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Wyszukujesz frazę ""Mutant Proteins"" wg kryterium: Temat


Tytuł :
DNA-binding properties of the MADS-domain transcription factor SEPALLATA3 and mutant variants characterized by SELEX-seq.
Autorzy :
Käppel S; Matthias Schleiden Institute/Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743, Jena, Germany.
Eggeling R; Department of Computer Science, University of Helsinki, Pietari Kalmin katu 5, 00014, Helsinki, Finland.; Methods in Medical Informatics, Department of Computer Science, University of Tübingen, Sand 14, 72076, Tübingen, Germany.; Institute for Biomedical Informatics, University of Tübingen, Tübingen, Germany.
Rümpler F; Matthias Schleiden Institute/Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743, Jena, Germany.
Groth M; Leibniz Institute on Aging-Fritz Lipmann Institute (FLI), Core Facility DNA Sequencing, Beutenbergstraße 11, 07745, Jena, Germany.
Melzer R; School of Biology and Environmental Science and Earth Institute, University College Dublin, Belfield, Dublin 4, Ireland.
Theißen G; Matthias Schleiden Institute/Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743, Jena, Germany. .
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Źródło :
Plant molecular biology [Plant Mol Biol] 2021 Mar; Vol. 105 (4-5), pp. 543-557. Date of Electronic Publication: 2021 Jan 24.
Typ publikacji :
Journal Article
MeSH Terms :
Arabidopsis Proteins/*metabolism
DNA, Plant/*metabolism
Homeodomain Proteins/*metabolism
Mutant Proteins/*metabolism
SELEX Aptamer Technique/*methods
Transcription Factors/*metabolism
Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/genetics ; Base Sequence ; Binding Sites/genetics ; DNA, Plant/chemistry ; DNA, Plant/genetics ; Homeodomain Proteins/chemistry ; Homeodomain Proteins/genetics ; Models, Molecular ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Mutation ; Nucleic Acid Conformation ; Protein Binding ; Protein Domains ; Transcription Factors/chemistry ; Transcription Factors/genetics
Czasopismo naukowe
Tytuł :
Inhibition of RANKL-Induced Osteoclastogenesis by Novel Mutant RANKL.
Autorzy :
Jang Y; Laboratory of Orthopaedic Research, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.; Department of Orthopaedic Surgery, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.
Sohn HM; Laboratory of Orthopaedic Research, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.; Department of Orthopaedic Surgery, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.
Ko YJ; Laboratory of Orthopaedic Research, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.; Department of Orthopaedic Surgery, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.
Hyun H; Department of Biomedical Sciences Chonnam National University Medical School, Gwangju 61469, Korea.
Lim W; Laboratory of Orthopaedic Research, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.; Department of Orthopaedic Surgery, Chosun University Hospital, Dong-Gu, Gwangju 61452, Korea.; Department of Premedical Science, College of Medicine, Chosun University, Dong-Gu, Gwangju 61452, Korea.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Jan 04; Vol. 22 (1). Date of Electronic Publication: 2021 Jan 04.
Typ publikacji :
Journal Article
MeSH Terms :
Mutation*
Osteogenesis*
Mutant Proteins/*metabolism
Osteoclasts/*cytology
RANK Ligand/*metabolism
Animals ; Cells, Cultured ; Female ; Mice ; Mice, Inbred C57BL ; Mutant Proteins/administration & dosage ; Mutant Proteins/genetics ; Osteoclasts/metabolism ; RANK Ligand/genetics ; Signal Transduction
Czasopismo naukowe
Tytuł :
Structure-Based Virtual Screening to Discover Potential Lead Molecules for the SARS-CoV-2 Main Protease.
Autorzy :
Gahlawat A; Department of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar 160062, Punjab, India.
Kumar N; Department of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar 160062, Punjab, India.
Kumar R; Department of Clinical Microbiology and Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, SE-90185 Umeå, Sweden.
Sandhu H; Department of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar 160062, Punjab, India.
Singh IP; Department of Natural Products, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar 160062, Punjab, India.
Singh S; Department of Pharmaceutical Analysis, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar 160062, Punjab, India.
Sjöstedt A; Department of Clinical Microbiology and Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, SE-90185 Umeå, Sweden.
Garg P; Department of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar 160062, Punjab, India.
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Źródło :
Journal of chemical information and modeling [J Chem Inf Model] 2020 Dec 28; Vol. 60 (12), pp. 5781-5793. Date of Electronic Publication: 2020 Aug 04.
Typ publikacji :
Journal Article
MeSH Terms :
Antiviral Agents/*chemistry
COVID-19/*drug therapy
Coronavirus 3C Proteases/*chemistry
Mutant Proteins/*chemistry
SARS-CoV-2/*drug effects
Viral Protease Inhibitors/*chemistry
Amino Acid Sequence ; Antiviral Agents/metabolism ; Antiviral Agents/pharmacology ; Catalytic Domain ; Coronavirus 3C Proteases/metabolism ; Databases, Factual ; Drug Design ; Humans ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Mutant Proteins/metabolism ; Protein Conformation ; Structure-Activity Relationship ; Viral Protease Inhibitors/metabolism ; Viral Protease Inhibitors/pharmacology
Czasopismo naukowe
Tytuł :
Trametinib Induces the Stabilization of a Dual GNAQ p.Gly48Leu- and FGFR4 p.Cys172Gly-Mutated Uveal Melanoma. The Role of Molecular Modelling in Personalized Oncology.
