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Wyszukujesz frazę ""Adenosine Triphosphatases"" wg kryterium: Temat


Tytuł :
Comprehensive classification of ABC ATPases and their functional radiation in nucleoprotein dynamics and biological conflict systems.
Autorzy :
Krishnan A; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Burroughs AM; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Iyer LM; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Aravind L; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2020 Oct 09; Vol. 48 (18), pp. 10045-10075.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural; Review
MeSH Terms :
ATP-Binding Cassette Transporters*/chemistry
ATP-Binding Cassette Transporters*/classification
ATP-Binding Cassette Transporters*/physiology
Adenosine Triphosphatases*/chemistry
Adenosine Triphosphatases*/classification
Adenosine Triphosphatases*/physiology
Evolution, Molecular*
Bacteria/enzymology ; Eukaryota/enzymology ; Nucleoproteins/metabolism
Czasopismo naukowe
Tytuł :
Genome-wide role of Rad26 in promoting transcription-coupled nucleotide excision repair in yeast chromatin.
Autorzy :
Duan M; School of Molecular Biosciences, Washington State University, Pullman, WA 99164.; Department of Internal Medicine, Program in Cellular and Molecular Oncology, University of New Mexico Comprehensive Cancer Center, Albuquerque, NM 87131.
Selvam K; School of Molecular Biosciences, Washington State University, Pullman, WA 99164.
Wyrick JJ; School of Molecular Biosciences, Washington State University, Pullman, WA 99164; .; Center for Reproductive Biology, Washington State University, Pullman, WA 99164.
Mao P; School of Molecular Biosciences, Washington State University, Pullman, WA 99164; .; Department of Internal Medicine, Program in Cellular and Molecular Oncology, University of New Mexico Comprehensive Cancer Center, Albuquerque, NM 87131.
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Aug 04; Vol. 117 (31), pp. 18608-18616. Date of Electronic Publication: 2020 Jul 20.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
Adenosine Triphosphatases*/genetics
Adenosine Triphosphatases*/metabolism
Saccharomyces cerevisiae Proteins*/genetics
Saccharomyces cerevisiae Proteins*/metabolism
DNA Repair/*genetics
Nucleosomes/*genetics
DNA Helicases ; DNA Repair Enzymes ; Genome, Fungal/genetics ; Humans ; Nucleosomes/metabolism ; Poly-ADP-Ribose Binding Proteins ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism
Czasopismo naukowe
Tytuł :
Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA.
Autorzy :
Kong M; Department of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
Cutts EE; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
Pan D; Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
Beuron F; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
Kaliyappan T; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
Xue C; Department of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
Morris EP; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
Musacchio A; Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
Vannini A; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK; Fondazione Human Technopole, Structural Biology Research Centre, 20157 Milan, Italy. Electronic address: .
Greene EC; Department of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA. Electronic address: .
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Źródło :
Molecular cell [Mol Cell] 2020 Jul 02; Vol. 79 (1), pp. 99-114.e9. Date of Electronic Publication: 2020 May 22.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Adenosine Triphosphatases/*chemistry
Adenosine Triphosphatases/*metabolism
Adenosine Triphosphate/*metabolism
DNA/*chemistry
DNA/*metabolism
DNA-Binding Proteins/*chemistry
DNA-Binding Proteins/*metabolism
Multiprotein Complexes/*chemistry
Multiprotein Complexes/*metabolism
Nucleosomes/*metabolism
Adenosine Triphosphatases/genetics ; DNA-Binding Proteins/genetics ; Humans ; Models, Molecular ; Multiprotein Complexes/genetics ; Protein Binding ; Protein Conformation ; Single Molecule Imaging/methods
Czasopismo naukowe
Tytuł :
The AAA+ ATPase Msp1 is a processive protein translocase with robust unfoldase activity.
Autorzy :
Castanzo DT; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.
LaFrance B; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.
Martin A; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720; .; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720.
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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 30; Vol. 117 (26), pp. 14970-14977. Date of Electronic Publication: 2020 Jun 15.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Adenosine Triphosphatases/*chemistry
Adenosine Triphosphatases/*metabolism
Adenosine Triphosphatases/genetics ; Humans ; Peroxisomes/genetics ; Peroxisomes/metabolism ; Protein Domains ; Protein Folding ; Protein Transport
Czasopismo naukowe
Tytuł :
S-nitrosylation affects TRAP1 structure and ATPase activity and modulates cell response to apoptotic stimuli.
