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Wyszukujesz frazę ""Protein Aggregates"" wg kryterium: Temat


Tytuł:
Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation.
Autorzy:
Chen G; Department of Biosciences and Nutrition, Karolinska Institutet, 141 83, Huddinge, Sweden. .
Leppert A; Department of Biosciences and Nutrition, Karolinska Institutet, 141 83, Huddinge, Sweden.; Department of Microbiology, Tumour and Cell Biology, Karolinska Institutet, 171 65, Solna, Sweden.
Poska H; Department of Biosciences and Nutrition, Karolinska Institutet, 141 83, Huddinge, Sweden.; School of Natural Sciences and Health, Tallinn University, Tallinn, Estonia.
Nilsson HE; School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, 141 52, Huddinge, Sweden.
Alvira CP; Department of Biosciences and Nutrition, Karolinska Institutet, 141 83, Huddinge, Sweden.
Zhong X; School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, 141 52, Huddinge, Sweden.
Koeck P; School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, 141 52, Huddinge, Sweden.
Jegerschöld C; School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, 141 52, Huddinge, Sweden.
Abelein A; Department of Biosciences and Nutrition, Karolinska Institutet, 141 83, Huddinge, Sweden.
Hebert H; School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, 141 52, Huddinge, Sweden.
Johansson J; Department of Biosciences and Nutrition, Karolinska Institutet, 141 83, Huddinge, Sweden. .
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Źródło:
Communications biology [Commun Biol] 2023 May 08; Vol. 6 (1), pp. 497. Date of Electronic Publication: 2023 May 08.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Amyloid*/metabolism
Protein Aggregates*
Protein Folding ; Molecular Chaperones/metabolism ; Amyloidogenic Proteins ; Hydrophobic and Hydrophilic Interactions
Czasopismo naukowe
Tytuł:
Lipids reverse supramolecular chirality and reduce toxicity of amyloid fibrils.
Autorzy:
Rizevsky S; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.; Department of Biotechnology, Binh Duong University, Thu Dau Mot, Vietnam.
Zhaliazka K; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
Matveyenka M; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
Quinn K; BioTools, Inc., Jupiter, FL, USA.
Kurouski D; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.; Department of Biomedical Engineering, Texas A&M University, College Station, TX, USA.
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Źródło:
The FEBS journal [FEBS J] 2022 Dec; Vol. 289 (23), pp. 7537-7544. Date of Electronic Publication: 2022 Jul 02.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms:
Amyloid*
Protein Aggregates*
Insulin
Czasopismo naukowe
Tytuł:
Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.
Autorzy:
Yagi-Utsumi M; Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.; Exploratory Research Center on Life and Living Systems and Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki 444-8787, Japan.
Kato K; Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.; Exploratory Research Center on Life and Living Systems and Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki 444-8787, Japan.
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Źródło:
Molecules (Basel, Switzerland) [Molecules] 2022 Jul 26; Vol. 27 (15). Date of Electronic Publication: 2022 Jul 26.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Amyloid*/chemistry
Protein Aggregates*
Amyloid beta-Peptides/metabolism ; Protein Conformation ; Protein Folding
Czasopismo naukowe
Tytuł:
Effect of 1-Ethyl-3-methylimidazolium Tetrafluoroborate and Acetate Ionic Liquids on Stability and Amyloid Aggregation of Lysozyme.
Autorzy:
Fedunova D; Institute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Antosova A; Institute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Marek J; Institute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Vanik V; Institute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Demjen E; Institute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Bednarikova Z; Institute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Gazova Z; Institute of Experimental Physics, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2022 Jan 11; Vol. 23 (2). Date of Electronic Publication: 2022 Jan 11.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Aggregates*
Acetates/*chemistry
Amyloid/*chemistry
Imidazoles/*chemistry
Ionic Liquids/*chemistry
Muramidase/*chemistry
Amyloidogenic Proteins/chemistry ; Hydrophobic and Hydrophilic Interactions ; Kinetics ; Models, Molecular ; Protein Conformation ; Protein Stability ; Solvents ; Temperature ; Thermodynamics
Czasopismo naukowe
Tytuł:
Searching for the Best Transthyretin Aggregation Protocol to Study Amyloid Fibril Disruption.