Autorzy :
Krebs FS; Computer-aided molecular engineering group, Department of Fundamental Oncology, Lausanne University, Ludwig Lausanne Branch, 1066 Epalinges, Switzerland.
Gérard C; Precision Oncology Center, Department of Oncology, Lausanne University Hospital, 1011 Lausanne, Switzerland.
Wicky A; Precision Oncology Center, Department of Oncology, Lausanne University Hospital, 1011 Lausanne, Switzerland.
Aedo-Lopez V; Service of Medical Oncology, Department of Oncology, Lausanne University Hospital, 1011 Lausanne, Switzerland.
Missiaglia E; SIB Swiss Institute of Bioinformatics, 1015 Lausanne, Switzerland.; University Institute of Pathology, Lausanne University Hospital, 1011 Lausanne, Switzerland.
Bisig B; University Institute of Pathology, Lausanne University Hospital, 1011 Lausanne, Switzerland.
Trimech M; University Institute of Pathology, Lausanne University Hospital, 1011 Lausanne, Switzerland.
Michielin O; Precision Oncology Center, Department of Oncology, Lausanne University Hospital, 1011 Lausanne, Switzerland.; Service of Medical Oncology, Department of Oncology, Lausanne University Hospital, 1011 Lausanne, Switzerland.; SIB Swiss Institute of Bioinformatics, 1015 Lausanne, Switzerland.
Homicsko K; Precision Oncology Center, Department of Oncology, Lausanne University Hospital, 1011 Lausanne, Switzerland.; SIB Swiss Institute of Bioinformatics, 1015 Lausanne, Switzerland.; Laboratory of Translational Oncology, EPFL, 1015 Lausanne, Switzerland.
Zoete V; Computer-aided molecular engineering group, Department of Fundamental Oncology, Lausanne University, Ludwig Lausanne Branch, 1066 Epalinges, Switzerland.; SIB Swiss Institute of Bioinformatics, 1015 Lausanne, Switzerland.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2020 Oct 28; Vol. 21 (21). Date of Electronic Publication: 2020 Oct 28.
Typ publikacji :
Case Reports; Journal Article
MeSH Terms :
Mutation*
GTP-Binding Protein alpha Subunits, Gq-G11/*chemistry
Melanoma/*drug therapy
Melanoma/*genetics
Mutant Proteins/*chemistry
Pyridones/*therapeutic use
Pyrimidinones/*therapeutic use
Receptor, Fibroblast Growth Factor, Type 4/*chemistry
Uveal Neoplasms/*drug therapy
Uveal Neoplasms/*genetics
Amino Acid Sequence ; Antineoplastic Agents/therapeutic use ; Female ; GTP-Binding Protein alpha Subunits, Gq-G11/genetics ; GTP-Binding Protein alpha Subunits, Gq-G11/metabolism ; Humans ; Melanoma/metabolism ; Melanoma/pathology ; Middle Aged ; Models, Molecular ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Protein Conformation ; Protein Stability ; Receptor, Fibroblast Growth Factor, Type 4/genetics ; Receptor, Fibroblast Growth Factor, Type 4/metabolism ; Sequence Homology ; Signal Transduction ; Uveal Neoplasms/metabolism ; Uveal Neoplasms/pathology
SCR Disease Name :
Uveal melanoma
Czasopismo naukowe
Tytuł :
Familial Alzheimer's disease mutations at position 22 of the amyloid β-peptide sequence differentially affect synaptic loss, tau phosphorylation and neuronal cell death in an ex vivo system.
Autorzy :
Tackenberg C; Institute for Regenerative Medicine, University of Zurich, Schlieren, Switzerland.; Neuroscience Center Zurich, University of Zurich and ETH Zurich, Zurich, Switzerland.
Kulic L; Institute for Regenerative Medicine, University of Zurich, Schlieren, Switzerland.; Neuroscience Center Zurich, University of Zurich and ETH Zurich, Zurich, Switzerland.
Nitsch RM; Institute for Regenerative Medicine, University of Zurich, Schlieren, Switzerland.; Neuroscience Center Zurich, University of Zurich and ETH Zurich, Zurich, Switzerland.
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Źródło :
PloS one [PLoS One] 2020 Sep 23; Vol. 15 (9), pp. e0239584. Date of Electronic Publication: 2020 Sep 23 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Mutation*
Alzheimer Disease/*genetics
Alzheimer Disease/*metabolism
Amyloid beta-Peptides/*genetics
Mutant Proteins/*genetics
tau Proteins/*metabolism
Alzheimer Disease/pathology ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Animals ; Cell Death ; Dendritic Spines/pathology ; Hippocampus/metabolism ; Hippocampus/pathology ; Humans ; In Vitro Techniques ; Kinetics ; Mice ; Mice, Transgenic ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Neurons/metabolism ; Neurons/pathology ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Phosphorylation ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Synapses/pathology
Czasopismo naukowe
Tytuł :
The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization.
