Temat: "Protein Aggregates" - OpacWWW

Skocz do pozycji: 1.

Tytuł:: ABCG2 transporter reduces protein aggregation in cigarette smoke condensate-exposed A549 lung cancer cells.
Autorzy:: Ajenu EO; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.
Seideneck AM; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.
Pandellapalli E; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.
Shinsky EM; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.
Humphries CL; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.
Aparicio NL; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.
Sharma M; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.
Marden JH; Department of Biology, Penn State University, University Park, Pennsylvania, United states of America.
Krasilnikova MM; Department of Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania, United states of America.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2024 Mar 05; Vol. 19 (3), pp. e0297661. Date of Electronic Publication: 2024 Mar 05 (Print Publication: 2024).
Typ publikacji:: Journal Article
MeSH Terms:: ATP Binding Cassette Transporter, Subfamily G, Member 2*/metabolism
Cigarette Smoking*
Lung Neoplasms*
Protein Aggregates*
Humans ; A549 Cells

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Skocz do pozycji: 2.

Tytuł:: Biased placement of Mitochondria fission facilitates asymmetric inheritance of protein aggregates during yeast cell division.
Autorzy:: Sun G; Center for Cell Dynamics and Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.; Biomedical Engineering Graduate Program, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Hwang C; Johns Hopkins University, Baltimore, Maryland, United States of America.
Jung T; Johns Hopkins University, Baltimore, Maryland, United States of America.
Liu J; Center for Cell Dynamics and Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.; Biochemistry, Cellular and Molecular Biology Graduate Program, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Li R; Center for Cell Dynamics and Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.; Biochemistry, Cellular and Molecular Biology Graduate Program, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.; Mechanobiology Institute, National University of Singapore, Singapore, Singapore.; Department of Biological Sciences, National University of Singapore, Singapore, Singapore.; Pokaż więcej
Źródło:: PLoS computational biology [PLoS Comput Biol] 2023 Nov 27; Vol. 19 (11), pp. e1011588. Date of Electronic Publication: 2023 Nov 27 (Print Publication: 2023).
Typ publikacji:: Journal Article
MeSH Terms:: Saccharomyces cerevisiae*/genetics
Saccharomyces cerevisiae*/metabolism
Protein Aggregates*
Cell Division/genetics ; Mitochondria/genetics ; Mitochondria/metabolism ; Organelles/metabolism ; Mitochondrial Dynamics/genetics

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Skocz do pozycji: 3.

Tytuł:: A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans.
Autorzy:: Jung R; German Center for Neurodegenerative Diseases (DZNE), Tübingen, Germany.
Lechler MC; German Center for Neurodegenerative Diseases (DZNE), Tübingen, Germany.; Graduate Training Centre of Neuroscience, International Max Planck Research School, Tübingen, Germany.
Fernandez-Villegas A; Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, United Kingdom.
Chung CW; Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, United Kingdom.
Jones HC; The Babraham Institute, Signalling Program, Cambridge, United Kingdom.
Choi YH; The Babraham Institute, Signalling Program, Cambridge, United Kingdom.
Thompson MA; The Babraham Institute, Signalling Program, Cambridge, United Kingdom.
Rödelsperger C; Max Planck Institute for Developmental Biology, Department for Integrative Evolutionary Biology, Tübingen, Germany.
Röseler W; Max Planck Institute for Developmental Biology, Department for Integrative Evolutionary Biology, Tübingen, Germany.
Kaminski Schierle GS; Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, United Kingdom.
Sommer RJ; Max Planck Institute for Developmental Biology, Department for Integrative Evolutionary Biology, Tübingen, Germany.
David DC; German Center for Neurodegenerative Diseases (DZNE), Tübingen, Germany.; The Babraham Institute, Signalling Program, Cambridge, United Kingdom.; Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.; Pokaż więcej
Źródło:: PLoS biology [PLoS Biol] 2023 Sep 14; Vol. 21 (9), pp. e3002284. Date of Electronic Publication: 2023 Sep 14 (Print Publication: 2023).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Caenorhabditis elegans*
Protein Aggregates*
Animals ; Aging ; Proteasome Endopeptidase Complex ; Proteostasis

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Skocz do pozycji: 4.