Autorzy :
Faienza F; Department of Biology, Tor Vergata University of Rome, 00133 Rome, Italy.
Lambrughi M; Computational Biology Laboratory, Center of Excellence in Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center, 2100 Copenhagen, Denmark.
Rizza S; Redox Signaling and Oxidative Stress Group, Danish Cancer Society Research Center, 2100 Copenhagen, Denmark.
Pecorari C; Department of Biology, Tor Vergata University of Rome, 00133 Rome, Italy; Redox Signaling and Oxidative Stress Group, Danish Cancer Society Research Center, 2100 Copenhagen, Denmark.
Giglio P; Department of Biology, Tor Vergata University of Rome, 00133 Rome, Italy.
Salamanca Viloria J; Computational Biology Laboratory, Center of Excellence in Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center, 2100 Copenhagen, Denmark.
Allega MF; Computational Biology Laboratory, Center of Excellence in Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center, 2100 Copenhagen, Denmark; Redox Signaling and Oxidative Stress Group, Danish Cancer Society Research Center, 2100 Copenhagen, Denmark.
Chiappetta G; Laboratory of Proteomics and Biological Mass Spectrometry, USR, CNRS - ESPCI Paris, PSL University, 3149, 10 rue, Vauquelin, Paris cedex, 05 75231, France.
Vinh J; Laboratory of Proteomics and Biological Mass Spectrometry, USR, CNRS - ESPCI Paris, PSL University, 3149, 10 rue, Vauquelin, Paris cedex, 05 75231, France.
Pacello F; Department of Biology, Tor Vergata University of Rome, 00133 Rome, Italy.
Battistoni A; Department of Biology, Tor Vergata University of Rome, 00133 Rome, Italy.
Rasola A; Department of Biomedical Sciences, University of Padova, Padova, Italy.
Papaleo E; Computational Biology Laboratory, Center of Excellence in Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center, 2100 Copenhagen, Denmark; Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. Electronic address: .
Filomeni G; Department of Biology, Tor Vergata University of Rome, 00133 Rome, Italy; Redox Signaling and Oxidative Stress Group, Danish Cancer Society Research Center, 2100 Copenhagen, Denmark; Center for Healthy Aging, University of Copenhagen, Denmark. Electronic address: .
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Źródło :
Biochemical pharmacology [Biochem Pharmacol] 2020 Jun; Vol. 176, pp. 113869. Date of Electronic Publication: 2020 Feb 21.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Apoptosis*
Protein Processing, Post-Translational*
Adenosine Triphosphatases/*metabolism
Nitric Oxide/*metabolism
TNF Receptor-Associated Factor 1/*metabolism
Zebrafish Proteins/*metabolism
Adenosine Triphosphatases/chemistry ; Adenosine Triphosphatases/genetics ; Animals ; Binding Sites/genetics ; Cysteine/genetics ; Cysteine/metabolism ; Humans ; Mitochondria/metabolism ; Molecular Dynamics Simulation ; Mutation ; Proteasome Endopeptidase Complex/metabolism ; Protein Conformation ; TNF Receptor-Associated Factor 1/chemistry ; TNF Receptor-Associated Factor 1/genetics ; Zebrafish ; Zebrafish Proteins/chemistry ; Zebrafish Proteins/genetics
Czasopismo naukowe
Tytuł :
Tetrameric architecture of an active phenol-bound form of the AAA transcriptional regulator DmpR.
Autorzy :
Park KH; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.
Kim S; Kavli Institute of Nanoscience and Department of Bionanoscience, Delft University of Technology, 2629 HZ, Delft, The Netherlands.
Lee SJ; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.; Department of Proteome Structural Biology, KRIBB School of Bioscience, University of Science and Technology (UST), Daejeon, 305-333, Republic of Korea.
Cho JE; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.
Patil VV; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.; Department of Proteome Structural Biology, KRIBB School of Bioscience, University of Science and Technology (UST), Daejeon, 305-333, Republic of Korea.