Autorzy :
Marvian AT; Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology, Tehran, Iran; Department of Neurology, School of Medicine, Technical University of Munich, Munich, Germany; Department of Translational Neurodegeneration, German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.
Aliakbari F; Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology, Tehran, Iran; Interdisciplinary Nanoscience Centre (iNANO), Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 14, DK-8000 Aarhus C, Denmark.
Mohammad-Beigi H; Interdisciplinary Nanoscience Centre (iNANO), Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 14, DK-8000 Aarhus C, Denmark.
Ahmadi ZA; Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology, Tehran, Iran.
Mehrpooyan S; Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology, Tehran, Iran.
Lermyte F; School of Engineering, University of Warwick, Coventry, UK.
Nasouti M; Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology, Tehran, Iran.
Collingwood JF; School of Engineering, University of Warwick, Coventry, UK.
Otzen DE; Interdisciplinary Nanoscience Centre (iNANO), Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 14, DK-8000 Aarhus C, Denmark.
Morshedi D; Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology, Tehran, Iran. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2020 Jul 15; Vol. 155, pp. 543-550. Date of Electronic Publication: 2020 Mar 31.
Typ publikacji :
Journal Article
MeSH Terms :
Mutation*
Amyloid/*chemistry
Mutant Proteins/*chemistry
alpha-Synuclein/*chemistry
Humans ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Protein Interaction Domains and Motifs ; Protein Multimerization ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
Czasopismo naukowe
Tytuł :
Parkinson's disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure.
Autorzy :
Zhao K; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Li Y; Key Laboratory of Protein Sciences (Tsinghua University), Ministry of Education, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Liu Z; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Long H; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Zhao C; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Luo F; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Sun Y; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Tao Y; Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai, 200030, China.
Su XD; State Key Laboratory of Protein and Plant Gene Research, and Biomedical Pioneering Innovation Center (BIOPIC), School of Life Sciences, Peking University, Beijing, 100871, China.
Li D; Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai, 200030, China. .; Bio-X-Renji Hospital Research Center, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200240, China. .
Li X; Key Laboratory of Protein Sciences (Tsinghua University), Ministry of Education, School of Life Sciences, Tsinghua University, Beijing, 100084, China. .
Liu C; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China. .; University of Chinese Academy of Sciences, Beijing, 100049, China. .
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Źródło :
Nature communications [Nat Commun] 2020 May 26; Vol. 11 (1), pp. 2643. Date of Electronic Publication: 2020 May 26.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Mutant Proteins/*chemistry
Mutant Proteins/*genetics
Parkinson Disease/*genetics
Parkinson Disease/*metabolism
alpha-Synuclein/*chemistry
alpha-Synuclein/*genetics
Acetylation ; Amino Acid Sequence ; Amino Acid Substitution ; Amyloid/chemistry ; Amyloid/genetics ; Amyloid/ultrastructure ; Cryoelectron Microscopy ; Humans ; Microscopy, Atomic Force ; Models, Molecular ; Mutant Proteins/ultrastructure ; Mutation, Missense ; Protein Conformation ; Protein Stability ; Static Electricity ; alpha-Synuclein/ultrastructure
Czasopismo naukowe
Tytuł :
Truncated Pneumolysin from Streptococcus pneumoniae as a TLR4-Antagonizing New Drug for Chronic Inflammatory Conditions.
Autorzy :
Chang SF; Department of Medical Research and Development, Chiayi Chang Gung Memorial Hospital, Chiayi 613, Taiwan.
Chen CN; Department of Biochemical Science and Technology, National Chiayi University, Chiayi 600, Taiwan.
Lin JC; Division of Infectious Diseases and Tropical Medicine, Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei 112, Taiwan.
Wang HE; Department of Biomedical Imaging and Radiological Sciences, National Yang-Ming University, Taipei 112, Taiwan.; Program in Molecular Medicine, National Yang-Ming University and Academia Sinica, Taipei 112, Taiwan.; Biophotonics & Molecular Imaging Research Center, National Yang-Ming University, Taipei 112, Taiwan.
Mori S; Department of Bacteriology II, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Li JJ; Division of Infectious Diseases and Tropical Medicine, Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei 112, Taiwan.; KeMyth Biotech Corporation, Innovation and Incubation Center, National Chiayi University, Chiayi 600, Taiwan.
Yen CK; Department of Biochemical Science and Technology, National Chiayi University, Chiayi 600, Taiwan.
Hsu CY; Division of Infectious Diseases and Tropical Medicine, Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei 112, Taiwan.
Fung CP; Section of Infectious Diseases, Department of Medicine, Taipei Veterans General Hospital, Taipei 112, Taiwan.
Chong PC; Graduate Institute of Basic Medical Science, China Medical University, Taichung 404, Taiwan.