Tytuł:: Tau protein aggregation associated with SARS-CoV-2 main protease.
Autorzy:: Eberle RJ; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.; Institute of Physical Biology, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Coronado MA; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Gering I; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Sommerhage S; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Korostov K; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Stefanski A; Molecular Proteomics Laboratory (MPL), BMFZ, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Stühler K; Molecular Proteomics Laboratory (MPL), BMFZ, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Kraemer-Schulien V; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Blömeke L; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.; Institute of Physical Biology, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Bannach O; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.; Institute of Physical Biology, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.; attyloid GmbH, Düsseldorf, Germany.
Willbold D; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.; Institute of Physical Biology, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.; JuStruct: Jülich Centre for Structural Biology, Forschungszentrum Jülich, Jülich, Germany.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2023 Aug 21; Vol. 18 (8), pp. e0288138. Date of Electronic Publication: 2023 Aug 21 (Print Publication: 2023).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Coronavirus 3C Proteases*/metabolism
COVID-19*
Protein Aggregates*
tau Proteins*/metabolism
Humans ; Endopeptidases ; Peptide Hydrolases ; SARS-CoV-2

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Skocz do pozycji: 5.

Tytuł:: Self-assembly coupled to liquid-liquid phase separation.
Autorzy:: Hagan MF; Martin A. Fisher School of Physics, Brandeis University, Waltham, Massachusetts, United States of America.
Mohajerani F; Martin A. Fisher School of Physics, Brandeis University, Waltham, Massachusetts, United States of America.; Pokaż więcej
Źródło:: PLoS computational biology [PLoS Comput Biol] 2023 May 15; Vol. 19 (5), pp. e1010652. Date of Electronic Publication: 2023 May 15 (Print Publication: 2023).
Typ publikacji:: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, N.I.H., Extramural
MeSH Terms:: Protein Aggregates*

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Skocz do pozycji: 6.

Tytuł:: Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.
Autorzy:: Carter Z; Faculty of Biology, Medicine and Health, School of Biological Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester, United Kingdom.
Creamer D; Faculty of Biology, Medicine and Health, School of Biological Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester, United Kingdom.
Kouvidi A; Faculty of Biology, Medicine and Health, School of Biological Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester, United Kingdom.
Grant CM; Faculty of Biology, Medicine and Health, School of Biological Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester, United Kingdom.; Pokaż więcej
Źródło:: PLoS genetics [PLoS Genet] 2024 Feb 29; Vol. 20 (2), pp. e1011194. Date of Electronic Publication: 2024 Feb 29 (Print Publication: 2024).
Typ publikacji:: Journal Article
MeSH Terms:: Prions*/genetics
Prions*/metabolism
Saccharomyces cerevisiae Proteins*/genetics
Saccharomyces cerevisiae Proteins*/metabolism
Protein Aggregates/genetics ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Oxidative Stress/genetics ; Amyloid/metabolism ; Oxidants/pharmacology ; Oxidants/metabolism ; Peptide Termination Factors/genetics ; Peptide Termination Factors/metabolism

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Skocz do pozycji: 7.

Tytuł:: Identification of interaction partners using protein aggregation and NMR spectroscopy.
Autorzy:: Chae YK; Department of Chemistry, Sejong University, Seoul, Korea.
Shin HB; Department of Chemistry, Sejong University, Seoul, Korea.
Woo TR; Department of Chemistry, Sejong University, Seoul, Korea.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2022 Sep 09; Vol. 17 (9), pp. e0270058. Date of Electronic Publication: 2022 Sep 09 (Print Publication: 2022).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*
Proteins*/chemistry
Magnetic Resonance Spectroscopy/methods

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Skocz do pozycji: 8.

Tytuł:: Unraveling the roles of aromatic cluster side-chain interactions on the structural stability and functional significance of psychrophilic Sphingomonas sp. glutaredoxin 3.
Autorzy:: Tran TV; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea.
Hoang T; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea.
Jang SH; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea.
Lee C; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2023 Aug 31; Vol. 18 (8), pp. e0290686. Date of Electronic Publication: 2023 Aug 31 (Print Publication: 2023).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Glutaredoxins*
Sphingomonas*/genetics
Humans ; Protein Aggregates ; Biological Evolution ; Fever

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Skocz do pozycji: 9.