Dumbrepatil AB; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.
Song HN; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.
Ahn WC; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.
Joo C; Kavli Institute of Nanoscience and Department of Bionanoscience, Delft University of Technology, 2629 HZ, Delft, The Netherlands. .
Lee SG; Synthetic Biology and Bioengineering Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea.
Shingler V; Department of Molecular Biology, Umeå University, 90187, Umeå, SE, Sweden.
Woo EJ; Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea. .; Department of Proteome Structural Biology, KRIBB School of Bioscience, University of Science and Technology (UST), Daejeon, 305-333, Republic of Korea. .
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Źródło :
Nature communications [Nat Commun] 2020 Jun 01; Vol. 11 (1), pp. 2728. Date of Electronic Publication: 2020 Jun 01.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Conformation*
Protein Multimerization*
Adenosine Triphosphatases/*chemistry
Bacterial Proteins/*chemistry
DNA-Binding Proteins/*chemistry
Trans-Activators/*chemistry
Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites/genetics ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Gene Expression Regulation, Bacterial ; Phenol/metabolism ; Protein Binding ; Pseudomonas putida/enzymology ; Pseudomonas putida/genetics ; Sequence Homology, Amino Acid ; Trans-Activators/genetics ; Trans-Activators/metabolism
Czasopismo naukowe
Tytuł :
The SMAC mimetic LCL161 is a direct ABCB1/MDR1-ATPase activity modulator and BIRC5/Survivin expression down-regulator in cancer cells.
Autorzy :
Chang YC; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Kondapuram SK; Centre for Bioinformatics, School of Life Sciences, Pondicherry University, Kalapet, Puducherry 605014, India.
Yang TH; Department of Pharmacology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Syed SB; Centre for Bioinformatics, School of Life Sciences, Pondicherry University, Kalapet, Puducherry 605014, India.
Cheng SM; National Institute of Cancer Research, National Health Research Institutes, Tainan, Taiwan.
Lin TY; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Lin YC; Department of Pharmacology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Coumar MS; Centre for Bioinformatics, School of Life Sciences, Pondicherry University, Kalapet, Puducherry 605014, India.
Chang JY; National Institute of Cancer Research, National Health Research Institutes, Tainan, Taiwan; Center of Infectious Disease and Signaling Research, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Division of Hematology and Oncology, Department of Internal Medicine, National Cheng Kung University Hospital, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Leung E; Auckland Cancer Society Research Centre, University of Auckland, Auckland, New Zealand.
Cheung CHA; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Department of Pharmacology, College of Medicine, National Cheng Kung University, Tainan, Taiwan. Electronic address: .
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Źródło :
Toxicology and applied pharmacology [Toxicol Appl Pharmacol] 2020 Aug 15; Vol. 401, pp. 115080. Date of Electronic Publication: 2020 Jun 01.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Adenosine Triphosphatases/*antagonists & inhibitors
Antineoplastic Agents/*pharmacology
Apoptosis Regulatory Proteins/*pharmacology
Mitochondrial Proteins/*pharmacology
Survivin/*antagonists & inhibitors
Thiazoles/*pharmacology
ATP Binding Cassette Transporter, Subfamily B/antagonists & inhibitors ; ATP Binding Cassette Transporter, Subfamily B/metabolism ; Adenosine Triphosphatases/metabolism ; Antineoplastic Agents/chemistry ; Apoptosis Regulatory Proteins/chemistry ; Biomimetic Materials/chemistry ; Biomimetic Materials/pharmacology ; Cell Survival/drug effects ; Cell Survival/physiology ; Dose-Response Relationship, Drug ; Down-Regulation/drug effects ; Down-Regulation/physiology ; Gene Expression Regulation, Neoplastic ; Humans ; MCF-7 Cells ; Mitochondrial Proteins/chemistry ; Protein Structure, Secondary ; Survivin/biosynthesis ; Survivin/genetics ; Thiazoles/chemistry
Czasopismo naukowe
Tytuł :
ATP Hydrolysis by the SNF2 Domain of Dnmt5 Is Coupled to Both Specific Recognition and Modification of Hemimethylated DNA.
Autorzy :
Dumesic PA; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
Stoddard CI; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
Catania S; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
Narlikar GJ; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: .