Leng CH; National Institute of Infectious Diseases and Vaccinology, National Health Research Institutes, Miaoli 350, Taiwan.
Ding YJ; National Institute of Infectious Diseases and Vaccinology, National Health Research Institutes, Miaoli 350, Taiwan.
Chang FY; Division of Infectious Diseases and Tropical Medicine, Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei 112, Taiwan.
Siu LK; Division of Infectious Diseases and Tropical Medicine, Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei 112, Taiwan.; KeMyth Biotech Corporation, Innovation and Incubation Center, National Chiayi University, Chiayi 600, Taiwan.; National Institute of Infectious Diseases and Vaccinology, National Health Research Institutes, Miaoli 350, Taiwan.
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Źródło :
Cells [Cells] 2020 May 09; Vol. 9 (5). Date of Electronic Publication: 2020 May 09.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Inflammation/*drug therapy
Mutant Proteins/*pharmacology
Mutant Proteins/*therapeutic use
Streptococcus pneumoniae/*metabolism
Streptolysins/*pharmacology
Toll-Like Receptor 4/*antagonists & inhibitors
Amino Acid Sequence ; Animals ; Apoptosis/drug effects ; Bacterial Proteins/chemistry ; Bacterial Proteins/pharmacology ; Binding Sites ; Caspase 3/metabolism ; Cell Survival/drug effects ; Diet, High-Fat ; E-Selectin/metabolism ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Human Umbilical Vein Endothelial Cells/drug effects ; Human Umbilical Vein Endothelial Cells/metabolism ; Humans ; Intercellular Adhesion Molecule-1/metabolism ; Lipopolysaccharides ; Mice ; Molecular Docking Simulation ; Mutant Proteins/chemistry ; NF-kappa B/metabolism ; Neutrophils/cytology ; Neutrophils/drug effects ; Phosphorylation/drug effects ; Solubility ; Streptolysins/chemistry ; Streptozocin ; Toll-Like Receptor 4/metabolism ; Transendothelial and Transepithelial Migration/drug effects ; Vascular Cell Adhesion Molecule-1/metabolism
Czasopismo naukowe
Tytuł :
The pharmacological chaperone N-n-butyl-deoxygalactonojirimycin enhances β-galactosidase processing and activity in fibroblasts of a patient with infantile GM1-gangliosidosis.
Autorzy :
Mohamed FE; Department of Pathology, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates.
Al Sorkhy M; Department of Pharmacology, Al Ain University, Al Ain, United Arab Emirates.
Ghattas MA; Department of Pharmacology, Al Ain University, Al Ain, United Arab Emirates.
Al-Gazali L; Department of Paediatrics, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates.
Al-Dirbashi O; Department of Paediatrics, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates.
Al-Jasmi F; Department of Paediatrics, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates.; Department of Genetics and Genomics College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates.
Ali BR; Department of Pathology, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates. .; Department of Genetics and Genomics College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates. .; Zayed Center for Health Sciences, United Arab Emirates University, Al-Ain, United Arab Emirates. .
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Źródło :
Human genetics [Hum Genet] 2020 May; Vol. 139 (5), pp. 657-673. Date of Electronic Publication: 2020 Mar 26.
Typ publikacji :
Case Reports; Journal Article
MeSH Terms :
Mutation*
1-Deoxynojirimycin/*pharmacology
Fibroblasts/*metabolism
Gangliosidosis, GM1/*metabolism
Mutant Proteins/*metabolism
Protein Processing, Post-Translational/*drug effects
beta-Galactosidase/*metabolism
1-Deoxynojirimycin/chemistry ; Child, Preschool ; Endoplasmic Reticulum Stress/drug effects ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Fibroblasts/drug effects ; Fibroblasts/pathology ; Gangliosidosis, GM1/drug therapy ; Gangliosidosis, GM1/pathology ; Humans ; Lysosomes/drug effects ; Lysosomes/metabolism ; Lysosomes/pathology ; Male ; Molecular Chaperones/pharmacology ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Protein Conformation ; Protein Transport ; beta-Galactosidase/chemistry ; beta-Galactosidase/genetics
Czasopismo naukowe
Tytuł :
A High-Throughput Screening System Based on Droplet Microfluidics for Glucose Oxidase Gene Libraries.
Autorzy :
Prodanović R; Faculty of Chemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia.; Department of Physics, School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138, USA.
Ung WL; Department of Physics, School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138, USA.
Đurđić KI; Faculty of Chemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia.
Fischer R; Departments of Biological Sciences and Chemistry, Purdue University, 207 S. Martin Jischke Dr., West Lafayette, IN 47907, USA.
Weitz DA; Department of Physics, School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138, USA.
Ostafe R; Purdue Institute of Inflammation, Immunology and Infectious Disease, Molecular Evolution, Protein Engineering and Production, Purdue University, 207 S. Martin Jischke Dr., West Lafayette, IN 47907, USA.