Tytuł:: A mathematical model for the dependence of keratin aggregate formation on the quantity of mutant keratin expressed in EGFP-K14 R125P keratinocytes.
Autorzy:: Gouveia M; Department of Physics, CFisUC, Center of Physics of the University of Coimbra, University of Coimbra, Coimbra, Portugal.
Sorčan T; AdriaBio Llc, Postojna, Slovenia.
Zemljič-Jokhadar Š; Faculty of Medicine, Institute for Biophysics, University of Ljubljana, Ljubljana, Slovenia.
Travasso RDM; Department of Physics, CFisUC, Center of Physics of the University of Coimbra, University of Coimbra, Coimbra, Portugal.
Liović M; Faculty of Medicine, Medical Center for Molecular Biology, Institute for Biochemistry and Molecular Genetics, University of Ljubljana, Ljubljana, Slovenia.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2021 Dec 28; Vol. 16 (12), pp. e0261227. Date of Electronic Publication: 2021 Dec 28 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*/drug effects
Keratinocytes/*metabolism
Keratins/*chemistry
Mutant Proteins/*chemistry
Cell Line ; Computer Simulation ; Fluorescent Dyes/chemistry ; Green Fluorescent Proteins/metabolism ; Humans ; Keratinocytes/drug effects ; Models, Biological ; Proteasome Inhibitors/pharmacology

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Skocz do pozycji: 10.

Tytuł:: A phenolic-rich extract from Ugni molinae berries reduces abnormal protein aggregation in a cellular model of Huntington's disease.
Autorzy:: Pérez-Arancibia R; Laboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.; Instituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Centro de Biología Integrativa, Facultad de Ciencias, Universidad Mayor, Santiago, Chile.
Ordoñez JL; Laboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.; Laboratorio de Química Inorgánica y Analítica, Departamento de Química Inorgánica y Analítica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.
Rivas A; Instituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Programa de Biología Celular y Molecular, Instituto de Ciencias Biomédicas, Universidad de Chile, Santiago, Chile.
Pihán P; Instituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Programa de Biología Celular y Molecular, Instituto de Ciencias Biomédicas, Universidad de Chile, Santiago, Chile.
Sagredo A; Instituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Programa de Biología Celular y Molecular, Instituto de Ciencias Biomédicas, Universidad de Chile, Santiago, Chile.
Ahumada U; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Centro de Biología Integrativa, Facultad de Ciencias, Universidad Mayor, Santiago, Chile.
Barriga A; Unidad de Espectrometría de Masas, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.
Seguel I; Laboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.
Cárdenas C; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Centro de Biología Integrativa, Facultad de Ciencias, Universidad Mayor, Santiago, Chile.; Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, United States of America.; Buck Institute for Research on Aging, Novato, California, United States of America.
Vidal RL; Instituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Centro de Biología Integrativa, Facultad de Ciencias, Universidad Mayor, Santiago, Chile.
Hetz C; Instituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.; Centro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.; Programa de Biología Celular y Molecular, Instituto de Ciencias Biomédicas, Universidad de Chile, Santiago, Chile.; Buck Institute for Research on Aging, Novato, California, United States of America.
Delporte C; Laboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2021 Jul 29; Vol. 16 (7), pp. e0254834. Date of Electronic Publication: 2021 Jul 29 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms:: Fruit*
Huntington Disease*
Protein Aggregates*
Antioxidants/pharmacology ; HEK293 Cells ; Humans ; Myrtaceae/chemistry ; Plant Extracts/pharmacology ; Plant Leaves

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Skocz do pozycji: 11.

Tytuł:: Phe-Gly motifs drive fibrillization of TDP-43's prion-like domain condensates.
Autorzy:: Pantoja-Uceda D; Rocasolano Institute of Physical Chemistry, Spanish National Research Council, Madrid, Spain.
Stuani C; International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Laurents DV; Rocasolano Institute of Physical Chemistry, Spanish National Research Council, Madrid, Spain.
McDermott AE; Department of Chemistry, Columbia University, New York, New York, United States of America.
Buratti E; International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Mompeán M; Rocasolano Institute of Physical Chemistry, Spanish National Research Council, Madrid, Spain.; Department of Chemistry, Columbia University, New York, New York, United States of America.; Pokaż więcej
Źródło:: PLoS biology [PLoS Biol] 2021 Apr 28; Vol. 19 (4), pp. e3001198. Date of Electronic Publication: 2021 Apr 28 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*
DNA-Binding Proteins/*chemistry
DNA-Binding Proteins/*metabolism
Dipeptides/*chemistry
Amino Acid Sequence ; Amyloid/chemistry ; Amyloid/metabolism ; Chemical Precipitation ; Dipeptides/physiology ; Humans ; Hydrogen-Ion Concentration ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Protein Interaction Domains and Motifs/physiology ; Solvents/chemistry ; Solvents/pharmacology