Madhani HD; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA; Chan-Zuckerberg Biohub, San Francisco, CA 94158, USA. Electronic address: .
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Źródło :
Molecular cell [Mol Cell] 2020 Jul 02; Vol. 79 (1), pp. 127-139.e4. Date of Electronic Publication: 2020 May 20.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
DNA Methylation*
Adenosine Triphosphatases/*metabolism
Adenosine Triphosphate/*metabolism
DNA (Cytosine-5-)-Methyltransferases/*metabolism
DNA, Fungal/*metabolism
Fungal Proteins/*metabolism
Nucleosomes/*metabolism
Adenosine Triphosphatases/genetics ; Cryptococcus neoformans/genetics ; Cryptococcus neoformans/metabolism ; DNA (Cytosine-5-)-Methyltransferases/genetics ; DNA, Fungal/chemistry ; DNA, Fungal/genetics ; Fungal Proteins/genetics ; Hydrolysis ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Substrate Specificity ; Transcription Factors/genetics ; Transcription Factors/metabolism
Czasopismo naukowe
Tytuł :
Molecular architecture of the DNA-binding sites of the P-loop ATPases MipZ and ParA from Caulobacter crescentus.
Autorzy :
Corrales-Guerrero L; Department of Biology, University of Marburg, D-35043 Marburg, Germany.
He B; Department of Biology, University of Marburg, D-35043 Marburg, Germany.
Refes Y; Department of Biology, University of Marburg, D-35043 Marburg, Germany.
Panis G; Department of Microbiology and Molecular Medicine, University of Geneva Medical School, CH-1211 Geneva, Switzerland.
Bange G; Center for Synthetic Microbiology, D-35043 Marburg, Germany.; Department of Chemistry, University of Marburg, D-35043 Marburg, Germany.
Viollier PH; Department of Microbiology and Molecular Medicine, University of Geneva Medical School, CH-1211 Geneva, Switzerland.
Steinchen W; Center for Synthetic Microbiology, D-35043 Marburg, Germany.; Department of Chemistry, University of Marburg, D-35043 Marburg, Germany.
Thanbichler M; Department of Biology, University of Marburg, D-35043 Marburg, Germany.; Center for Synthetic Microbiology, D-35043 Marburg, Germany.; Max Planck Fellow Group Bacterial Cell Biology, Max Planck Institute for Terrestrial Microbiology, D-35043 Marburg, Germany.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2020 May 21; Vol. 48 (9), pp. 4769-4779.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Adenosine Triphosphatases/*chemistry
Bacterial Proteins/*chemistry
Caulobacter crescentus/*enzymology
DNA-Binding Proteins/*chemistry
Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; DNA/chemistry ; DNA/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Diffusion ; Hydrogen Deuterium Exchange-Mass Spectrometry ; Mutation ; Protein Binding
Czasopismo naukowe
Tytuł :
A MORC-driven transcriptional switch controls Toxoplasma developmental trajectories and sexual commitment.
Autorzy :
Farhat DC; Institute for Advanced Biosciences (IAB), Team Host-Pathogen Interactions and Immunity to Infection, INSERM U1209, CNRS UMR5309, University Grenoble Alpes, Grenoble, France.
Swale C; Institute for Advanced Biosciences (IAB), Team Host-Pathogen Interactions and Immunity to Infection, INSERM U1209, CNRS UMR5309, University Grenoble Alpes, Grenoble, France.
Dard C; Institute for Advanced Biosciences (IAB), Team Host-Pathogen Interactions and Immunity to Infection, INSERM U1209, CNRS UMR5309, University Grenoble Alpes, Grenoble, France.
Cannella D; Institute for Advanced Biosciences (IAB), Team Host-Pathogen Interactions and Immunity to Infection, INSERM U1209, CNRS UMR5309, University Grenoble Alpes, Grenoble, France.
Ortet P; BIAM-LEMIRE, UMR 7265, CEA, CNRS, University Aix-Marseille, St-Paul-Lez-Durance, France.
Barakat M; BIAM-LEMIRE, UMR 7265, CEA, CNRS, University Aix-Marseille, St-Paul-Lez-Durance, France.
