Výsledky vyhledávání

The Familial alpha-Synuclein A53E Mutation Enhances Cell Death in Response to Environmental Toxins Due to a Larger Population of Oligomers

Autor: MOHITE, GM, NAVALKAR, A, KUMAR, R, MEHRA, S, DAS, S, GADHE, LG, GHOSH, D, ALIAS, B, CHANDRAWANSHI, V, RAMAKRISHNAN, A, MAJI, SK

Publikováno v: IndraStra Global.

Amyloid formation of alpha-synuclein (alpha-Syn) and its familial mutations are directly linked with Parkinson's disease (PD) pathogenesis. Recently, a new familial alpha-Syn mutation (A53E) was discovered, associated with an early onset aggressive f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=issn23813652::188089aec48c5aeb95a9bff082e81d00

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Detection and differentiation of alpha-Synuclein monomer and fibril by chitosan film coated nanogold array on optical sensor platform

Autor: KHATRIL, A, PUNJABI, N, GHOSH, D, MAJI, SK, MUKHERJI, S

Publikováno v: IndraStra Global.

alpha-Synuclein protein, whose aggregation is associated with Parkinson's disease, is detected using a compact, label-free, localized surface plasmon resonance (LSPR) based optical sensor. U-shaped fiber optic probe immobilized with gold nanoparticle

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=issn23813652::92f6f326c502a3b30314516d2456d559
http://dspace.library.iitb.ac.in/xmlui/handle/100/22690

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Glycosaminoglycans have variable effects on alpha-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils

Autor: MEHRA, S, GHOSHN, D, KUMAR, R, MONDAL, M, GADHE, LG, DAS, S, ANOOP, A, JHA, NN, JACOB, RS, CHATTERJEE, D, RAY, S, SINGH, N, KUMAR, A, MAJI, SK

Publikováno v: IndraStra Global.

Parkinson's disease is mainly a sporadic disorder in which both environmental and cellular factors play a major role in the initiation of this disease. Glycosaminoglycans (GAG) are integral components of the extracellular matrix and are known to infl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=issn23813652::8a3b1aa7d26e140406c1eb595f69f36e
http://dspace.library.iitb.ac.in/xmlui/handle/100/23610

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Multitude NMR studies of alpha-synuclein familial mutants: probing their differential aggregation propensities

Autor: BHATTACHARYYA, D, KUMAR, R, MEHRA, S, GHOSH, A, MAJI, SK, BHUNIA, A

Publikováno v: IndraStra Global.

Familial mutations in alpha-synuclein affect the immediate chemical environment of the protein's backbone, changing its aggregation kinetics and forming diverse structural and functional intermediates. This study, concerning two oppositely aggregatin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=issn23813652::bb7921006f080ab8d73f462350cd8238
https://igi.indrastra.com/items/show/59350

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Complexation of NAC-Derived Peptide Ligands with the C-Terminus of alpha-Synuclein Accelerates Its Aggregation

Autor: JHA, NN, RANGANATHAN, S, KUMAR, R, MEHRA, S, PANIGRAHI, R, NAVALKAR, A, GHOSH, D, KUMAR, A, PADINHATEERI, R, MAJI, SK

Publikováno v: IndraStra Global.

Aggregation of alpha-synuclein (alpha-Syn) into neurotoxic oligomers and amyloid fibrils is suggested to be the pathogenic mechanism for Parkinson's disease (PD). Recent studies'have indicated that oligomeric species of alpha-Syn are more cytotoxic t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=issn23813652::0bf3f0b881388e49d9e0f7fe819ba5b9
http://dspace.library.iitb.ac.in/xmlui/handle/100/24967

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Naturally Occurring Variants of the Dysglycemic Peptide Pancreastatin DIFFERENTIAL POTENCIES FOR MULTIPLE CELLULAR FUNCTIONS AND STRUCTURE-FUNCTION CORRELATION

Autor: ALLU, PKR, CHIRASANI, VR, GHOSH, D, MANI, A, BERA, AK, MAJI, SK, SENAPATI, S, MULLASARI, AS, MAHAPATRA, NR

Publikováno v: IndraStra Global.

Pancreastatin (PST), a chromogranin A-derived peptide, is a potent physiological inhibitor of glucose-induced insulin secretion. PST also triggers glycogenolysis in liver and reduces glucose uptake in adipocytes and hepatocytes. Here, we probed for g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=issn23813652::5c358e0cf869a3c854152de1e7f99d8f
https://igi.indrastra.com/items/show/48614

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Elucidating the Role of Disulfide Bond on Amyloid Formation and Fibril Reversibility of Somatostatin-14 RELEVANCE TO ITS STORAGE AND SECRETION

Autor: ANOOP, A, RANGANATHAN, S, DAS DHAKED, B, JHA, NN, PRATIHAR, S, GHOSH, S, SAHAY, S, KUMAR, S, DAS, S, KOMBRABAIL, M, AGARWAL, K, JACOB, RS, SINGRU, P, BHAUMIK, P, PADINHATEERI, R, KUMAR, A, MAJI, SK

Publikováno v: IndraStra Global.

The storage of protein/peptide hormones within subcellular compartments and subsequent release are crucial for their native function, and hence these processes are intricately regulated in mammalian systems. Several peptide hormones were recently sug

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=issn23813652::f7820bf2574fb54cf80ba5d1836b2eb0

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In vivo demonstration that alpha-synuclein oligomers are toxic

Autor: Winner B, Jappelli R, Maji SK, Desplats PA, Boyer L, Aigner S, Hetzer C, Loher T, Vilar M, Campioni S, Tzitzilonis C, Soragni A, Jessberger S, Mira H, Consiglio A, Pham E, Masliah E, Gage FH, Riek R

Publikováno v: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
instname
r-FSJD: Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
Fundació Sant Joan de Déu

The aggregation of proteins into oligomers and amyloid fibrils is characteristic of several neurodegenerative diseases, including Parkinson disease (PD). In PD, the process of aggregation of a-synuclein (a-syn) from monomers, via oligomeric intermedi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::72f352b8ce4d3bd0ff389bc1063f7dee
http://hdl.handle.net/11379/166379

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