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Źródło :
Molecules (Basel, Switzerland) [Molecules] 2020 May 22; Vol. 25 (10). Date of Electronic Publication: 2020 May 22.
Typ publikacji :
Journal Article
MeSH Terms :
High-Throughput Screening Assays*
Glucose Oxidase/*genetics
Mutant Proteins/*genetics
Saccharomyces cerevisiae/*genetics
Directed Molecular Evolution ; Flow Cytometry ; Gene Library ; Glucose Oxidase/chemistry ; Glucose Oxidase/isolation & purification ; Lab-On-A-Chip Devices ; Mutagenesis/genetics ; Mutant Proteins/isolation & purification ; Protein Conformation ; Protein Engineering ; Saccharomyces cerevisiae/enzymology ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
A Chitosanase mutant from Streptomyces sp. N174 prefers to produce functional chitopentasaccharide.
Autorzy :
Ding M; Endoscopy Center, China Japan Union Hospital of Jilin University, Changchun 130033, China.
Zhang T; Gastrointestinal and Colorectal Surgery, China Japan Union Hospital of Jilin University, Changchun 130033, China.
Sun C; Endoscopy Center, China Japan Union Hospital of Jilin University, Changchun 130033, China.
Zhang H; Endoscopy Center, China Japan Union Hospital of Jilin University, Changchun 130033, China. Electronic address: .
Zhang Y; Endoscopy Center, China Japan Union Hospital of Jilin University, Changchun 130033, China. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2020 May 15; Vol. 151, pp. 1091-1098. Date of Electronic Publication: 2019 Nov 15.
Typ publikacji :
Journal Article
MeSH Terms :
Mutant Proteins*
Chitosan/*chemistry
Glycoside Hydrolases/*chemistry
Streptomyces/*enzymology
Amino Acid Sequence ; Chitosan/metabolism ; Codon ; Gastrointestinal Microbiome ; Gene Expression ; Glycoside Hydrolases/genetics ; Hydrolysis ; Mass Spectrometry ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Engineering
Czasopismo naukowe
Tytuł :
Atypical chemokine receptor ACKR2-V41A has decreased CCL2 binding, scavenging, and activation, supporting sustained inflammation and increased Alzheimer's disease risk.
Autorzy :
Murcia JDG; Brigham Young University, Department of Biology, 4102 Life Sciences Building, Provo, Utah, 84602, USA.
Weinert A; Brigham Young University, Department of Microbiology and Molecular Biology, 4007 Life Sciences Building, Provo, Utah, 84602, USA.
Freitas CMT; Brigham Young University, Department of Microbiology and Molecular Biology, 4007 Life Sciences Building, Provo, Utah, 84602, USA.; Roseman University of Health Science College of Dental Medicine 10894 S, River Front Parkway, South Jordan, UT, 84095, USA.
Arens DK; Brigham Young University, Department of Microbiology and Molecular Biology, 4007 Life Sciences Building, Provo, Utah, 84602, USA.
Ferrel MN; Brigham Young University, Department of Biology, 4102 Life Sciences Building, Provo, Utah, 84602, USA.
Grose JH; Brigham Young University, Department of Microbiology and Molecular Biology, 4007 Life Sciences Building, Provo, Utah, 84602, USA.
Ridge PG; Brigham Young University, Department of Biology, 4102 Life Sciences Building, Provo, Utah, 84602, USA.
Wilson E; Brigham Young University, Department of Microbiology and Molecular Biology, 4007 Life Sciences Building, Provo, Utah, 84602, USA.
Kauwe JSK; Brigham Young University, Department of Biology, 4102 Life Sciences Building, Provo, Utah, 84602, USA. .
Weber KS; Brigham Young University, Department of Microbiology and Molecular Biology, 4007 Life Sciences Building, Provo, Utah, 84602, USA. .
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Źródło :
Scientific reports [Sci Rep] 2020 May 15; Vol. 10 (1), pp. 8019. Date of Electronic Publication: 2020 May 15.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Mutant Proteins*
Alzheimer Disease/*etiology
Chemokine CCL2/*metabolism
Inflammation/*metabolism
Receptors, Chemokine/*chemistry
Receptors, Chemokine/*metabolism
Actin Depolymerizing Factors/metabolism ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amino Acid Substitution ; Animals ; CHO Cells ; Cricetulus ; Disease Susceptibility ; Humans ; Hydrophobic and Hydrophilic Interactions ; Inflammation/complications ; Inflammation/genetics ; Kinetics ; Models, Molecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Receptors, Chemokine/genetics ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
A small molecule chaperone rescues the stability and activity of a cancer-associated variant of NAD(P)H:quinone oxidoreductase 1 in vitro.
Autorzy :
Strandback E; Institute of Biochemistry, Graz University of Technology, Austria.
Lienhart WD; Institute of Biochemistry, Graz University of Technology, Austria.
Hromic-Jahjefendic A; Institute of Molecular Biosciences, University of Graz, Austria.; Department of Genetics and Bioengineering, Faculty of Engineering and Natural Sciences, International University of Sarajevo, Sarajevo, Bosnia and Herzegovina.