Sindikubwabo F; Institute for Advanced Biosciences (IAB), Team Host-Pathogen Interactions and Immunity to Infection, INSERM U1209, CNRS UMR5309, University Grenoble Alpes, Grenoble, France.
Belmudes L; University Grenoble Alpes, CEA, INSERM, Grenoble, France.
De Bock PJ; University Grenoble Alpes, CEA, INSERM, Grenoble, France.
Couté Y; University Grenoble Alpes, CEA, INSERM, Grenoble, France.
Bougdour A; Institute for Advanced Biosciences (IAB), Team Host-Pathogen Interactions and Immunity to Infection, INSERM U1209, CNRS UMR5309, University Grenoble Alpes, Grenoble, France.
Hakimi MA; Institute for Advanced Biosciences (IAB), Team Host-Pathogen Interactions and Immunity to Infection, INSERM U1209, CNRS UMR5309, University Grenoble Alpes, Grenoble, France. .
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Źródło :
Nature microbiology [Nat Microbiol] 2020 Apr; Vol. 5 (4), pp. 570-583. Date of Electronic Publication: 2020 Feb 24.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Transcription, Genetic*
Adenosine Triphosphatases/*genetics
Histone Deacetylases/*genetics
Histones/*metabolism
Protozoan Proteins/*genetics
Toxoplasma/*genetics
Transcription Factors/*genetics
Adenosine Triphosphatases/chemistry ; Adenosine Triphosphatases/metabolism ; Animals ; Cats ; Chromatin ; Fibroblasts/parasitology ; Histone Code ; Histone Deacetylases/chemistry ; Histone Deacetylases/metabolism ; Histones/genetics ; Humans ; Life Cycle Stages/genetics ; Models, Molecular ; Primary Cell Culture ; Protein Binding ; Protein Processing, Post-Translational ; Protein Structure, Secondary ; Protozoan Proteins/chemistry ; Protozoan Proteins/metabolism ; Toxoplasma/growth & development ; Toxoplasma/metabolism ; Transcription Factors/chemistry ; Transcription Factors/metabolism
Czasopismo naukowe
Tytuł :
The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening.
Autorzy :
Muir KW; European Molecular Biology Laboratory, Grenoble, France. .; MRC Laboratory of Molecular Biology, Cambridge, UK. .
Li Y; European Molecular Biology Laboratory, Grenoble, France.
Weis F; European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Panne D; European Molecular Biology Laboratory, Grenoble, France. .; Department of Molecular and Cell Biology, Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK. .
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Źródło :
Nature structural & molecular biology [Nat Struct Mol Biol] 2020 Mar; Vol. 27 (3), pp. 233-239. Date of Electronic Publication: 2020 Feb 17.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Adenosine Triphosphatases/*chemistry
Cell Cycle Proteins/*chemistry
Chromosomal Proteins, Non-Histone/*chemistry
Saccharomyces cerevisiae/*chemistry
Saccharomyces cerevisiae Proteins/*chemistry
Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/analogs & derivatives ; Adenosine Triphosphate/chemistry ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Chaetomium/chemistry ; Chaetomium/genetics ; Chaetomium/metabolism ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Cloning, Molecular ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid
Czasopismo naukowe
Tytuł :
Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance.
Autorzy :
Kao CH; Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Ryu SW; Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Kim MJ; Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Wen X; Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Wimalarathne O; Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Paull TT; Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA .
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Źródło :
Molecular and cellular biology [Mol Cell Biol] 2020 May 28; Vol. 40 (12). Date of Electronic Publication: 2020 May 28 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Adenosine Triphosphatases/*metabolism
HSC70 Heat-Shock Proteins/*metabolism
HSP70 Heat-Shock Proteins/*metabolism
Prions/*metabolism
Saccharomyces cerevisiae/*metabolism
Saccharomyces cerevisiae Proteins/*metabolism
Adenosine Triphosphatases/chemistry ; Binding Sites ; Cell Line ; HSC70 Heat-Shock Proteins/chemistry ; HSP70 Heat-Shock Proteins/chemistry ; Humans ; Metals, Heavy/metabolism ; Phosphorylation ; Protein Aggregates ; Protein Denaturation ; Protein Domains ; Protein Folding ; Proteostasis ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae Proteins/chemistry ; Stress, Physiological
Czasopismo naukowe
Tytuł :
Cohesin Causes Replicative DNA Damage by Trapping DNA Topological Stress.
