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Pamela V. Martino Adami
Researcher at Fundación Instituto Leloir
Publications - 20
Citations - 532
Pamela V. Martino Adami is an academic researcher from Fundación Instituto Leloir. The author has contributed to research in topics: Dementia & Internal medicine. The author has an hindex of 8, co-authored 15 publications receiving 374 citations. Previous affiliations of Pamela V. Martino Adami include University of Cologne & National Scientific and Technical Research Council.
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Journal ArticleDOI
Synaptopathies: synaptic dysfunction in neurological disorders - A review from students to students
Katarzyna Lepeta,Mychael V. Lourenco,Barbara Schweitzer,Pamela V. Martino Adami,Priyanjalee Banerjee,Silvina Catuara-Solarz,Mario de la Fuente Revenga,Alain M. Guillem,Mouna Haidar,Omamuyovwi M. Ijomone,Bettina Nadorp,Lin Qi,Nirma D Perera,Louise K. Refsgaard,Kimberley M. Reid,Mariam Sabbar,Arghyadip Sahoo,Natascha Schaefer,Rebecca K. Sheean,Anna Suska,Rajkumar Verma,Cinzia Vicidomini,Dean J. Wright,Xingding Zhang,Constanze I. Seidenbecher +24 more
TL;DR: Basic concepts of synapse structure and function are discussed, and a critical view of how aberrant synapse physiology may contribute to neurodevelopmental disorders as well as neurodegenerative disorders are provided.
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Longitudinal analysis of the behavioral phenotype in a novel transgenic rat model of early stages of Alzheimer's disease
Pablo Galeano,Pablo Galeano,Pamela V. Martino Adami,Sonia Do Carmo,Eduardo Blanco,Cecilia Rotondaro,Francisco Capani,Eduardo M. Castaño,A. Claudio Cuello,Laura Morelli +9 more
TL;DR: The data from the present study demonstrate that the hemizygous transgenic McGill-R-Thy1-APP rat has a wide array of behavioral and cognitive impairments from young adulthood to middle-age, which supports its potential use for drug discovery purposes in early AD.
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Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic aβ peptide aggregates.
Matias Blas de Tullio,Valeria Castelletto,Ian W. Hamley,Pamela V. Martino Adami,Laura Morelli,Eduardo M. Castaño +5 more
TL;DR: The results suggest that IDE has a chaperone-like activity upon amyloid-forming peptides and whether other highly conserved metallopeptidases have a dual protease-chaperone function to prevent the formation of toxic peptide oligomers from bacteria to mammals.
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Synaptosomal bioenergetic defects are associated with cognitive impairment in a transgenic rat model of early Alzheimer's disease.
Pamela V. Martino Adami,Cecilia Quijano,Natalia Magnani,Pablo Galeano,Pablo Galeano,Pablo Evelson,Adriana Cassina,Sonia Do Carmo,Maria Celeste Leal,Eduardo M. Castaño,Claudio Cuello,Laura Morelli +11 more
TL;DR: Evidence is provided that, as described in AD brain and not proven in Tg mice models with AD-like phenotype, the mitochondrial bioenergetic capacity of synaptosomes is not conserved in the Tg(+/−) rats, which may be suitable for understanding the basic biochemical mechanisms involved in early AD.
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Perturbed mitochondria–ER contacts in live neurons that model the amyloid pathology of Alzheimer's disease
Pamela V. Martino Adami,Pamela V. Martino Adami,Zuzana Nichtova,David Weaver,Adam Bartok,Thomas Wisniewski,Drew R. Jones,Sonia Do Carmo,Eduardo M. Castaño,Claudio Cuello,György Hajnóczky,Laura Morelli +11 more
TL;DR: Dynamic analysis of live neurons modelling Alzheimer's disease (AD)-like amyloid pathology shows loosened mitochondria-ER contacts (MERC), providing a novel perturbation of the MERC axis in AD.