Amyloidogenic Proceses Of Intrinsically Disordered Proteins: Understanding the aggregation process of intrinsically unstructured proteins related to neurodegenerative diseases - Couverture souple

Kumar, Dhruv; Brucale, Marco; Samori, Bruno

 
9783659592928: Amyloidogenic Proceses Of Intrinsically Disordered Proteins: Understanding the aggregation process of intrinsically unstructured proteins related to neurodegenerative diseases
Couverture souple
ISBN 10 : 3659592927 ISBN 13 : 9783659592928
Editeur : LAP LAMBERT Academic Publishing, 2014

Synopsis

Many untreatable neurodegenerative human disorders, like Parkinson’s, Alzheimer’s, and prion diseases, are associated with the aggregation of misfolded or natively unfolded proteins into amyloid fibrils. Cells have adapted two main sophisticated quality-control measures to protect against these protein aggregation processes: the molecular chaperones against the misfolded protein conformations that trigger the aggregation, and the ubiquitin-proteasome system to degrade those proteins that remain misfolded. Despite these natural defense mechanisms amyloidoses may very soon be the most prevalent and socially disruptive illness in the aging population. Currently available therapies against these diseases can neither arrest nor reverse their progression: only the symptoms can be managed. Most current efforts to develop new therapeutics are based on antibodies or synthetic molecules with sufficiently high affinity to compete against, and to inhibit the aggregation of proteins and/or to potentially dissolve their aggregates, once they are formed.

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

Présentation de l'éditeur

Many untreatable neurodegenerative human disorders, like Parkinson’s, Alzheimer’s, and prion diseases, are associated with the aggregation of misfolded or natively unfolded proteins into amyloid fibrils. Cells have adapted two main sophisticated quality-control measures to protect against these protein aggregation processes: the molecular chaperones against the misfolded protein conformations that trigger the aggregation, and the ubiquitin-proteasome system to degrade those proteins that remain misfolded. Despite these natural defense mechanisms amyloidoses may very soon be the most prevalent and socially disruptive illness in the aging population. Currently available therapies against these diseases can neither arrest nor reverse their progression: only the symptoms can be managed. Most current efforts to develop new therapeutics are based on antibodies or synthetic molecules with sufficiently high affinity to compete against, and to inhibit the aggregation of proteins and/or to potentially dissolve their aggregates, once they are formed.

Biographie de l'auteur

I graduated in Chemistry (Hons.) from Banaras Hindu University (BHU), Varanasi, India in 2006. I have completed Master of Science in Bioinformatics from University of Allahabad, Allahabad, India in 2008. After completion of my master's degree I joined University of Bologna, Italy to complete my PhD in Cellular, Molecular and Industrial Biology.

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
LAP LAMBERT Academic Publishing
Date d'édition
2014
Langue
anglais
ISBN 10 
3659592927
ISBN 13 
9783659592928
Reliure
Broché
Nombre de pages
124
Coordonnées du fabricant
non disponible
Personne responsable
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