نتائج البحث - "Tiago F. Outeiro"

1

Synthesis and evaluation of esterified Hsp70 agonists in cellular models of protein aggregation and folding

المؤلفون: Carly S. Mazzone, Antonio Dominguez-Meijide, Jeffrey L. Brodsky, Mary Liang, Tiago F. Outeiro, Annette N. Chiang, David Newhouse, Peter Wipf, Nathan M. Kendsersky, Megan E. Yates, Patrick G. Needham, Caterina Masaracchia, Alexandra Manos-Turvey, Jennifer L. Goeckeler-Fried

المصدر: Bioorganic & Medicinal Chemistry. 27:79-91

مصطلحات موضوعية: Protein Folding, Clinical Biochemistry, Mutant, Cystic Fibrosis Transmembrane Conductance Regulator, Enzyme Activators, Pharmaceutical Science, Pyrimidinones, Saccharomyces cerevisiae, Protein aggregation, 01 natural sciences, Biochemistry, Article, Structure-Activity Relationship, Cell Line, Tumor, Cellular stress response, Drug Discovery, Humans, HSP70 Heat-Shock Proteins, Molecular Biology, Adenosine Triphosphatases, Molecular Structure, biology, 010405 organic chemistry, Activator (genetics), Chemistry, Organic Chemistry, HEK 293 cells, Esters, Cystic fibrosis transmembrane conductance regulator, 3. Good health, 0104 chemical sciences, Hsp70, Cell biology, 010404 medicinal & biomolecular chemistry, HEK293 Cells, Proteostasis, alpha-Synuclein, biology.protein, Molecular Medicine, Protein Multimerization

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6e5c63d4a71c5b638613d360a3ee103Test
https://doi.org/10.1016/j.bmc.2018.11.011Test

2

Monitoring α‐synuclein multimerization in vivo

المؤلفون: Joerg B. Schulz, Philipp J. Kahle, Istvan Katona, Yasmine Wasser, Anand Goswami, Tiago F. Outeiro, Vibha Prasad, Aaron Voigt, Friederike Hans

المصدر: The FASEB journal 33(2), 2116-2131 (2018). doi:10.1096/fj.201800148RRR

مصطلحات موضوعية: Male, 0301 basic medicine, Amyloid, Parkinson's disease, animal diseases, Protein aggregation, environment and public health, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, Bimolecular fluorescence complementation, 0302 clinical medicine, In vivo, ddc:570, metabolism [Drosophila melanogaster], Serine, Genetics, medicine, chemistry [Amyloid], Animals, metabolism [Reactive Oxygen Species], metabolism [alpha-Synuclein], Phosphorylation, Molecular Biology, biology, Chemistry, Rotenone, biology.organism_classification, medicine.disease, nervous system diseases, Cell biology, Disease Models, Animal, Drosophila melanogaster, 030104 developmental biology, Proteostasis, chemistry [alpha-Synuclein], nervous system, genetics [alpha-Synuclein], alpha-Synuclein, health occupations, growth & development [Drosophila melanogaster], Protein Multimerization, Reactive Oxygen Species, 030217 neurology & neurosurgery, Biotechnology

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54a7b50613981fe877563d0c69c3a021Test
https://doi.org/10.1096/fj.201800148rrrTest

3

In silico analysis of the aggregation propensity of the SARS-CoV-2 proteome: Insight into possible cellular pathologies

المؤلفون: Anita Krisko, Tiago F. Outeiro, Manuel Flores-León, Diana F. Lázaro, Liana Shvachiy

المصدر: Biochimica et biophysica acta / Proteins and proteomics 1869(10), 140693 (2021). doi:10.1016/j.bbapap.2021.140693
Biochimica et Biophysica Acta. Proteins and Proteomics

مصطلحات موضوعية: Proteome, metabolism [Viral Proteins], Bioinformatics, In silico, viruses, Biophysics, Plasma protein binding, Disease, Protein aggregation, Biology, medicine.disease_cause, APR, aggregation-prone regions, Virus Replication, Biochemistry, pathogenicity [SARS-CoV-2], Analytical Chemistry, CoVex, Coronavirus Explorer, metabolism [SARS-CoV-2], 03 medical and health sciences, Open Reading Frames, Viral Proteins, 0302 clinical medicine, ORF, open reading frame, PDB, Protein Data Bank, ddc:570, medicine, Molecular Biology, 030304 developmental biology, Coronavirus, Genetics, 0303 health sciences, SARS-CoV-2, Severe acute respiratory syndrome coronavirus 2, PASTA, prediction of amyloid structural aggregation, SARS-CoV-2, genetics [SARS-CoV-2], Entry into host, 3. Good health, Proteostasis, Mutation, NSP, non-structural proteins, A3D, Aggrescan3D, 030217 neurology & neurosurgery, COVID-19, coronavirus disease 19, Research Paper, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c5e3302f41d3ee8b3a2526f7302e165Test
https://pub.dzne.de/record/155650Test

4

صورة

Image_7_Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation.TIF

المؤلفون: Blagovesta Popova (14546), Dan Wang (34472), Abirami Rajavel (10584206), Karthikeyan Dhamotharan (10584209), Diana F. Lázaro (10224463), Jennifer Gerke (236089), Joachim F. Uhrig (10584212), Michael Hoppert (712772), Tiago F. Outeiro (191379), Gerhard H. Braus (150631)

