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Wyszukujesz frazę ""Catalytic Domain"" wg kryterium: Temat


Tytuł :
Catalytic site seeing.
Autorzy :
Mortensen M; Department of Chemical and Biomolecular Engineering, University of Tennessee, Knoxville, TN, USA. .
Laursen S; Department of Chemical and Biomolecular Engineering, University of Tennessee, Knoxville, TN, USA. .
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Źródło :
Nature chemistry [Nat Chem] 2022 May; Vol. 14 (5), pp. 483-485.
Typ publikacji :
Journal Article
MeSH Terms :
Catalytic Domain*
Czasopismo naukowe
Tytuł :
Biochemical and in silico identification of the active site and the catalytic mechanism of the circadian deadenylase HESPERIN.
Autorzy :
Beta RAA; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Kyritsis A; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Douka V; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Papanastasi E; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Rizouli M; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Leonidas DD; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Vlachakis D; Genetics Laboratory, Department of Biotechnology, Agricultural University of Athens, Greece.
Balatsos NAA; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
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Źródło :
FEBS open bio [FEBS Open Bio] 2022 May; Vol. 12 (5), pp. 1036-1049. Date of Electronic Publication: 2022 Mar 29.
Typ publikacji :
Journal Article
MeSH Terms :
Catalytic Domain*
Catalysis ; RNA, Messenger/genetics
Czasopismo naukowe
Tytuł :
Conformational Variation in Enzyme Catalysis: A Structural Study on Catalytic Residues.
Autorzy :
Riziotis IG; European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, CB10 1SD Cambridge, UK. Electronic address: .
Ribeiro AJM; European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, CB10 1SD Cambridge, UK.
Borkakoti N; European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, CB10 1SD Cambridge, UK.
Thornton JM; European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, CB10 1SD Cambridge, UK.
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Źródło :
Journal of molecular biology [J Mol Biol] 2022 Apr 15; Vol. 434 (7), pp. 167517. Date of Electronic Publication: 2022 Feb 28.
Typ publikacji :
Journal Article
MeSH Terms :
Biocatalysis*
Catalytic Domain*
Enzymes*/chemistry
Databases, Protein ; Ligands
Czasopismo naukowe
Tytuł :
Molecular Dynamics-Derived Descriptor Informs the Impact of Mutation on the Catalytic Turnover Number in Lactonase Across Substrates.
Autorzy :
Jiang Y; Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37235, United States.
Yan B; Department of Biostatistics, Vanderbilt University, Nashville, Tennessee 37235, United States.
Chen Y; School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu 210023, China.
Juarez RJ; Chemical and Physical Biology Program, Vanderbilt University, Nashville, Tennessee 37235, United States.
Yang ZJ; Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37235, United States.; Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37235, United States.; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, Tennessee 37235, United States.; Data Science Institute, Vanderbilt University, Nashville, Tennessee 37235, United States.
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Źródło :
The journal of physical chemistry. B [J Phys Chem B] 2022 Apr 07; Vol. 126 (13), pp. 2486-2495. Date of Electronic Publication: 2022 Mar 24.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*/genetics
Molecular Dynamics Simulation*
Mutation*/genetics
Mutation*/physiology
Catalysis ; Substrate Specificity
Czasopismo naukowe
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
Tytuł :
Catalytic trajectory of a dimeric nonribosomal peptide synthetase subunit with an inserted epimerase domain.
Autorzy :
Wang J; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Li D; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Chen L; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Cao W; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Kong L; National Facility for Protein Science in Shanghai, Chinese Academy of Sciences, Shanghai, 201204, China.
Zhang W; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Croll T; Cambridge Institute for Medical Research, University of Cambridge, Keith Peters Building, Cambridge, CB2 0XY, UK.
Deng Z; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China. .
Liang J; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China. .
Wang Z; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China. .
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Źródło :
Nature communications [Nat Commun] 2022 Feb 01; Vol. 13 (1), pp. 592. Date of Electronic Publication: 2022 Feb 01.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*
Peptide Synthases/*chemistry
Peptide Synthases/*metabolism
Racemases and Epimerases/*chemistry
Racemases and Epimerases/*metabolism
Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Catalysis ; Cryoelectron Microscopy ; Escherichia coli ; Models, Molecular
Czasopismo naukowe
Tytuł :
Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate.
Autorzy :
Holmes JB; Department of Chemistry, University of California, Riverside, CA 92521.