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Skocz do pozycji: 12.

Tytuł:: Reduction of WDR81 impairs autophagic clearance of aggregated proteins and cell viability in neurodegenerative phenotypes.
Autorzy:: Liu X; Department of Pharmacology, School of Basic Medical Science, Fudan University, Shanghai, China.; Division of Experimental Hematology and Cancer Biology, Department of Pediatrics, Brain Tumor Center, Cincinnati Children's Hospital Medical Center, Cincinnati, United States of America.
Yin L; Department of Pharmacology, School of Basic Medical Science, Fudan University, Shanghai, China.; Shanghai Key Laboratory of Bioactive Small Molecules, Fudan University, Shanghai, China.
Li T; Department of Pharmacology, School of Basic Medical Science, Fudan University, Shanghai, China.; Shanghai Key Laboratory of Bioactive Small Molecules, Fudan University, Shanghai, China.
Lin L; Department of Pharmacology, School of Basic Medical Science, Fudan University, Shanghai, China.
Zhang J; Department of Pharmacology, School of Basic Medical Science, Fudan University, Shanghai, China.; Shanghai Key Laboratory of Bioactive Small Molecules, Fudan University, Shanghai, China.
Li Y; Department of Pharmacology, School of Basic Medical Science, Fudan University, Shanghai, China.; Shanghai Key Laboratory of Bioactive Small Molecules, Fudan University, Shanghai, China.; Pokaż więcej
Źródło:: PLoS genetics [PLoS Genet] 2021 Mar 17; Vol. 17 (3), pp. e1009415. Date of Electronic Publication: 2021 Mar 17 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't; Retracted Publication
MeSH Terms:: Phenotype*
Protein Aggregates*
Autophagy/*genetics
Nerve Tissue Proteins/*genetics
Nerve Tissue Proteins/*metabolism
Protein Aggregation, Pathological/*genetics
Protein Aggregation, Pathological/*metabolism
Autophagy-Related Protein 12/metabolism ; Autophagy-Related Protein 5/metabolism ; Carrier Proteins ; Cell Survival/genetics ; Disease Susceptibility ; Fluorescent Antibody Technique ; Gene Expression ; Humans ; Models, Biological ; Mutation ; Neurodegenerative Diseases/etiology ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neurons/metabolism ; Protein Binding

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Skocz do pozycji: 13.

Tytuł:: An apta-aggregation based machine learning assay for rapid quantification of lysozyme through texture parameters.
Autorzy:: Sanjay M; Biosensors and Bioanalysis Laboratory (LABB), Department of Biological Chemistry and IQUIBICEN-CONICET, Exact and Natural Sciences Faculty (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
Gaurav K; Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati, Assam, India.
Gonzalez-Pabon MJ; Biosensors and Bioanalysis Laboratory (LABB), Department of Biological Chemistry and IQUIBICEN-CONICET, Exact and Natural Sciences Faculty (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
Fuchs J; Biosensors and Bioanalysis Laboratory (LABB), Department of Biological Chemistry and IQUIBICEN-CONICET, Exact and Natural Sciences Faculty (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
Mikkelsen SR; Department of Chemistry, University of Waterloo, Waterloo, Ontario, Canada.
Cortón E; Biosensors and Bioanalysis Laboratory (LABB), Department of Biological Chemistry and IQUIBICEN-CONICET, Exact and Natural Sciences Faculty (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2021 Mar 08; Vol. 16 (3), pp. e0248159. Date of Electronic Publication: 2021 Mar 08 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Machine Learning*
Protein Aggregates*
Aptamers, Nucleotide/*chemistry
Avian Proteins/*analysis
Muramidase/*analysis
Animals ; Chickens

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Skocz do pozycji: 14.