Bourgeois B; Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Molecular Biology and Biochemistry, Medical University of Graz, Austria.
Högler A; Institute of Biochemistry, Graz University of Technology, Austria.
Waltenstorfer D; Institute of Biochemistry, Graz University of Technology, Austria.
Winkler A; Institute of Biochemistry, Graz University of Technology, Austria.
Zangger K; Institute of Chemistry, University of Graz, Austria.
Madl T; Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Molecular Biology and Biochemistry, Medical University of Graz, Austria.; BioTechMed-Graz, Austria.
Gruber K; Institute of Molecular Biosciences, University of Graz, Austria.
Macheroux P; Institute of Biochemistry, Graz University of Technology, Austria.
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Źródło :
FEBS letters [FEBS Lett] 2020 Feb; Vol. 594 (3), pp. 424-438. Date of Electronic Publication: 2019 Oct 30.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Mutation*
Mutant Proteins/*genetics
Mutant Proteins/*metabolism
NAD(P)H Dehydrogenase (Quinone)/*genetics
NAD(P)H Dehydrogenase (Quinone)/*metabolism
Neoplasms/*genetics
Amino Acid Sequence ; Drug Evaluation, Preclinical ; Enzyme Activation/drug effects ; Enzyme Stability/drug effects ; Ligands ; Molecular Docking Simulation ; Mutant Proteins/antagonists & inhibitors ; Mutant Proteins/chemistry ; NAD(P)H Dehydrogenase (Quinone)/antagonists & inhibitors ; NAD(P)H Dehydrogenase (Quinone)/chemistry ; Protein Conformation
Czasopismo naukowe
Tytuł :
Mechanism and functional role of the interaction between CP190 and the architectural protein Pita in Drosophila melanogaster.
Autorzy :
Sabirov, Marat (AUTHOR)
Kyrchanova, Olga (AUTHOR)
Pokholkova, Galina V. (AUTHOR)
Bonchuk, Artem (AUTHOR)
Klimenko, Natalia (AUTHOR)
Belova, Elena (AUTHOR)
Zhimulev, Igor F. (AUTHOR)
Maksimenko, Oksana (AUTHOR)
Georgiev, Pavel (AUTHOR)
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Źródło :
Epigenetics & Chromatin. 3/22/2021, Vol. 14 Issue 1, p1-16. 16p.
Czasopismo naukowe
Tytuł :
Exploiting the activity-stability trade-off of glucose oxidase from Aspergillus niger using a simple approach to calculate thermostability of mutants.
Autorzy :
Jiang X; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Wang Y; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Wang Y; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Huang H; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Bai Y; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Su X; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Zhang J; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Yao B; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Tu T; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China. Electronic address: .
Luo H; Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China. Electronic address: .
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Źródło :
Food chemistry [Food Chem] 2021 Apr 16; Vol. 342, pp. 128270. Date of Electronic Publication: 2020 Oct 02.
Typ publikacji :
Journal Article
MeSH Terms :
Temperature*
Aspergillus niger/*enzymology
Glucose Oxidase/*genetics
Glucose Oxidase/*metabolism
Mutant Proteins/*genetics
Mutant Proteins/*metabolism
Biocatalysis ; Enzyme Stability/genetics ; Kinetics ; Molecular Dynamics Simulation
Czasopismo naukowe
Tytuł :
A novel carcinogenic PI3Kα mutation suggesting the role of helical domain in transmitting nSH2 regulatory signals to kinase domain.
Autorzy :
Ghalamkari S; Department of Genetics and Molecular Biology, Isfahan University of Medical Sciences, Isfahan, Iran.
Alavi S; Department of Cell and Molecular Biology and Microbiology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran.
Mianesaz H; Department of Genetics and Molecular Biology, Isfahan University of Medical Sciences, Isfahan, Iran.
Khosravian F; Cellular, Molecular and Genetics Research Center, Isfahan University of Medical Sciences, Isfahan, Iran; Medical Genetics Research Center of Genome, Isfahan University of Medical Sciences, Isfahan, Iran.
Bahreini A; Department of Human Genetics, Graduate School of Public Health, University of Pittsburgh, PA, USA; KaryoGen, Isfahan, Iran. Electronic address: .
Salehi M; Department of Genetics and Molecular Biology, Isfahan University of Medical Sciences, Isfahan, Iran; Cellular, Molecular and Genetics Research Center, Isfahan University of Medical Sciences, Isfahan, Iran; Medical Genetics Research Center of Genome, Isfahan University of Medical Sciences, Isfahan, Iran. Electronic address: .
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Źródło :
Life sciences [Life Sci] 2021 Mar 15; Vol. 269, pp. 118759. Date of Electronic Publication: 2020 Nov 12.
Typ publikacji :
Journal Article
MeSH Terms :
Signal Transduction*
Carcinogenesis/*genetics
Class I Phosphatidylinositol 3-Kinases/*chemistry
Class I Phosphatidylinositol 3-Kinases/*genetics
Mutation/*genetics
Adult ; Allosteric Regulation ; Biocatalysis ; Exons/genetics ; Female ; Humans ; Middle Aged ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Protein Domains ; Protein Structure, Secondary ; Substrate Specificity
Czasopismo naukowe
Tytuł :
Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis.