Liu V; Department of Chemistry, University of California, Riverside, CA 92521.
Caulkins BG; Department of Chemistry, University of California, Riverside, CA 92521.; W.M. Keck Science Department, Claremont McKenna, Pitzer, and Scripps Colleges, Claremont, CA 91711.
Hilario E; Department of Chemistry, University of California, Riverside, CA 92521.
Ghosh RK; Department of Biochemistry, University of California, Riverside, CA 92521.
Drago VN; Department of Chemistry and Biochemistry, University of Toledo, Toledo, OH 43606.
Young RP; Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99354.
Romero JA; Department of Chemistry, University of California, Riverside, CA 92521.
Gill AD; Department of Biochemistry, University of California, Riverside, CA 92521.
Bogie PM; Department of Chemistry, University of California, Riverside, CA 92521.
Paulino J; National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310.
Wang X; National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310.
Riviere G; Department of Biochemistry and Molecular Biology, McKnight Brain Institute, National High Magnetic Field Laboratory, University of Florida, Gainesville, FL 32610.
Bosken YK; Department of Biochemistry, University of California, Riverside, CA 92521.
Struppe J; Bruker Biospin Corporation, Billerica, MA 01821.
Hassan A; Bruker Switzerland AG 8117 Fällanden, Switzerland.
Guidoulianov J; Bruker Switzerland AG 8117 Fällanden, Switzerland.
Perrone B; Bruker Switzerland AG 8117 Fällanden, Switzerland.
Mentink-Vigier F; National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310.
Chang CA; Department of Chemistry, University of California, Riverside, CA 92521.
Long JR; Department of Biochemistry and Molecular Biology, McKnight Brain Institute, National High Magnetic Field Laboratory, University of Florida, Gainesville, FL 32610.
Hooley RJ; Department of Chemistry, University of California, Riverside, CA 92521.; Department of Biochemistry, University of California, Riverside, CA 92521.
Mueser TC; Department of Chemistry and Biochemistry, University of Toledo, Toledo, OH 43606.
Dunn MF; Department of Biochemistry, University of California, Riverside, CA 92521; .
Mueller LJ; Department of Chemistry, University of California, Riverside, CA 92521; .
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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] 2022 Jan 11; Vol. 119 (2).
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 :
Catalytic Domain*
Alanine/*analogs & derivatives
Crystallography, X-Ray/*methods
Magnetic Resonance Spectroscopy/*methods
Tryptophan Synthase/*chemistry
Catalysis ; Indoles ; Magnetic Resonance Imaging ; Nuclear Magnetic Resonance, Biomolecular ; Pyridoxal Phosphate/metabolism ; Tryptophan Synthase/metabolism
Czasopismo naukowe
Tytuł :
Seq2Enz: An application of mask BLAST methodology with a new chemical logic of amino acids for improved enzyme function prediction.
Autorzy :
Pathak A; Department of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi 110016, India; Supercomputing Facility for Bioinformatics & Computational Biology, Indian Institute of Technology, Hauz Khas, New Delhi 110016, India.
Jayaram B; Department of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi 110016, India; Supercomputing Facility for Bioinformatics & Computational Biology, Indian Institute of Technology, Hauz Khas, New Delhi 110016, India; Kusuma School of Biological Sciences, Indian Institute of Technology, Hauz Khas, New Delhi 110016, India. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Proteins and proteomics [Biochim Biophys Acta Proteins Proteom] 2022 Jan; Vol. 1870 (1), pp. 140721. Date of Electronic Publication: 2021 Oct 06.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*
Software*
Sequence Analysis, Protein/*methods
Animals ; Enzymes/chemistry ; Enzymes/metabolism ; Humans
Czasopismo naukowe
Tytuł :
Binding interactions in a kinase active site modulate background ATP hydrolysis.
Autorzy :
Wang Y; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal, Quebec H3A 0B8, Canada.
Hanrahan G; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal, Quebec H3A 0B8, Canada.
Azar FA; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal, Quebec H3A 0B8, Canada.
Mittermaier A; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal, Quebec H3A 0B8, Canada. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Proteins and proteomics [Biochim Biophys Acta Proteins Proteom] 2022 Jan; Vol. 1870 (1), pp. 140720. Date of Electronic Publication: 2021 Sep 28.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*
Adenosine Triphosphate/*metabolism
Kanamycin Kinase/*metabolism
Allosteric Regulation ; Aminoglycosides/metabolism ; Hydrolysis ; Kanamycin Kinase/chemistry ; Kinetics ; Protein Binding
Czasopismo naukowe
Tytuł :
Histidine protonation states are key in the LigI catalytic reaction mechanism.
