MAIN


©1996-2019. All Rights Reserved. Online Journal of Bioinformatics . You may not store these pages in any form except for your own personal use. All other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the  before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to OJB publications. This article may be copied once but may not be, reproduced or  re-transmitted without the express permission of the editors. This journal satisfies the refereeing requirements (DEST) for the Higher Education Research Data Collection (Australia). Linking: To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.


OJBTM

 Online Journal of Bioinformatics © 

 Volume 15 (1): 87-97, 2014.


Structure prediction of alpha-synuclein protein and link with neurodegenerative disease.

 

Rashmika Singh1, 3, Navin K Gaur2, 3, Ankur Mohan3, Pallavi Gangwar3

 

1Institute of Engineering and Technology, Lucknow, 2Harcourt Butler Technological Institute, Kanpur, 3Bio-EGICORE (Dept. of Life Science of EGICORE) Lucknow, India.

 

ABSTRACT

 

Singh R, Gaur NK, Mohan A, Gangwar P., Structure prediction of alpha-synuclein protein and link with neurodegenerative disease, Onl J Bioinform., 15(1)87-97, 2014. Neurodegenerative diseases, such as Parkinsonís disease (PD) and Alzheimerís disease (AD), are a group of pathologies characterized by a progressive and specific loss of certain brain areas. The pathogenesis of these disorders centrally involves abnormal accumulation and aggregation of specific proteins. Pathological studies showed that Alpha-synuclein protein is responsible for formation of intraneuronal Lewy bodies and Lewy neuritis (hallmarks of PD) while others proteins like tau and beta amyloid form extracellular β-amyloid deposits intracellular neurofibrillary tangles (hallmarks of AD). However evidence from in vitro and in vivo studies showed that these proteins are responsible for each otherís aggregation with different seeding abilities. This idea is taken further to develop a common therapeutic treatment for both the diseases by targeting alpha synuclein pathologies involved in both of them. Since the precise structure of alpha synuclein protein is not yet available. Therefore, a theoretical model of this protein was generated using homology Modeling. Validation of structure was done by using PROCHECK available at SAVES server.

 

Keywords: Alzheimerís disease, Parkinsonís disease, SNCA, Homology Modeling, PMDB, SAVES.


MAIN

 

FULL-TEXT (SUBSCRIBE OR PURCHASE TITLE $25USD)