Autorzy :
Johnson BA; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Xie X; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Bailey AL; Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, USA.
Kalveram B; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Lokugamage KG; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Muruato A; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Zou J; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Zhang X; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Juelich T; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Smith JK; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Zhang L; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Bopp N; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Schindewolf C; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Vu M; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Vanderheiden A; Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA.; Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, USA.
Winkler ES; Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, USA.; Department of Medicine, Washington University School of Medicine, St Louis, MO, USA.
Swetnam D; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Plante JA; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Aguilar P; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Plante KS; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Popov V; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Lee B; Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Weaver SC; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.; Institute for Human Infection and Immunity, University of Texas Medical Branch, Galveston, TX, USA.
Suthar MS; Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA.; Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, USA.; Yerkes National Primate Research Center, Atlanta, GA, USA.
Routh AL; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Ren P; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.
Ku Z; Texas Therapeutics Institute, Brown Foundation Institute of Molecular Medicine, University of Texas Health Science Center at Houston, Houston, USA.
An Z; Texas Therapeutics Institute, Brown Foundation Institute of Molecular Medicine, University of Texas Health Science Center at Houston, Houston, USA.
Debbink K; Department of Natural Sciences Bowie State University, Bowie, MD, USA.
Diamond MS; Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, USA.; Department of Medicine, Washington University School of Medicine, St Louis, MO, USA.; Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO, USA.
Shi PY; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.; Institute for Human Infection and Immunity, University of Texas Medical Branch, Galveston, TX, USA.
Freiberg AN; Department of Pathology, University of Texas Medical Branch, Galveston, TX, USA.; Institute for Human Infection and Immunity, University of Texas Medical Branch, Galveston, TX, USA.
Menachery VD; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA. .; Institute for Human Infection and Immunity, University of Texas Medical Branch, Galveston, TX, USA. .
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Źródło :
Nature [Nature] 2021 Mar; Vol. 591 (7849), pp. 293-299. Date of Electronic Publication: 2021 Jan 25.
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 :
Mutation*
COVID-19/*virology
Furin/*metabolism
SARS-CoV-2/*genetics
SARS-CoV-2/*pathogenicity
Spike Glycoprotein, Coronavirus/*chemistry
Spike Glycoprotein, Coronavirus/*genetics
Amino Acid Sequence ; Animals ; Antibodies, Neutralizing/immunology ; COVID-19/pathology ; COVID-19/physiopathology ; Cell Line ; Chlorocebus aethiops ; Cricetinae ; Female ; Humans ; Lung Diseases/pathology ; Lung Diseases/physiopathology ; Lung Diseases/virology ; Male ; Mice ; Mice, Transgenic ; Models, Molecular ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Proteolysis ; SARS-CoV-2/chemistry ; SARS-CoV-2/metabolism ; Serine Endopeptidases/metabolism ; Spike Glycoprotein, Coronavirus/metabolism ; Vero Cells ; Virus Replication/genetics
Czasopismo naukowe
Tytuł :
Structure-function analysis of naturally occurring apolipoprotein A-I L144R, A164S and L178P mutants provides insight on their role on HDL levels and cardiovascular risk.
Autorzy :
Gkolfinopoulou C; Institute of Biosciences and Applications, National Center for Scientific Research 'Demokritos', Agia Paraskevi, 15341, Athens, Greece.
Soukou F; Institute of Biosciences and Applications, National Center for Scientific Research 'Demokritos', Agia Paraskevi, 15341, Athens, Greece.
Dafnis I; Institute of Biosciences and Applications, National Center for Scientific Research 'Demokritos', Agia Paraskevi, 15341, Athens, Greece.
Kellici TF; Laboratory of Organic Chemistry, Department of Chemistry, National and Kapodistrian University of Athens, Panepistimioupolis Zografou, Athens, Greece.
Sanoudou D; 4th Department of Internal Medicine, Clinical Genomics and Pharmacogenomics Unit, 'Attikon' Hospital, Medical School, National and Kapodistrian University of Athens, Athens, Greece.; Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, Athens, Greece.; Center for New Biotechnologies and Precision Medicine, Medical School, National and Kapodistrian University of Athens, Athens, Greece.
Mavromoustakos T; Laboratory of Organic Chemistry, Department of Chemistry, National and Kapodistrian University of Athens, Panepistimioupolis Zografou, Athens, Greece.
Stratikos E; Protein Chemistry Laboratory, Institute of Nuclear and Radiological Sciences and Technology, Energy and Safety, National Center for Scientific Research 'Demokritos', Agia Paraskevi, Athens, Greece.
Chroni A; Institute of Biosciences and Applications, National Center for Scientific Research 'Demokritos', Agia Paraskevi, 15341, Athens, Greece. .
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Źródło :
Cellular and molecular life sciences : CMLS [Cell Mol Life Sci] 2021 Feb; Vol. 78 (4), pp. 1523-1544. Date of Electronic Publication: 2020 Jul 14.