Autorzy :
Zhao LN; Department of Clinical Sciences, Lund University, Malmö, Sweden.
Mondal D; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California, USA.
Li W; School of Physics, Shandong University, Jinan, China.
Mu Y; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Kaldis P; Department of Clinical Sciences, Lund University, Malmö, Sweden.
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Źródło :
Proteins [Proteins] 2022 Jan; Vol. 90 (1), pp. 123-130. Date of Electronic Publication: 2021 Aug 09.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*
Carboxylic Ester Hydrolases/*chemistry
Histidine/*chemistry
Carboxylic Ester Hydrolases/metabolism ; Catalysis ; Histidine/metabolism ; Hydrolysis ; Lignin/chemistry ; Lignin/metabolism ; Protons
Czasopismo naukowe
Tytuł :
Crystal structure of a novel putative sugar isomerase from the psychrophilic bacterium Paenibacillus sp. R4.
Autorzy :
Kwon S; Department of Biotechnology, Konkuk University, Chungju, Chungbuk, 27478, Republic of Korea.
Ha HJ; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea.
Kang YJ; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea.
Sung JH; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea.
Hwang J; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon, 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, Republic of Korea.
Lee MJ; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.
Lee JH; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon, 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, Republic of Korea. Electronic address: .
Park HH; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea. Electronic address: .
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Źródło :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2021 Dec 31; Vol. 585, pp. 48-54. Date of Electronic Publication: 2021 Nov 11.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*
Protein Conformation*
Bacterial Proteins/*chemistry
Paenibacillus/*enzymology
Triose-Phosphate Isomerase/*chemistry
Amino Acids/genetics ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites/genetics ; Crystallography, X-Ray ; Metals/chemistry ; Metals/metabolism ; Models, Molecular ; Paenibacillus/genetics ; Triose-Phosphate Isomerase/genetics ; Triose-Phosphate Isomerase/metabolism
Czasopismo naukowe
Tytuł :
Modeling an Enzyme Active Site using Molecular Visualization Freeware.
Autorzy :
Procko K; The University of Texas at Austin; .
Bakheet S; The University of Texas at Austin.
Beckham JT; The University of Texas at Austin.
Franzen MA; Mount Mary University.
Jakubowski H; College of St. Benedict/St. John's University.
Novak WRP; Wabash College.
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Źródło :
Journal of visualized experiments : JoVE [J Vis Exp] 2021 Dec 25 (178). Date of Electronic Publication: 2021 Dec 25.
Typ publikacji :
Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Video-Audio Media
MeSH Terms :
Catalytic Domain*
Humans ; Ligands
Czasopismo naukowe
Tytuł :
Caught in motion: human NTHL1 undergoes interdomain rearrangement necessary for catalysis.
Autorzy :
Carroll BL; Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Zahn KE; Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Hanley JP; Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Wallace SS; Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Dragon JA; Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Doublié S; Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2021 Dec 16; Vol. 49 (22), pp. 13165-13178.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Catalytic Domain*
DNA Repair*
Protein Domains*
DNA/*chemistry
Deoxyribonuclease (Pyrimidine Dimer)/*chemistry
Amino Acid Sequence ; Biocatalysis ; DNA/genetics ; DNA/metabolism ; Deoxyribonuclease (Pyrimidine Dimer)/genetics ; Deoxyribonuclease (Pyrimidine Dimer)/metabolism ; Humans ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Pyrimidines/metabolism ; Sequence Homology, Amino Acid
Czasopismo naukowe
Tytuł :
Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions.
Autorzy :
Hamza A; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India.
Samad A; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India.
Imam MA; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India.
Faizan MI; Multidisciplinary Centre for Advance Research and Studies, Jamia Millia Islamia, New Delhi 110025, India.
Ahmed A; Center of Excellence in Biotechnology Research, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.
Almajhdi FN; Center of Excellence in Biotechnology Research, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.; Department of Botany & Microbiology, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.
Hussain T; Center of Excellence in Biotechnology Research, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.
Islam A; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India.
Parveen S; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India.
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Źródło :
Molecules (Basel, Switzerland) [Molecules] 2021 Dec 06; Vol. 26 (23). Date of Electronic Publication: 2021 Dec 06.