Autorzy:
Ferreira E; Chemistry Department and Coimbra Chemistry Centre-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.
Almeida ZL; Chemistry Department and Coimbra Chemistry Centre-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.
Cruz PF; Chemistry Department and Coimbra Chemistry Centre-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.
Silva E Sousa M; Chemistry Department and Coimbra Chemistry Centre-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.
Veríssimo P; Centre for Neuroscience and Cell Biology, University of Coimbra, 3004-517 Coimbra, Portugal.
Brito RMM; Chemistry Department and Coimbra Chemistry Centre-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Dec 30; Vol. 23 (1). Date of Electronic Publication: 2021 Dec 30.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Aggregates*
Amyloid/*metabolism
Prealbumin/*chemistry
Amyloid/ultrastructure ; Circular Dichroism ; Doxycycline/chemistry ; Doxycycline/pharmacology ; Hydrogen-Ion Concentration ; Nephelometry and Turbidimetry ; Prealbumin/ultrastructure ; Protein Structure, Secondary ; Proton Magnetic Resonance Spectroscopy
Czasopismo naukowe
Tytuł:
Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET.
Autorzy:
Katina N; Institute of Protein Research, Pushchino, 142290 Moscow, Russia.
Mikhaylina A; Institute of Protein Research, Pushchino, 142290 Moscow, Russia.
Ilina N; Institute of Protein Research, Pushchino, 142290 Moscow, Russia.
Eliseeva I; Institute of Protein Research, Pushchino, 142290 Moscow, Russia.
Balobanov V; Institute of Protein Research, Pushchino, 142290 Moscow, Russia.
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Źródło:
Molecules (Basel, Switzerland) [Molecules] 2021 Dec 15; Vol. 26 (24). Date of Electronic Publication: 2021 Dec 15.
Typ publikacji:
Journal Article
MeSH Terms:
Fluorescence Resonance Energy Transfer*
Protein Aggregates*
Amyloid/*chemistry
Amyloid beta-Peptides/*chemistry
Peptide Fragments/*chemistry
Amyloid/metabolism ; Amyloid beta-Peptides/metabolism ; Humans ; Peptide Fragments/metabolism
Czasopismo naukowe
Tytuł:
Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.
Autorzy:
Ziaunys M; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
Sakalauskas A; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
Mikalauskaite K; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
Smirnovas V; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Nov 17; Vol. 22 (22). Date of Electronic Publication: 2021 Nov 17.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Aggregates*
Protein Aggregation, Pathological*
Amyloid/*chemistry
alpha-Synuclein/*chemistry
Amyloid/metabolism ; In Vitro Techniques/methods ; Kinetics ; Osmolar Concentration ; Parkinson Disease/metabolism ; Protein Binding ; Protein Structure, Secondary ; alpha-Synuclein/metabolism
Czasopismo naukowe
Tytuł:
β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis.
Autorzy:
Sulatskaya AI; Laboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, 3 Podbelskogo Sh., Pushkin, 196608 St. Petersburg, Russia.; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russia.
Kosolapova AO; Laboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, 3 Podbelskogo Sh., Pushkin, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 7/9 Universitetskaya Emb., 199034 St. Petersburg, Russia.
Bobylev AG; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 3 Institutskaya St., 142290 Moscow, Russia.
Belousov MV; Laboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, 3 Podbelskogo Sh., Pushkin, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 7/9 Universitetskaya Emb., 199034 St. Petersburg, Russia.
Antonets KS; Laboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, 3 Podbelskogo Sh., Pushkin, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 7/9 Universitetskaya Emb., 199034 St. Petersburg, Russia.
Sulatsky MI; Laboratory of Cell Morphology, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russia.
Kuznetsova IM; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russia.
Turoverov KK; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russia.
Stepanenko OV; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russia.
