann Arbor, Michigan.; Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan.
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Źródło :
American journal of physiology. Cell physiology 2020 Jun 01; Vol. 318 (6), pp. C1305-C1315. Date of Electronic Publication: 2020 Apr 29.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Ion Channel Gating*
Calcium Channels/*metabolism
Conjunctiva/*metabolism
Dry Eye Syndromes/*metabolism
Goblet Cells/*metabolism
Receptors, Purinergic P2X7/*metabolism
Tears/*metabolism
Adaptation, Physiological ; Animals ; Conjunctiva/pathology ; Dry Eye Syndromes/pathology ; Female ; Goblet Cells/pathology ; Male ; Membrane Potentials ; Osmolar Concentration ; Osmoregulation ; Rats, Long-Evans ; Rats, Sprague-Dawley ; Signal Transduction
Czasopismo naukowe
Tytuł :
Molecular dysregulation of ciliary polycystin-2 channels caused by variants in the TOP domain.
Autorzy :
Vien TN; Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611.
Wang J; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112.
Ng LCT; Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611.
Cao E; Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112.
DeCaen PG; Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611; .
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 May 12; Vol. 117 (19), pp. 10329-10338. Date of Electronic Publication: 2020 Apr 24.
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 :
Ion Channel Gating*
Mutation*
Calcium/*metabolism
Cilia/*pathology
Polycystic Kidney, Autosomal Dominant/*pathology
TRPP Cation Channels/*metabolism
Cilia/metabolism ; HEK293 Cells ; Humans ; Polycystic Kidney, Autosomal Dominant/genetics ; Polycystic Kidney, Autosomal Dominant/metabolism ; Protein Domains ; TRPP Cation Channels/chemistry ; TRPP Cation Channels/genetics
Czasopismo naukowe
Tytuł :
Spider venom-derived peptide induces hyperalgesia in Na v 1.7 knockout mice by activating Na v 1.9 channels.
Autorzy :
Zhou X; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Ma T; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology (HUST), Wuhan, 430074, China.
Yang L; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology (HUST), Wuhan, 430074, China.
Peng S; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Li L; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology (HUST), Wuhan, 430074, China.
Wang Z; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Xiao Z; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Zhang Q; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Wang L; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Huang Y; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Chen M; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Liang S; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
Zhang X; Department of Anesthesiology, Tongji Hospital of HUST, Wuhan, 430030, China.
Liu JY; Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology (HUST), Wuhan, 430074, China. liujy@ion.ac.cn.; 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. liujy@ion.ac.cn.
Liu Z; The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China. .
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Źródło :
Nature communications [Nat Commun] 2020 May 08; Vol. 11 (1), pp. 2293. Date of Electronic Publication: 2020 May 08.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Ion Channel Gating*
Hyperalgesia/*chemically induced
Hyperalgesia/*metabolism
NAV1.7 Voltage-Gated Sodium Channel/*metabolism
NAV1.9 Voltage-Gated Sodium Channel/*metabolism
Peptides/*adverse effects
Spider Venoms/*adverse effects
Amino Acid Sequence ; Animals ; Female ; Ganglia, Spinal/pathology ; Humans ; Hyperalgesia/complications ; Male ; Mice, Knockout ; NAV1.7 Voltage-Gated Sodium Channel/chemistry ; NAV1.8 Voltage-Gated Sodium Channel/metabolism ; NAV1.9 Voltage-Gated Sodium Channel/chemistry ; Neurons/drug effects ; Neurons/pathology ; Pain/complications ; Pain/physiopathology ; Rats
Czasopismo naukowe
Tytuł :
A Plug-and-Latch Mechanism for Gating the Mechanosensitive Piezo Channel.
Autorzy :
Geng J; State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, IDG/McGovern Institute for Brain Research, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China.
Liu W; State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, IDG/McGovern Institute for Brain Research, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China; Joint Graduate Program of Peking-Tsinghua-NIBS, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China.
Zhou H; MOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Zhang T; State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, IDG/McGovern Institute for Brain Research, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China.
Wang L; State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, IDG/McGovern Institute for Brain Research, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China.
Zhang M; State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, IDG/McGovern Institute for Brain Research, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China.
Li Y; State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, IDG/McGovern Institute for Brain Research, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China.
Shen B; MOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Li X; MOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. Electronic address: .
Xiao B; State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, IDG/McGovern Institute for Brain Research, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China. Electronic address: .
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Źródło :
Neuron [Neuron] 2020 May 06; Vol. 106 (3), pp. 438-451.e6. Date of Electronic Publication: 2020 Mar 05.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Ion Channel Gating*
Ion Channels/*metabolism
Animals ; HEK293 Cells ; HeLa Cells ; Humans ; Ion Channels/chemistry ; Male ; Mechanotransduction, Cellular ; Mice ; Mice, Inbred C57BL ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism
Czasopismo naukowe
Tytuł :
Conductance Mechanisms of Rapidly Desensitizing Cation Channelrhodopsins from Cryptophyte Algae.
Autorzy :
Sineshchekov OA; Center for Membrane Biology, Department of Biochemistry & Molecular Biology, The University of Texas Health Science Center at Houston McGovern Medical School, Houston, Texas, USA.
Govorunova EG; Center for Membrane Biology, Department of Biochemistry & Molecular Biology, The University of Texas Health Science Center at Houston McGovern Medical School, Houston, Texas, USA.