Typ publikacji :
Journal Article
MeSH Terms :
Catalytic Domain*
Host-Pathogen Interactions*
Heparitin Sulfate/*metabolism
Molecular Docking Simulation/*methods
Respiratory Syncytial Virus, Human/*metabolism
Viral Envelope Proteins/*chemistry
Viral Envelope Proteins/*metabolism
Cell Membrane/metabolism ; Humans ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Protein Aggregates ; Protein Aggregation, Pathological/metabolism ; Protein Denaturation/drug effects ; Protein Structure, Tertiary ; Spectrometry, Fluorescence/methods ; Urea/pharmacology
Czasopismo naukowe
Tytuł :
A Panel of Engineered Ubiquitin Variants Targeting the Family of Domains Found in Ubiquitin Specific Proteases (DUSPs).
Autorzy :
Tang JQ; The Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada. Electronic address: https://twitter.com/jasonqtang.
Veggiani G; The Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada.
Singer A; The Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada.
Teyra J; The Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada.
Chung J; The Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada.
Sidhu SS; The Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Dec 03; Vol. 433 (24), pp. 167300. Date of Electronic Publication: 2021 Oct 16.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*
Ubiquitin/*chemistry
Ubiquitin-Specific Proteases/*chemistry
Biocatalysis ; Conserved Sequence ; Humans ; Peptide Library ; Protein Engineering ; Sequence Alignment ; Substrate Specificity ; Ubiquitin/genetics ; Ubiquitin-Specific Proteases/genetics
Czasopismo naukowe
Tytuł :
Visualizing transiently associated catalytic domains in assembly-line biosynthesis using cryo-electron microscopy.
Autorzy :
Faylo JL; Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Christianson DW; Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA. Electronic address: .
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Źródło :
Journal of structural biology [J Struct Biol] 2021 Dec; Vol. 213 (4), pp. 107802. Date of Electronic Publication: 2021 Oct 01.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
Catalytic Domain*
Cryoelectron Microscopy/*methods
Enzymes/*ultrastructure
Fatty Acids/*biosynthesis
Multiprotein Complexes/*ultrastructure
Polyketides/*metabolism
Terpenes/*metabolism
Alkyl and Aryl Transferases/chemistry ; Alkyl and Aryl Transferases/metabolism ; Alkyl and Aryl Transferases/ultrastructure ; Crystallography, X-Ray ; Enzymes/chemistry ; Enzymes/metabolism ; Fatty Acid Synthases/chemistry ; Fatty Acid Synthases/metabolism ; Fatty Acid Synthases/ultrastructure ; Imaging, Three-Dimensional/methods ; Models, Molecular ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Polyketide Synthases/chemistry ; Polyketide Synthases/metabolism ; Polyketide Synthases/ultrastructure ; Protein Binding ; Reproducibility of Results
Czasopismo naukowe
Tytuł :
Conformational flexibility of the conserved hydrophobic pocket of HIV-1 gp41. Implications for the discovery of small-molecule fusion inhibitors.
Autorzy :
Cano-Muñoz M; Departamento de Química Física, Instituto de Biotecnología y Unidad de Excelencia de Química Aplicada a Biomedicina y Medioambiente (UEQ), Facultad de Ciencias, Universidad de Granada, 18071 Granada, Spain. Electronic address: .
Jurado S; Departamento de Química Física, Instituto de Biotecnología y Unidad de Excelencia de Química Aplicada a Biomedicina y Medioambiente (UEQ), Facultad de Ciencias, Universidad de Granada, 18071 Granada, Spain.
Morel B; Departamento de Química Física, Instituto de Biotecnología y Unidad de Excelencia de Química Aplicada a Biomedicina y Medioambiente (UEQ), Facultad de Ciencias, Universidad de Granada, 18071 Granada, Spain.
Conejero-Lara F; Departamento de Química Física, Instituto de Biotecnología y Unidad de Excelencia de Química Aplicada a Biomedicina y Medioambiente (UEQ), Facultad de Ciencias, Universidad de Granada, 18071 Granada, Spain. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2021 Dec 01; Vol. 192, pp. 90-99. Date of Electronic Publication: 2021 Oct 05.