Nizhnikov AA; Laboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, 3 Podbelskogo Sh., Pushkin, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 7/9 Universitetskaya Emb., 199034 St. Petersburg, Russia.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Oct 20; Vol. 22 (21). Date of Electronic Publication: 2021 Oct 20.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Amyloid/*physiology
Protein Aggregates/*physiology
Protein Conformation, beta-Strand/*physiology
Amyloid/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloidogenic Proteins/metabolism ; Amyloidosis/metabolism ; Humans ; Molecular Dynamics Simulation ; Protein Aggregates/genetics
Czasopismo naukowe
Tytuł:
Unzipping the Secrets of Amyloid Disassembly by the Human Disaggregase.
Autorzy:
Franco A; Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country UPV/EHU, 48080 Bilbao, Spain.; Instituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940 Leioa, Spain.
Velasco-Carneros L; Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country UPV/EHU, 48080 Bilbao, Spain.; Instituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940 Leioa, Spain.
Alvarez N; Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country UPV/EHU, 48080 Bilbao, Spain.; Instituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940 Leioa, Spain.
Orozco N; Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country UPV/EHU, 48080 Bilbao, Spain.; Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), Barrio Sarriena s/n, 48940 Leioa, Spain.
Moro F; Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country UPV/EHU, 48080 Bilbao, Spain.; Instituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940 Leioa, Spain.
Prado A; Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country UPV/EHU, 48080 Bilbao, Spain.; Instituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940 Leioa, Spain.
Muga A; Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country UPV/EHU, 48080 Bilbao, Spain.; Instituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, 48940 Leioa, Spain.
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Źródło:
Cells [Cells] 2021 Oct 14; Vol. 10 (10). Date of Electronic Publication: 2021 Oct 14.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't; Review
MeSH Terms:
Protein Aggregates*
Amyloid/*metabolism
Molecular Chaperones/*metabolism
Amyloid/toxicity ; Humans ; Models, Biological ; Nerve Degeneration/metabolism ; Nerve Degeneration/pathology ; alpha-Synuclein/metabolism
Czasopismo naukowe
Tytuł:
Members of the GADD45 Protein Family Show Distinct Propensities to form Toxic Amyloid-Like Aggregates in Physiological Conditions.
Autorzy:
Smaldone G; IRCCS SDN, Napoli, Via E. Gianturco 113, 80143 Napoli, Italy.
Caruso D; Institute of Biostructures and Bioimaging, C.N.R., Via Mezzocannone 16, 80134 Napoli, Italy.
Sandomenico A; Institute of Biostructures and Bioimaging, C.N.R., Via Mezzocannone 16, 80134 Napoli, Italy.
Iaccarino E; Institute of Biostructures and Bioimaging, C.N.R., Via Mezzocannone 16, 80134 Napoli, Italy.
Focà A; Institute of Biostructures and Bioimaging, C.N.R., Via Mezzocannone 16, 80134 Napoli, Italy.
Ruggiero A; Institute of Biostructures and Bioimaging, C.N.R., Via Mezzocannone 16, 80134 Napoli, Italy.
Ruvo M; Institute of Biostructures and Bioimaging, C.N.R., Via Mezzocannone 16, 80134 Napoli, Italy.
Vitagliano L; Institute of Biostructures and Bioimaging, C.N.R., Via Mezzocannone 16, 80134 Napoli, Italy.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Oct 02; Vol. 22 (19). Date of Electronic Publication: 2021 Oct 02.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Aggregates*
Amyloid/*metabolism
Intracellular Signaling Peptides and Proteins/*chemistry
Intracellular Signaling Peptides and Proteins/*metabolism
Amyloid/chemistry ; Cell Survival ; Cells, Cultured ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; MAP Kinase Kinase 7/metabolism ; Protein Aggregation, Pathological/metabolism ; Protein Binding ; Protein Conformation, beta-Strand ; Protein Stability ; Recombinant Proteins ; Thermodynamics ; GADD45 Proteins
Czasopismo naukowe
Tytuł:
Co-Aggregation of S100A9 with DOPA and Cyclen-Based Compounds Manifested in Amyloid Fibril Thickening without Altering Rates of Self-Assembly.