Typ publikacji :
Journal Article
MeSH Terms :
ATP Binding Cassette Transporter, Subfamily G, Member 1/*genetics
Apolipoprotein A-I/*genetics
Cardiovascular Diseases/*genetics
Cholesterol, HDL/*genetics
ATP Binding Cassette Transporter, Subfamily G, Member 1/metabolism ; Apolipoprotein A-I/metabolism ; Apolipoprotein A-I/ultrastructure ; Cardiovascular Diseases/pathology ; Cell Movement/genetics ; Cholesterol, HDL/metabolism ; Cholesterol, HDL/ultrastructure ; Endothelial Cells/metabolism ; Endothelial Cells/pathology ; Heart Disease Risk Factors ; Humans ; Ketocholesterols/genetics ; Ketocholesterols/metabolism ; Lipoproteins, HDL/genetics ; Lipoproteins, HDL/metabolism ; Lipoproteins, HDL/ultrastructure ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Mutant Proteins/ultrastructure ; Mutation/genetics ; Scavenger Receptors, Class E/genetics ; Scavenger Receptors, Class E/metabolism ; Structure-Activity Relationship ; Thermodynamics
Czasopismo naukowe
Tytuł :
Genetic and structural studies of RABL3 reveal an essential role in lymphoid development and function.
Autorzy :
Zhong X; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Su L; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Yang Y; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Nair-Gill E; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Tang M; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Anderton P; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Li X; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Wang J; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Zhan X; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Tomchick DR; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Brautigam CA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390.; Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Moresco EMY; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505.
Choi JH; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505; .; Department of Immunology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Beutler B; Center for the Genetics of Host Defense, University of Texas Southwestern Medical Center, Dallas, TX 75390-8505; .
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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. 8563-8572. Date of Electronic Publication: 2020 Mar 27.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Lymphopoiesis*
B-Lymphocytes/*immunology
Mutant Proteins/*metabolism
Receptors, G-Protein-Coupled/*metabolism
T-Lymphocytes/*immunology
rab GTP-Binding Proteins/*chemistry
rab GTP-Binding Proteins/*physiology
Animals ; B-Lymphocytes/metabolism ; B-Lymphocytes/pathology ; Crystallography, X-Ray ; Female ; Herpesviridae Infections/immunology ; Herpesviridae Infections/virology ; Killer Cells, Natural/immunology ; Killer Cells, Natural/metabolism ; Killer Cells, Natural/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Muromegalovirus/immunology ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Mutation ; Protein Conformation ; T-Lymphocytes/metabolism ; T-Lymphocytes/pathology
Czasopismo naukowe
Tytuł :
Characterisation of ACP5 missense mutations encoding tartrate-resistant acid phosphatase associated with spondyloenchondrodysplasia.
Autorzy :
Ramesh J; Department of Medical Biochemistry, Dr. ALM-PGIBMS, University of Madras, Madras, India.
Parthasarathy LK; Department of Psychiatry, University of Louisville School of Medicine, Louisville, KY, United States of America.
Janckila AJ; Department of Microbiology and Immunology, University of Louisville, School of Medicine, Louisville, KY, United States of America.
Begum F; Department of Medical Biochemistry, Dr. ALM-PGIBMS, University of Madras, Madras, India.
Murugan R; Department of Medical Biochemistry, Dr. ALM-PGIBMS, University of Madras, Madras, India.
Murthy BPSS; Department of Vascular and Endovascular Sciences, Tamilnadu Government Multi Super Speciality Hospital, Chennai, India.
El-Mallakh RS; Department of Psychiatry, University of Louisville School of Medicine, Louisville, KY, United States of America.
Parthasarathy RN; Department of Medical Biochemistry, Dr. ALM-PGIBMS, University of Madras, Madras, India.; Department of Psychiatry, University of Louisville School of Medicine, Louisville, KY, United States of America.; Department of Psychiatry, Molecular Biology and Biochemistry, University of Louisville School of Medicine, Louisville, KY, United States of America.
Venugopal B; Department of Medical Biochemistry, Dr. ALM-PGIBMS, University of Madras, Madras, India.
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Źródło :
PloS one [PLoS One] 2020 Mar 26; Vol. 15 (3), pp. e0230052. Date of Electronic Publication: 2020 Mar 26 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Mutation, Missense*
Autoimmune Diseases/*pathology
Mutant Proteins/*metabolism
Osteochondrodysplasias/*pathology
Tartrate-Resistant Acid Phosphatase/*metabolism
Amino Acid Substitution ; Autoimmune Diseases/enzymology ; Autoimmune Diseases/genetics ; Glycosylation ; Humans ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Osteochondrodysplasias/enzymology ; Osteochondrodysplasias/genetics ; Proteolysis ; Tartrate-Resistant Acid Phosphatase/chemistry ; Tartrate-Resistant Acid Phosphatase/genetics
SCR Disease Name :
Spondyloenchondrodysplasia
Czasopismo naukowe

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