مصطلحات موضوعية: Molecular Biology, Neuroscience, Structural Biology, Central Nervous System, Molecular Evolution, Molecular Medicine, α-synuclein, Parkinson’s disease, protein aggregation, oligomerization, peptide drug discovery, yeast, library screening

العلاقة: https://figshare.com/articles/figure/Image_7_Identification_of_Two_Novel_Peptides_That_Inhibit_-Synuclein_Toxicity_and_Aggregation_TIF/14400758Test

الإتاحة: https://doi.org/10.3389/fnmol.2021.659926.s007Test

View record in BASE

5

صورة

Image_4_Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation.TIF

المؤلفون: Blagovesta Popova, Dan Wang, Abirami Rajavel, Karthikeyan Dhamotharan, Diana F. Lázaro, Jennifer Gerke, Joachim F. Uhrig, Michael Hoppert, Tiago F. Outeiro, Gerhard H. Braus

مصطلحات موضوعية: Molecular Biology, Neuroscience, Structural Biology, Central Nervous System, Molecular Evolution, Molecular Medicine, α-synuclein, Parkinson’s disease, protein aggregation, oligomerization, peptide drug discovery, yeast, library screening

العلاقة: https://figshare.com/articles/figure/Image_4_Identification_of_Two_Novel_Peptides_That_Inhibit_-Synuclein_Toxicity_and_Aggregation_TIF/14400749Test

الإتاحة: https://doi.org/10.3389/fnmol.2021.659926.s004Test
https://figshare.com/articles/figure/Image_4_Identification_of_Two_Novel_Peptides_That_Inhibit_-Synuclein_Toxicity_and_Aggregation_TIF/14400749Test

View record in BASE

6

Small Molecules Detected by Second-Harmonic Generation Modulate the Conformation of Monomeric α-Synuclein and Reduce Its Aggregation in Cells

المؤلفون: Guowei Yin, Karin Giller, Markus Zweckstetter, Tiago F. Outeiro, Timo Strohäker, Francesca Munari, Joshua Salafsky, Ben Moree, Diana F. Lázaro, Stefan Becker

المصدر: Journal of Biological Chemistry
The Journal of Biological Chemistry
The journal of biological chemistry 290(46), 27582-27593 (2015). doi:10.1074/jbc.M114.636027

مصطلحات موضوعية: Protein Conformation, animal diseases, pharmacology [Small Molecule Libraries], Protein aggregation, Ligands, Biochemistry, Antiparkinson Agents, chemistry.chemical_compound, 0302 clinical medicine, Protein structure, Neurons, 0303 health sciences, Tumor, Drug discovery, Parkinson Disease, Small molecule, 3. Good health, metabolism [Neurons], ddc:540, chemistry [Antiparkinson Agents], alpha-Synuclein, Parkinson disease, drug discovery, protein aggregation, protein conformation, protein drug interaction, Cell Line, Tumor, Humans, Protein Aggregates, Protein Aggregation, Pathological, Small Molecule Libraries, isolation & purification [Small Molecule Libraries], Molecular Biophysics, chemistry [Small Molecule Libraries], metabolism [Parkinson Disease], Cell Line, 03 medical and health sciences, metabolism [Protein Aggregation, Pathological], Pathological, mental disorders, Molecular Biology, 030304 developmental biology, Alpha-synuclein, pharmacology [Antiparkinson Agents], drug therapy [Protein Aggregation, Pathological], Binding protein, drug effects [Protein Aggregates], Cell Biology, Protein Aggregation, drug therapy [Parkinson Disease], isolation & purification [Antiparkinson Agents], nervous system diseases, drug effects [Protein Conformation], chemistry [alpha-Synuclein], nervous system, chemistry, Biophysics, 030217 neurology & neurosurgery, Protein ligand

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e94d4e41f529440ed17d7b805a1a18abTest
https://doi.org/10.1074/jbc.m114.636027Test

7

Molecular characterization of an aggregation-prone variant of alpha-synuclein used to model synucleinopathies

المؤلفون: Timo Strohäker, Ariel A. Valiente-Gabioud, Claudio O. Fernández, Pablo Peralta, Markus Zweckstetter, Filippo Favretto, Diana F. Lázaro, Annekatrin König, Caterina Masaracchia, Tiago F. Outeiro

المصدر: Biochimica et biophysica acta / Proteins and proteomics 1868(1), 140298 (2020). doi:10.1016/j.bbapap.2019.140298
Biochimica et Biophysica Acta-Proteins and Proteomics

مصطلحات موضوعية: 0301 basic medicine, Synucleinopathies, Parkinson's disease, Biophysics, Protein aggregation, Electron, Protein Aggregation, Pathological, Biochemistry, Cell Line, Analytical Chemistry, Alpha-synuclein, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Microscopy, Electron, Transmission, Pathological, ddc:570, Cell Line, Tumor, Mammalian cell, Escherichia coli, medicine, Transmission, Humans, metabolism [alpha-Synuclein], Neurodegeneration, Molecular Biology, Microscopy, Physiological function, Misfolding, Tumor, Chemistry, Vesicle, ultrastructure [alpha-Synuclein], genetics [Escherichia coli], medicine.disease, Pathogenicity, Protein Aggregation, 030104 developmental biology, chemistry [alpha-Synuclein], genetics [alpha-Synuclein], alpha-Synuclein, 030217 neurology & neurosurgery