Autorzy:
Arabuli L; Department of Medical Biochemistry and Biophysics, Umeå University, SE-90781 Umeå, Sweden.; Department of Natural Sciences, School of Science and Technology, University of Georgia, 0171 Tbilisi, Georgia.
Iashchishyn IA; Department of Medical Biochemistry and Biophysics, Umeå University, SE-90781 Umeå, Sweden.
Romanova NV; Department of Medical Biochemistry and Biophysics, Umeå University, SE-90781 Umeå, Sweden.
Musteikyte G; Institute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, Lithuania.
Smirnovas V; Institute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, Lithuania.
Chaudhary H; Department of Medical Biochemistry and Biophysics, Umeå University, SE-90781 Umeå, Sweden.
Svedružić ŽM; Department of Biotechnology, University of Rijeka, HR-51000 Rijeka, Croatia.
Morozova-Roche LA; Department of Medical Biochemistry and Biophysics, Umeå University, SE-90781 Umeå, Sweden.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Aug 09; Vol. 22 (16). Date of Electronic Publication: 2021 Aug 09.
Typ publikacji:
Journal Article
MeSH Terms:
Molecular Dynamics Simulation*
Protein Aggregates*
Amyloid/*chemistry
Calgranulin B/*chemistry
Dihydroxyphenylalanine/*chemistry
Humans
Czasopismo naukowe
Tytuł:
Experimental and theoretical studies on the anti-amyloidogenic and destabilizing effects of pyrogallol against human insulin protein.
Autorzy:
Shouhani P; Department of Biology, MSc of Biology, Lorestan University, Khorramabad, Iran.
Bahramikia S; Department of Biology, Faculty of Basic Sciences, Lorestan University, Khorramabad, Iran.
Hejazi SH; Department of Biology, Faculty of Basic Sciences, Lorestan University, Khorramabad, Iran.
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Źródło:
Journal of food biochemistry [J Food Biochem] 2022 Oct; Vol. 46 (10), pp. e14293. Date of Electronic Publication: 2022 Jun 28.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Amyloid*/chemistry
Amyloid*/metabolism
Amyloid*/ultrastructure
Insulin*/chemistry
Amides ; Anti-Bacterial Agents ; Antifungal Agents ; Antioxidants/chemistry ; Antiviral Agents ; Humans ; Models, Theoretical ; Protein Aggregates ; Pyrogallol/pharmacology
Czasopismo naukowe
Tytuł:
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation.
Autorzy:
Toleikis Z; Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, Lithuania.; Latvian Institute of Organic Synthesis, Aizkraukles 21, LV-1006 Riga, Latvia.
Ziaunys M; Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, Lithuania.
Baranauskiene L; Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, Lithuania.
Petrauskas V; Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, Lithuania.
Jaudzems K; Latvian Institute of Organic Synthesis, Aizkraukles 21, LV-1006 Riga, Latvia.
Smirnovas V; Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, Lithuania.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Jul 26; Vol. 22 (15). Date of Electronic Publication: 2021 Jul 26.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Aggregates*
Amyloid/*chemistry
Calgranulin B/*chemistry
alpha-Synuclein/*chemistry
Humans ; Recombinant Proteins/chemistry
Czasopismo naukowe
Tytuł:
Understanding Amyloid Structures and Disease: A Continuing Challenge in Health Research.
Autorzy:
Chiellini G; Department of Pathology, University of Pisa, 56100 Pisa, Italy.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Jun 21; Vol. 22 (12). Date of Electronic Publication: 2021 Jun 21.
Typ publikacji:
Editorial; Introductory Journal Article
MeSH Terms:
Amyloid*
Amyloidosis*
Protein Aggregates*
Neurodegenerative Diseases/*etiology
Protein Aggregation, Pathological/*complications
Animals ; Humans
Czasopismo naukowe
Tytuł:
Understanding the Role of Protein Glycation in the Amyloid Aggregation Process.
Autorzy:
Sirangelo I; Department of Precision Medicine, Università degli Studi della Campania 'Luigi Vanvitelli', Via L. De Crecchio 7, 80138 Naples, Italy.