Autorzy :
Minchell NE; Genome Damage and Stability Centre, School of Life Sciences, Science Park Road, University of Sussex, Falmer, Brighton, East Sussex BN1 9RQ, UK.
Keszthelyi A; Genome Damage and Stability Centre, School of Life Sciences, Science Park Road, University of Sussex, Falmer, Brighton, East Sussex BN1 9RQ, UK.
Baxter J; Genome Damage and Stability Centre, School of Life Sciences, Science Park Road, University of Sussex, Falmer, Brighton, East Sussex BN1 9RQ, UK. Electronic address: .
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Źródło :
Molecular cell [Mol Cell] 2020 May 21; Vol. 78 (4), pp. 739-751.e8. Date of Electronic Publication: 2020 Apr 06.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Chromosomes, Fungal*
DNA Damage*
DNA Replication*
Adenosine Triphosphatases/*metabolism
Cell Cycle Proteins/*metabolism
Chromosomal Proteins, Non-Histone/*metabolism
DNA-Binding Proteins/*metabolism
Multiprotein Complexes/*metabolism
Saccharomyces cerevisiae/*genetics
Saccharomyces cerevisiae Proteins/*metabolism
Adenosine Triphosphatases/genetics ; Cell Cycle Proteins/genetics ; Chromosomal Proteins, Non-Histone/genetics ; DNA Topoisomerases, Type II/genetics ; DNA Topoisomerases, Type II/metabolism ; DNA, Fungal/genetics ; DNA, Fungal/metabolism ; DNA, Ribosomal/genetics ; DNA, Ribosomal/metabolism ; DNA-Binding Proteins/genetics ; Multiprotein Complexes/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics
Czasopismo naukowe
Tytuł :
Exploration of highly selective fluorogenic 'on-off' chemosensor for H 2 PO 4 ions: ICT-based sensing and ATPase activity profiling.
Autorzy :
Wagh YB; School of Chemical Sciences, Kavayitri Bahinabai Chaudhari North Maharashtra University, Jalgaon, (MS), India.
Tayade KC; Department of Chemistry and Analytical Chemistry, Rajarshi Shahu Mahavidyalaya (Autonomous), Latur, India.
Kuwar A; School of Chemical Sciences, Kavayitri Bahinabai Chaudhari North Maharashtra University, Jalgaon, (MS), India.
Sahoo SK; Department of Applied Chemistry, S. V National Institute Technology, 395007 Gujarat, Surat, India.
Mayank; Department of Chemistry, Indian Institute of Technology, Ropar, Punjab, India.
Singh N; Department of Chemistry, Indian Institute of Technology, Ropar, Punjab, India.
Dalal DS; School of Chemical Sciences, Kavayitri Bahinabai Chaudhari North Maharashtra University, Jalgaon, (MS), India.
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Źródło :
Luminescence : the journal of biological and chemical luminescence [Luminescence] 2020 May; Vol. 35 (3), pp. 379-384. Date of Electronic Publication: 2019 Dec 16.
Typ publikacji :
Journal Article
MeSH Terms :
Adenosine Triphosphatases/*metabolism
Fluorescent Dyes/*chemistry
Phosphoric Acids/*analysis
Adenosine Triphosphatases/chemistry ; Density Functional Theory ; Electron Transport ; Fluorescence ; Fluorescent Dyes/metabolism ; Hydrogen Bonding ; Ions/analysis ; Ions/metabolism ; Molecular Structure ; Phosphoric Acids/metabolism
Czasopismo naukowe
Tytuł :
Hydrogen peroxide reduced ATPase activity and the levels of ATP, ADP, and energy charge and its association with pulp breakdown occurrence of longan fruit during storage.
Autorzy :
Lin Y; Institute of Postharvest Technology of Agricultural Products, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; Key Laboratory of Postharvest Biology of Subtropical Special Agricultural Products (Fujian Agriculture and Forestry University), Fujian Province University, Fuzhou, Fujian 350002, China.