Tytuł:: DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization.
Autorzy:: Popova B; Department of Molecular Microbiology and Genetics, Institute for Microbiology and Genetics, University of Goettingen, Göttingen, Germany.
Wang D; Department of Molecular Microbiology and Genetics, Institute for Microbiology and Genetics, University of Goettingen, Göttingen, Germany.
Pätz C; Department of Molecular Microbiology and Genetics, Institute for Microbiology and Genetics, University of Goettingen, Göttingen, Germany.
Akkermann D; Department of Molecular Microbiology and Genetics, Institute for Microbiology and Genetics, University of Goettingen, Göttingen, Germany.
Lázaro DF; Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, University Medical Center Goettingen, Göttingen, Germany.
Galka D; Department of Molecular Microbiology and Genetics, Institute for Microbiology and Genetics, University of Goettingen, Göttingen, Germany.
Kolog Gulko M; Department of Molecular Microbiology and Genetics, Institute for Microbiology and Genetics, University of Goettingen, Göttingen, Germany.
Bohnsack MT; Department of Molecular Biology, University Medical Center Goettingen, Göttingen, Germany.
Möbius W; Department of Neurogenetics, Electron Microscopy Core Unit, Max-Planck-Institute of Experimental Medicine, Göttingen, Germany.
Bohnsack KE; Department of Molecular Biology, University Medical Center Goettingen, Göttingen, Germany.
Outeiro TF; Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, University Medical Center Goettingen, Göttingen, Germany.; Translational and Clinical Research Institute, Newcastle University, Newcastle upon Tyne, United Kingdom.
Braus GH; Department of Molecular Microbiology and Genetics, Institute for Microbiology and Genetics, University of Goettingen, Göttingen, Germany.; Pokaż więcej
Źródło:: PLoS genetics [PLoS Genet] 2021 Mar 03; Vol. 17 (3), pp. e1009407. Date of Electronic Publication: 2021 Mar 03 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*
Protein Multimerization*
DEAD-box RNA Helicases/*metabolism
Protein Aggregation, Pathological/*metabolism
alpha-Synuclein/*metabolism
Amyloid/metabolism ; Amyloid/ultrastructure ; Gene Expression Regulation ; Humans ; Inclusion Bodies/metabolism ; Inclusion Bodies/pathology ; Models, Biological ; Neurodegenerative Diseases/etiology ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Protein Binding ; Protein Transport ; Yeasts/genetics ; Yeasts/metabolism ; alpha-Synuclein/chemistry ; alpha-Synuclein/genetics

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Skocz do pozycji: 15.

Tytuł:: Aggregated LDL turn human macrophages into foam cells and induce mitochondrial dysfunction without triggering oxidative or endoplasmic reticulum stress.
Autorzy:: Sanda GM; Lipidomics Department, Institute of Cellular Biology and Pathology 'Nicolae Simionescu' of the Romanian Academy, Bucharest, Romania.
Stancu CS; Lipidomics Department, Institute of Cellular Biology and Pathology 'Nicolae Simionescu' of the Romanian Academy, Bucharest, Romania.
Deleanu M; Lipidomics Department, Institute of Cellular Biology and Pathology 'Nicolae Simionescu' of the Romanian Academy, Bucharest, Romania.; Faculty of Biotechnology, University of Agronomical Sciences and Veterinary Medicine, Bucharest, Romania.
Toma L; Lipidomics Department, Institute of Cellular Biology and Pathology 'Nicolae Simionescu' of the Romanian Academy, Bucharest, Romania.
Niculescu LS; Lipidomics Department, Institute of Cellular Biology and Pathology 'Nicolae Simionescu' of the Romanian Academy, Bucharest, Romania.
Sima AV; Lipidomics Department, Institute of Cellular Biology and Pathology 'Nicolae Simionescu' of the Romanian Academy, Bucharest, Romania.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2021 Jan 25; Vol. 16 (1), pp. e0245797. Date of Electronic Publication: 2021 Jan 25 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*
Endoplasmic Reticulum Stress/*drug effects
Foam Cells/*drug effects
Lipoproteins, LDL/*chemistry
Lipoproteins, LDL/*pharmacology
Mitochondria/*drug effects
Oxidative Stress/*drug effects
Apoptosis/drug effects ; Cell Line, Tumor ; Cholesterol/metabolism ; Foam Cells/cytology ; Foam Cells/metabolism ; Humans ; Intracellular Space/drug effects ; Intracellular Space/metabolism ; Mitochondria/metabolism

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Skocz do pozycji: 16.