Iannuzzi C; Department of Precision Medicine, Università degli Studi della Campania 'Luigi Vanvitelli', Via L. De Crecchio 7, 80138 Naples, Italy.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Jun 21; Vol. 22 (12). Date of Electronic Publication: 2021 Jun 21.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Carbohydrate Metabolism*
Protein Aggregates*
Protein Aggregation, Pathological*
Amyloid/*metabolism
Animals ; Humans
Czasopismo naukowe
Tytuł:
Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells.
Autorzy:
Sang JC; Department of Chemistry, University of Cambridge, Cambridge, UK.; UK Dementia Research Institute at Cambridge, Cambridge, UK.
Hidari E; Department of Chemistry, University of Cambridge, Cambridge, UK.; UK Dementia Research Institute at Cambridge, Cambridge, UK.
Meisl G; Department of Chemistry, University of Cambridge, Cambridge, UK.
Ranasinghe RT; Department of Chemistry, University of Cambridge, Cambridge, UK.
Spillantini MG; Department of Clinical Neuroscience, University of Cambridge, Cambridge, UK.
Klenerman D; Department of Chemistry, University of Cambridge, Cambridge, UK. .; UK Dementia Research Institute at Cambridge, Cambridge, UK. .
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Źródło:
Communications biology [Commun Biol] 2021 May 21; Vol. 4 (1), pp. 613. Date of Electronic Publication: 2021 May 21.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Aggregates*
Amyloid/*chemistry
Molecular Imaging/*methods
Neuroblastoma/*pathology
alpha-Synuclein/*chemistry
alpha-Synuclein/*metabolism
Humans ; Neuroblastoma/metabolism ; Tumor Cells, Cultured
Czasopismo naukowe
Tytuł:
Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals.
Autorzy:
Pathak R; School of Chemistry, The University of Melbourne, Melbourne, VIC, 3010, Australia.; Department of Chemical Engineering, The University of Melbourne, Melbourne, VIC, 3010, Australia.; The ARC Dairy Innovation Hub, The University of Melbourne, Melbourne, VIC, 3010, Australia.
Bhangu SK; School of Science, RMIT University, Melbourne, VIC, 3000, Australia.
Martin GJO; Department of Chemical Engineering, The University of Melbourne, Melbourne, VIC, 3010, Australia.; The ARC Dairy Innovation Hub, The University of Melbourne, Melbourne, VIC, 3010, Australia.
Separovic F; School of Chemistry, The University of Melbourne, Melbourne, VIC, 3010, Australia. .; Bio21 Institute, The University of Melbourne, Melbourne, VIC, 3010, Australia. .
Ashokkumar M; School of Chemistry, The University of Melbourne, Melbourne, VIC, 3010, Australia. .; The ARC Dairy Innovation Hub, The University of Melbourne, Melbourne, VIC, 3010, Australia. .
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Źródło:
European biophysics journal : EBJ [Eur Biophys J] 2022 Jul; Vol. 51 (4-5), pp. 335-352. Date of Electronic Publication: 2022 May 16.
Typ publikacji:
Journal Article
MeSH Terms:
Amyloid*/chemistry
Lactoglobulins*/chemistry
Protein Aggregates ; Spectroscopy, Fourier Transform Infrared
Czasopismo naukowe
Tytuł:
Thioflavin-positive tau aggregates complicating quantification of amyloid plaques in the brain of 5XFAD transgenic mouse model.
Autorzy:
Shin J; Department of Pharmacy, Yonsei University, Incheon, 21983, Republic of Korea.
Park S; Department of Pharmacy, Yonsei University, Incheon, 21983, Republic of Korea.
Lee H; Department of Pharmacy, Yonsei University, Incheon, 21983, Republic of Korea.
Kim Y; Department of Pharmacy, Yonsei University, Incheon, 21983, Republic of Korea. .