Lin H; Institute of Postharvest Technology of Agricultural Products, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; Key Laboratory of Postharvest Biology of Subtropical Special Agricultural Products (Fujian Agriculture and Forestry University), Fujian Province University, Fuzhou, Fujian 350002, China. Electronic address: .
Lin M; Food Science Program, Division of Food System & Bioengineering, University of Missouri, Columbia, MO 65211-5160, United States.
Chen Y; Institute of Postharvest Technology of Agricultural Products, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; Key Laboratory of Postharvest Biology of Subtropical Special Agricultural Products (Fujian Agriculture and Forestry University), Fujian Province University, Fuzhou, Fujian 350002, China.
Wang H; Institute of Postharvest Technology of Agricultural Products, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; Key Laboratory of Postharvest Biology of Subtropical Special Agricultural Products (Fujian Agriculture and Forestry University), Fujian Province University, Fuzhou, Fujian 350002, China.
Fan Z; Institute of Postharvest Technology of Agricultural Products, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; Key Laboratory of Postharvest Biology of Subtropical Special Agricultural Products (Fujian Agriculture and Forestry University), Fujian Province University, Fuzhou, Fujian 350002, China.
Ritenour MA; Indian River Research & Education Center, Institute of Food and Agricultural Sciences, University of Florida, Fort Pierce 34945-3138, United States.
Lin Y; Institute of Postharvest Technology of Agricultural Products, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; Key Laboratory of Postharvest Biology of Subtropical Special Agricultural Products (Fujian Agriculture and Forestry University), Fujian Province University, Fuzhou, Fujian 350002, China. Electronic address: .
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Źródło :
Food chemistry [Food Chem] 2020 May 01; Vol. 311, pp. 126008. Date of Electronic Publication: 2019 Dec 16.
Typ publikacji :
Journal Article
MeSH Terms :
Adenosine Triphosphatases/*metabolism
Hydrogen Peroxide/*metabolism
Sapindaceae/*metabolism
Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/antagonists & inhibitors ; Adenosine Triphosphate/metabolism ; Energy Metabolism/drug effects ; Food Storage ; Fruit/metabolism ; Hydrogen Peroxide/chemistry ; Hydrogen Peroxide/pharmacology ; Mitochondrial Membranes/drug effects ; Mitochondrial Membranes/metabolism
SCR Organism :
Dimocarpus
Czasopismo naukowe
Tytuł :
OsPDR2 mediates the regulation on the development response and maintenance of Pi homeostasis in rice.
Autorzy :
Cao Y; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Jain A; Amity Institute of Biotechnology, Amity University Rajasthan, Jaipur, India. Electronic address: .
Ai H; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Liu X; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Wang X; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China; Landscape Architecture Department, College of Horticulture, Nanjing Agricultural University, 210095, China. Electronic address: .
Hu Z; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Sun Y; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China; Institute of Eco-Environment and Plant Protection, Shanghai Academy of Agricultural Sciences, Shanghai, 201403, China. Electronic address: .
Hu S; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Shen X; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Lan X; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Xu G; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
Sun S; State Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Ministry of Agriculture, Nanjing Agricultural University, 210095, China. Electronic address: .
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Źródło :
Plant physiology and biochemistry : PPB 2020 Apr; Vol. 149, pp. 1-10. Date of Electronic Publication: 2020 Jan 21.
Typ publikacji :
Journal Article
MeSH Terms :
Adenosine Triphosphatases*/metabolism
Homeostasis*/genetics
Oryza*/genetics
Oryza*/growth & development
Oryza*/metabolism
Phosphates*/metabolism
Phosphates*/pharmacology
Gene Expression Regulation, Plant/drug effects ; Plant Roots/genetics ; Plant Roots/growth & development ; Plant Roots/metabolism
Czasopismo naukowe
Tytuł :
Accumulation of unacetylatable Snf2p at the INO1 promoter is detrimental to remodeler recycling supply for CUP1 induction.
Autorzy :
Esposito M; Department of Biology, College of Staten Island, City University of New York, Staten Island, New York, United States of America.; PhD Program in Biology, The Graduate Center, City University of New York, New York, New York, United States of America.
Sherr GL; Department of Biology, College of Staten Island, City University of New York, Staten Island, New York, United States of America.; PhD Program in Biology, The Graduate Center, City University of New York, New York, New York, United States of America.