Li H; Center for Membrane Biology, Department of Biochemistry & Molecular Biology, The University of Texas Health Science Center at Houston McGovern Medical School, Houston, Texas, USA.
Wang Y; Center for Membrane Biology, Department of Biochemistry & Molecular Biology, The University of Texas Health Science Center at Houston McGovern Medical School, Houston, Texas, USA.
Melkonian M; Institute for Plant Sciences, Department of Biology, University of Cologne, Cologne, Germany.; Central Collection of Algal Cultures, Faculty of Biology, University of Duisburg-Essen, Essen, Germany.
Wong GK; Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada.; Department of Medicine, University of Alberta, Edmonton, Alberta, Canada.; Beijing Genomics Institute-Shenzhen, Shenzhen, China.
Brown LS; Department of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada.
Spudich JL; Center for Membrane Biology, Department of Biochemistry & Molecular Biology, The University of Texas Health Science Center at Houston McGovern Medical School, Houston, Texas, USA .
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Źródło :
MBio [mBio] 2020 Apr 21; Vol. 11 (2). Date of Electronic Publication: 2020 Apr 21.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Ion Channel Gating*
Cations/*metabolism
Channelrhodopsins/*metabolism
Cryptophyta/*physiology
Cryptophyta/classification ; Electrophysiological Phenomena ; Gene Expression Regulation ; Membrane Potentials ; Mutagenesis ; Optogenetics ; Patch-Clamp Techniques ; Photochemical Processes ; Phylogeny ; Spectrum Analysis
Czasopismo naukowe
Tytuł :
A paradigm of thermal adaptation in penguins and elephants by tuning cold activation in TRPM8.
Autorzy :
Yang S; Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, 650223 Kunming, Yunnan, China.; College of Wildlife and Protected Area, Northeast Forestry University, 150040 Harbin, China.
Lu X; Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, 650223 Kunming, Yunnan, China.; College of Life Sciences, University of Chinese Academy of Sciences, 100049 Bejing, China.
Wang Y; Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, 650223 Kunming, Yunnan, China.; College of Wildlife and Protected Area, Northeast Forestry University, 150040 Harbin, China.
Xu L; Department of Biophysics and Kidney Disease Center, First Affiliated Hospital, Institute of Neuroscience, National Health Commission and Chinese Academy of Medical Sciences Key Laboratory of Medical Neurobiology, Zhejiang University School of Medicine, 310058 Hangzhou, Zhejiang, China.
Chen X; Department of Biophysics and Kidney Disease Center, First Affiliated Hospital, Institute of Neuroscience, National Health Commission and Chinese Academy of Medical Sciences Key Laboratory of Medical Neurobiology, Zhejiang University School of Medicine, 310058 Hangzhou, Zhejiang, China.
Yang F; Department of Biophysics and Kidney Disease Center, First Affiliated Hospital, Institute of Neuroscience, National Health Commission and Chinese Academy of Medical Sciences Key Laboratory of Medical Neurobiology, Zhejiang University School of Medicine, 310058 Hangzhou, Zhejiang, China; .
Lai R; Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, 650223 Kunming, Yunnan, China; .; Kunming Institute of Zoology-Chinese University of Hong Kong Joint Laboratory of Bioresources and Molecular Research in Common Diseases, Kunming Institute of Zoology, Chinese Academy of Sciences, 650223 Kunming, Yunnan, China.; Sino-African Joint Research Center, Kunming Institute of Zoology, Chinese Academy of Sciences, 650223 Kunming, Yunnan, China.; Center for Biosafety Mega-Science, Chinese Academy of Sciences, 430071 Wuhan, Hubei, China.; Institute for Drug Discovery and Development, Chinese Academy of Sciences, 201203 Shanghai, China.
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Apr 14; Vol. 117 (15), pp. 8633-8638. Date of Electronic Publication: 2020 Mar 27.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Adaptation, Physiological*
Cold Temperature*
Ion Channel Gating*
Elephants/*physiology
Spheniscidae/*physiology
TRPM Cation Channels/*metabolism
Amino Acid Sequence ; Animals ; Sequence Homology ; TRPM Cation Channels/genetics
Czasopismo naukowe
Tytuł :
Ball-and-chain inactivation in a calcium-gated potassium channel.
Autorzy :
Fan C; Department of Anesthesiology, Weill Cornell Medical College, New York, NY, USA.
Sukomon N; Department of Anesthesiology, Weill Cornell Medical College, New York, NY, USA.
Flood E; School of Science, RMIT University, Melbourne, Victoria, Australia.
Rheinberger J; Department of Anesthesiology, Weill Cornell Medical College, New York, NY, USA.; Department of Structural Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.
Allen TW; School of Science, RMIT University, Melbourne, Victoria, Australia.
Nimigean CM; Department of Anesthesiology, Weill Cornell Medical College, New York, NY, USA. .; Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY, USA. .
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Źródło :
Nature [Nature] 2020 Apr; Vol. 580 (7802), pp. 288-293. Date of Electronic Publication: 2020 Mar 18.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Cryoelectron Microscopy*
Ion Channel Gating*
Methanobacterium/*chemistry
Potassium Channels, Calcium-Activated/*antagonists & inhibitors
Potassium Channels, Calcium-Activated/*ultrastructure
Calcium/metabolism ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Models, Molecular ; Potassium Channels, Calcium-Activated/chemistry ; Potassium Channels, Calcium-Activated/metabolism ; Protein Structure, Secondary ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Thermodynamics
Czasopismo naukowe

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