Tytuł:: In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers.
Autorzy:: Zurlo E; Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands.
Kumar P; Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands.
Meisl G; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, United Kingdom.
Dear AJ; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, United Kingdom.
Mondal D; Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands.
Claessens MMAE; Nanobiophysics Group, Department of Science and Technology, University Twente, Enschede, The Netherlands.
Knowles TPJ; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, United Kingdom.; Cavendish Laboratory, University of Cambridge, Cambridge, United Kingdom.
Huber M; Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2021 Jan 22; Vol. 16 (1), pp. e0245548. Date of Electronic Publication: 2021 Jan 22 (Print Publication: 2021).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*
Protein Multimerization*
alpha-Synuclein/*chemistry
Kinetics ; Protein Structure, Quaternary

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Skocz do pozycji: 17.

Tytuł:: Elimination of protein aggregates prevents premature senescence in human trisomy 21 fibroblasts.
Autorzy:: Nawa N; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Hirata K; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.; Department of Neonatal Medicine, Osaka Women's and Children's Hospital, Izumi, Osaka, Japan.
Kawatani K; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Nambara T; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Omori S; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Banno K; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.; Department of Pediatrics, Indiana University School of Medicine, Indianapolis, Indiana, United States of America.
Kokubu C; Department of Genome Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Takeda J; Department of Genome Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Nishimura K; Laboratory of Gene Regulation, Faculty of Medicine, University of Tsukuba, Tsukuba, Ibaraki, Japan.
Ohtaka M; Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan.
Nakanishi M; Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan.
Okuzaki D; Genome Information Research Center, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
Taniguchi H; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Arahori H; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Wada K; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.; Department of Neonatal Medicine, Osaka Women's and Children's Hospital, Izumi, Osaka, Japan.
Kitabatake Y; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Ozono K; Department of Pediatrics, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2019 Jul 29; Vol. 14 (7), pp. e0219592. Date of Electronic Publication: 2019 Jul 29 (Print Publication: 2019).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Cellular Senescence*/drug effects
Protein Aggregates*/drug effects
Fibroblasts/*pathology
Trisomy/*pathology
Aneuploidy ; Cell Proliferation/drug effects ; Energy Metabolism/drug effects ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Glucose/metabolism ; Humans ; Induced Pluripotent Stem Cells/drug effects ; Induced Pluripotent Stem Cells/metabolism ; Lactates/metabolism ; Mitochondria/drug effects ; Mitochondria/pathology ; Oxidative Stress/drug effects ; Phenylbutyrates/pharmacology ; RNA/metabolism ; Trisomy/genetics

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Skocz do pozycji: 18.

Tytuł:: The interaction of several herbal extracts with α-synuclein: Fibril formation and surface plasmon resonance analysis.
Autorzy:: Honarmand S; Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University,Tehran, Iran.
Dabirmanesh B; Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University,Tehran, Iran.
Amanlou M; Department of Medicinal Chemistry, Faculty of Pharmacy and Drug Design and Development Research Center, Tehran University of Medical Sciences, Tehran, Iran.
Khajeh K; Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University,Tehran, Iran.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2019 Jun 11; Vol. 14 (6), pp. e0217801. Date of Electronic Publication: 2019 Jun 11 (Print Publication: 2019).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*
Amyloid/*chemistry
Flavonoids/*chemistry
Plant Extracts/*chemistry
Plants, Medicinal/*chemistry
alpha-Synuclein/*chemistry
Amyloid/metabolism ; Cell Line, Tumor ; Humans ; Surface Plasmon Resonance ; alpha-Synuclein/metabolism

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Skocz do pozycji: 19.