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Źródło:
Scientific reports [Sci Rep] 2021 Jan 15; Vol. 11 (1), pp. 1617. Date of Electronic Publication: 2021 Jan 15.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Aggregates*/drug effects
Amyloid/*metabolism
Benzothiazoles/*chemistry
Brain/*pathology
tau Proteins/*metabolism
Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid/chemistry ; Amyloid beta-Peptides/metabolism ; Animals ; Brain/metabolism ; Disease Models, Animal ; Female ; Male ; Mice ; Mice, Transgenic ; Phosphorylation ; Piperazines/pharmacology ; Piperazines/therapeutic use ; Protein Conformation, beta-Strand
Czasopismo naukowe
Tytuł:
Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.
Autorzy:
Bobyleva LG; Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
Shumeyko SA; Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
Yakupova EI; Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
Surin AK; Laboratory of Bioinformatics and Proteomics, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.; Biological Testing Laboratory, Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.; Laboratory of the Biochemistry of Pathogenic Microorganisms, State Research Centre for Applied Microbiology and Biotechnology, Obolensk, 142279 Serpukhov District, Russia.
Galzitskaya OV; Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.; Laboratory of Bioinformatics and Proteomics, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Kihara H; Department of Early Childhood Education, Himeji-Hinomoto College, 890 Koro, Kodera-cho, Himeji 679-2151, Japan.
Timchenko AA; Group of Experimental Research and Engineering of Oligomeric Structures, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Timchenko MA; Laboratory of Applied Enzymology, FRC PSCBR, Russian Academy of Sciences, 142290 Pushchino, Russia.
Penkov NV; Laboratory of the Methods of Optical Spectral Analysis, Institute of Cell Biophysics, Russian Academy of Sciences, FRC PSCBR RAS, 142290 Pushchino, Russia.
Nikulin AD; Laboratory for Structural Studies of the Translational Apparatus, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Suvorina MY; Laboratory of Bioinformatics and Proteomics, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Molochkov NV; Laboratory of NMR Investigations of Biosystems, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
Lobanov MY; Laboratory of Bioinformatics and Proteomics, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Fadeev RS; Laboratory of Pharmacological Regulation of Cell Resistance, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
Vikhlyantsev IM; Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
Bobylev AG; Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Jan 13; Vol. 22 (2). Date of Electronic Publication: 2021 Jan 13.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Aggregates*
Amyloid/*chemistry
Amyloid/*metabolism
Carrier Proteins/*chemistry
Carrier Proteins/*metabolism
Amino Acid Sequence ; Amyloid/ultrastructure ; Chromatography, High Pressure Liquid ; Circular Dichroism ; Dynamic Light Scattering ; In Vitro Techniques ; Kinetics ; Mass Spectrometry ; Models, Molecular ; Protein Aggregation, Pathological ; Protein Conformation ; Structure-Activity Relationship ; X-Ray Diffraction
Czasopismo naukowe
Tytuł:
"What Doesn't Kill You Makes You Stronger": Future Applications of Amyloid Aggregates in Biomedicine.
Autorzy:
Abdelrahman S; Laboratory for Nanomedicine, Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal 23955-6900, Saudi Arabia.
Alghrably M; Division of Biological and Environmental Sciences and Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia.
Lachowicz JI; Department of Medical Sciences and Public Health, University of Cagliari, Policlinico Universitario, I-09042 Monserrato, Italy.
Emwas AH; Core Labs, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia.
Hauser CAE; Laboratory for Nanomedicine, Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, Thuwal 23955-6900, Saudi Arabia.
Jaremko M; Division of Biological and Environmental Sciences and Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia.
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Źródło:
Molecules (Basel, Switzerland) [Molecules] 2020 Nov 11; Vol. 25 (22). Date of Electronic Publication: 2020 Nov 11.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Protein Aggregates*
Alzheimer Disease/*metabolism
Amyloid/*metabolism
Alzheimer Disease/therapy ; Amino Acid Motifs ; Amyloidosis/metabolism ; Amyloidosis/therapy ; Animals ; Antiviral Agents/pharmacology ; Binding Sites ; Cell-Penetrating Peptides/therapeutic use ; Humans ; Ions ; Metals/chemistry ; Nanomedicine ; Protein Binding ; Virus Diseases/drug therapy
Czasopismo naukowe

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