Esposito A; Department of Biology, New Jersey City University, Jersey City, New Jersey, United States of America.
Kaluski G; Department of Biology, College of Staten Island, City University of New York, Staten Island, New York, United States of America.
Ellington F; Department of Biology, College of Staten Island, City University of New York, Staten Island, New York, United States of America.
Shen CH; Department of Biology, College of Staten Island, City University of New York, Staten Island, New York, United States of America.; PhD Program in Biology, The Graduate Center, City University of New York, New York, New York, United States of America.; PhD Program in Biochemistry, The Graduate Center, City University of New York, New York, New York, United States of America.; Institute for Macromolecular Assemblies, City University of New York, Staten Island, New York, United States of America.
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Źródło :
PloS one [PLoS One] 2020 Mar 25; Vol. 15 (3), pp. e0230572. Date of Electronic Publication: 2020 Mar 25 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Adenosine Triphosphatases/*metabolism
Metallothionein/*metabolism
Myo-Inositol-1-Phosphate Synthase/*genetics
Saccharomyces cerevisiae/*metabolism
Saccharomyces cerevisiae Proteins/*genetics
Saccharomyces cerevisiae Proteins/*metabolism
Transcription Factors/*metabolism
Acetylation ; Adenosine Triphosphatases/genetics ; Cell Survival/drug effects ; Chromatin/metabolism ; Chromatin Assembly and Disassembly ; Copper/metabolism ; Copper/toxicity ; Histones/metabolism ; Metallothionein/genetics ; Myo-Inositol-1-Phosphate Synthase/metabolism ; Nucleosomes/metabolism ; Promoter Regions, Genetic ; Transcription Factors/genetics ; Transcriptional Activation
Czasopismo naukowe
Tytuł :
DNA-mediated coupling of ATPase, translocase and nuclease activities of a Type ISP restriction-modification enzyme.
Autorzy :
Chand MK; Division of Biology, Indian Institute of Science Education and Research, Pune 411008, India.
Carle V; Division of Biology, Indian Institute of Science Education and Research, Pune 411008, India.
Anuvind KG; Division of Biology, Indian Institute of Science Education and Research, Pune 411008, India.
Saikrishnan K; Division of Biology, Indian Institute of Science Education and Research, Pune 411008, India.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2020 Mar 18; Vol. 48 (5), pp. 2594-2603.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Adenosine Triphosphatases/*metabolism
DNA/*metabolism
DNA Restriction Enzymes/*metabolism
Endonucleases/*metabolism
Nucleotide Transport Proteins/*metabolism
Adenosine Triphosphatases/chemistry ; Amino Acid Motifs ; Base Sequence ; DNA Restriction Enzymes/chemistry ; Enzyme Activation ; Mutation/genetics ; Protein Domains ; Protein Structure, Secondary ; Sequence Deletion ; Substrate Specificity
Czasopismo naukowe
Tytuł :
An F-Box Protein, Mdm30, Interacts with TREX Subunit Sub2 To Regulate Cellular Abundance Cotranscriptionally in Orchestrating mRNA Export Independently of Splicing and Mitochondrial Function.
Autorzy :
Ferdoush J; Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Sen R; Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Durairaj G; Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Barman P; Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Kaja A; Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Guha S; Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Bhaumik SR; Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA .
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Źródło :
Molecular and cellular biology [Mol Cell Biol] 2020 Mar 16; Vol. 40 (7). Date of Electronic Publication: 2020 Mar 16 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Active Transport, Cell Nucleus/*physiology
Adenosine Triphosphatases/*metabolism
F-Box Proteins/*metabolism
Mitochondria/*physiology
RNA, Messenger/*metabolism
Saccharomyces cerevisiae Proteins/*metabolism
Adenosine Triphosphatases/genetics ; GTP Phosphohydrolases/genetics ; Membrane Proteins/genetics ; Mitochondrial Dynamics/genetics ; Mitochondrial Proteins/genetics ; Proteasome Endopeptidase Complex/metabolism ; RNA Splicing ; RNA Transport ; RNA, Messenger/genetics ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/genetics ; Transcription, Genetic/genetics ; Ubiquitination
Czasopismo naukowe

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