Tytuł:: A discrete mathematical model for the aggregation of β-Amyloid.
Autorzy:: Dayeh MA; Department of Space Research, Southwest Research Institute, San Antonio, Texas, United States of America.
Livadiotis G; Department of Space Research, Southwest Research Institute, San Antonio, Texas, United States of America.
Elaydi S; Department of Mathematics, Trinity University, San Antonio, Texas, United States of America.; Pokaż więcej
Źródło:: PloS one [PLoS One] 2018 May 23; Vol. 13 (5), pp. e0196402. Date of Electronic Publication: 2018 May 23 (Print Publication: 2018).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Protein Aggregates*
Amyloid beta-Peptides/*chemistry
Amyloid beta-Peptides/*metabolism
Protein Aggregation, Pathological/*metabolism
Alzheimer Disease/etiology ; Alzheimer Disease/metabolism ; Humans ; Kinetics ; Mathematical Concepts ; Models, Chemical ; Models, Molecular ; Protein Multimerization ; Protein Stability

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Skocz do pozycji: 20.

Tytuł:: A light-inducible protein clustering system for in vivo analysis of α-synuclein aggregation in Parkinson disease.
Autorzy:: Bérard M; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Sheta R; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Malvaut S; CERVO Brain Research Centre, Quebec City, Canada.; Department of Psychiatry and Neurosciences, Faculty of Medicine, Université Laval, Quebec City, Canada.
Rodriguez-Aller R; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.; CERVO Brain Research Centre, Quebec City, Canada.
Teixeira M; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Idi W; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Turmel R; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Alpaugh M; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Psychiatry and Neurosciences, Faculty of Medicine, Université Laval, Quebec City, Canada.
Dubois M; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Dahmene M; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Salesse C; CERVO Brain Research Centre, Quebec City, Canada.; Department of Psychiatry and Neurosciences, Faculty of Medicine, Université Laval, Quebec City, Canada.
Lamontagne-Proulx J; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Faculty of Pharmacy, Université Laval, Quebec City, Canada.
St-Pierre MK; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Tavassoly O; McGill Parkinson Program and Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Canada.
Luo W; McGill Parkinson Program and Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Canada.; The Neuro's Early Drug Discovery Unit (EDDU), Montreal Neurological Institute, McGill University, Montreal, Canada.
Del Cid-Pellitero E; McGill Parkinson Program and Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Canada.; The Neuro's Early Drug Discovery Unit (EDDU), Montreal Neurological Institute, McGill University, Montreal, Canada.
Qazi R; Department of Electrical, Computer, and Energy Engineering, University of Colorado, Boulder, Colorado, United States of America.
Jeong JW; Department of Electrical, Computer, and Energy Engineering, University of Colorado, Boulder, Colorado, United States of America.; School of Electrical Engineering Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.
Durcan TM; McGill Parkinson Program and Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Canada.; The Neuro's Early Drug Discovery Unit (EDDU), Montreal Neurological Institute, McGill University, Montreal, Canada.
Vallières L; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.
Tremblay ME; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.; Division of Medical Sciences, University of Victoria, Victoria, Canada.
Soulet D; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Faculty of Pharmacy, Université Laval, Quebec City, Canada.
Lévesque M; CERVO Brain Research Centre, Quebec City, Canada.; Department of Psychiatry and Neurosciences, Faculty of Medicine, Université Laval, Quebec City, Canada.
Cicchetti F; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Psychiatry and Neurosciences, Faculty of Medicine, Université Laval, Quebec City, Canada.
Fon EA; McGill Parkinson Program and Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Canada.; The Neuro's Early Drug Discovery Unit (EDDU), Montreal Neurological Institute, McGill University, Montreal, Canada.
Saghatelyan A; CERVO Brain Research Centre, Quebec City, Canada.; Department of Psychiatry and Neurosciences, Faculty of Medicine, Université Laval, Quebec City, Canada.
Oueslati A; CHU de Québec Research Center, Axe Neurosciences, Quebec City, Canada.; Department of Molecular Medicine, Faculty of Medicine, Université Laval, Quebec City, Canada.; Pokaż więcej
Źródło:: PLoS biology [PLoS Biol] 2022 Mar 09; Vol. 20 (3), pp. e3001578. Date of Electronic Publication: 2022 Mar 09 (Print Publication: 2022).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Parkinson Disease*/metabolism
alpha-Synuclein*/metabolism
Cluster Analysis ; Humans ; Lewy Bodies/metabolism ; Lewy Bodies/pathology ; Protein Aggregates

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