Senthil T Kumar

发表

A simple, versatile and robust centrifugation‐based filtration protocol for the isolation and quantification of α‐synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α‐synuclein research

H. Lashuel, A. Chiki, Senthil T. Kumar, 2019, bioRxiv.

Amyloid fibril recognition with the conformational B10 antibody fragment depends on electrostatic interactions.

M. Fändrich, C. Parthier, M. Stubbs, 2011, Journal of molecular biology.

Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation

C. Mawrin, M. Fändrich, J. Balbach, 2016, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.

Solvent Removal Induces a Reversible β-to-α Switch in Oligomeric Aβ Peptide.

M. Fändrich, M. Görlach, Senthil T. Kumar, 2016, Journal of molecular biology.

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM

F. Stellacci, A. Alexander-Katz, H. Lashuel, 2019, Proceedings of the National Academy of Sciences.

Structure and biomedical applications of amyloid oligomer nanoparticles.

M. Fändrich, T. Simmet, T. Aumüller, 2014, ACS nano.

How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology

H. Vanderstichele, H. Lashuel, Senthil T. Kumar, 2020, Neurobiology of Disease.

Disulfide conformation and design at helix N‐termini

R. Varadarajan, C. Ramakrishnan, S. Thakurela, 2009, Proteins.

H. Lashuel, A. Chiki, Senthil T. Kumar, 2020, Journal of neurochemistry.

Pattern recognition with a fibril-specific antibody fragment reveals the surface variability of natural amyloid fibrils.

M. Fändrich, C. Röcken, P. Hortschansky, 2011, Journal of molecular biology.

Liquefaction of Semen Generates and Later Degrades a Conserved Semenogelin Peptide That Enhances HIV Infection

K. Pollard, W. Greene, F. Kirchhoff, 2014, Journal of Virology.

Structural characterization of amyloid fibrils from the human parathyroid hormone.

H. Scheidt, D. Huster, M. Fändrich, 2015, Biochimica et biophysica acta.

Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology: How specific are the conformation-specific α-synuclein antibodies?

H. Vanderstichele, H. Lashuel, Senthil T. Kumar, 2020, bioRxiv.

Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases

C. Strand, J. Holton, H. Lashuel, 2022, bioRxiv.

Chronic corticosterone aggravates behavioral and neuronal symptomatology in a mouse model of alpha-synuclein pathology

C. Sandi, H. Lashuel, A. Chiki, 2019, Neurobiology of Aging.

Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases

C. Strand, J. Holton, H. Lashuel, 2023, bioRxiv.

Post-fibrillization nitration of alpha-synuclein abolishes its seeding activity and pathology formation in primary neurons and in vivo

D. D. Di Monte, H. Lashuel, A. Chiki, 2023, bioRxiv.

A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity

H. Lashuel, F. Sobott, Rani Moons, 2022, Science advances.

Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage

H. Lashuel, S. Porta, Senthil T. Kumar, 2023, Nature Neuroscience.

A novel mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein fibrils and recapitulates its pathological diversity

H. Lashuel, F. Sobott, Rani Moons, 2021, bioRxiv.