Typ publikacji :
Journal Article
MeSH Terms :
Amino Acid Sequence*
Catalytic Domain*
Conserved Sequence*
Hydrophobic and Hydrophilic Interactions*
Models, Molecular*
Protein Conformation*
HIV Envelope Protein gp41/*chemistry
Binding Sites ; Drug Design ; HIV Envelope Protein gp41/antagonists & inhibitors ; HIV Fusion Inhibitors/chemistry ; HIV Fusion Inhibitors/pharmacology ; Humans ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Peptide Fragments/chemistry ; Protein Binding ; Spectrum Analysis ; Thermodynamics
Czasopismo naukowe
Tytuł :
The crystal structure of the domain-swapped dimer of onconase highlights some catalytic and antitumor activity features of the enzyme.
Autorzy :
Gotte G; Department of Neuroscience, Biomedicine and Movement Sciences, Biological Chemistry Section, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy. Electronic address: .
Campagnari R; Department of Neuroscience, Biomedicine and Movement Sciences, Biological Chemistry Section, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy.
Loreto D; Department of Chemical Sciences, University of Naples Federico II, Via Cintia, 80126 Naples, Italy.
Bettin I; Department of Neuroscience, Biomedicine and Movement Sciences, Biological Chemistry Section, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy.
Calzetti F; Department of Medicine, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy.
Menegazzi M; Department of Neuroscience, Biomedicine and Movement Sciences, Biological Chemistry Section, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy. Electronic address: .
Merlino A; Department of Chemical Sciences, University of Naples Federico II, Via Cintia, 80126 Naples, Italy. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2021 Nov 30; Vol. 191, pp. 560-571. Date of Electronic Publication: 2021 Sep 24.
Typ publikacji :
Journal Article
MeSH Terms :
Catalytic Domain*
Antineoplastic Agents/*chemistry
Melanoma/*metabolism
Ribonucleases/*chemistry
Antineoplastic Agents/pharmacology ; Apoptosis ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Humans ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Ribonucleases/metabolism ; STAT3 Transcription Factor/genetics ; STAT3 Transcription Factor/metabolism
Czasopismo naukowe
Tytuł :
Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.
Autorzy :
Loch JI; Department of Crystal Chemistry and Crystal Physics, Faculty of Chemistry, Jagiellonian University, Krakow, Poland.
Imiolczyk B; Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
Sliwiak J; Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
Wantuch A; Department of Crystal Chemistry and Crystal Physics, Faculty of Chemistry, Jagiellonian University, Krakow, Poland.
Bejger M; Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
Gilski M; Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.; Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland.
Jaskolski M; Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland. .; Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland. .
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Źródło :
Nature communications [Nat Commun] 2021 Nov 18; Vol. 12 (1), pp. 6717. Date of Electronic Publication: 2021 Nov 18.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Catalytic Domain*
Asparaginase/*metabolism
Bacterial Proteins/*metabolism
Rhizobium etli/*enzymology
Asparaginase/chemistry ; Asparaginase/genetics ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Binding Sites/genetics ; Biocatalysis ; Cations/chemistry ; Cations/metabolism ; Crystallography, X-Ray ; Enzyme Stability ; Hydrogen-Ion Concentration ; Kinetics ; Metals/chemistry ; Metals/metabolism ; Models, Molecular ; Mutation ; Protein Binding ; Protein Folding ; Protein Multimerization ; Rhizobium etli/genetics ; Temperature
Czasopismo naukowe
Tytuł :
FAN1's protection against CGG repeat expansion requires its nuclease activity and is FANCD2-independent.
Autorzy :
Zhao X; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
Lu H; Laboratory Animal Sciences section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
Usdin K; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2021 Nov 18; Vol. 49 (20), pp. 11643-11652.
Typ publikacji :
Journal Article; Research Support, N.I.H., Intramural
MeSH Terms :
Catalytic Domain*
Trinucleotide Repeat Expansion*
Endodeoxyribonucleases/*metabolism
Exodeoxyribonucleases/*metabolism
Multifunctional Enzymes/*metabolism
Animals ; DNA Repair Enzymes/metabolism ; Endodeoxyribonucleases/chemistry ; Endodeoxyribonucleases/genetics ; Exodeoxyribonucleases/chemistry ; Exodeoxyribonucleases/genetics ; Fanconi Anemia Complementation Group D2 Protein/genetics ; Fanconi Anemia Complementation Group D2 Protein/metabolism ; Mice ; Mice, Inbred C57BL ; Multifunctional Enzymes/chemistry ; Multifunctional Enzymes/genetics ; MutS Homolog 3 Protein/metabolism ; Point Mutation
Czasopismo naukowe

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