Functional and Structural characterization of ADF/cofilin homologue from Leishmania donovani.

Tammana, T V S

dc.contributor.author	Tammana, T V S
dc.date.accessioned	2014-01-24T10:15:28Z
dc.date.available	2014-01-24T10:15:28Z
dc.date.issued	2010
dc.identifier.uri	http://hdl.handle.net/123456789/1179
dc.description	Guide- Dr. C M Gupta, Ph D Thesis submitted to JNU New Delhi in 2009.	en
dc.description.abstract	ADF/cofilin family of proteins is ubiquitously present in all eukaryotes. Metazoans have two or more members of this group of proteins, yeast and amoeba express only one member of ADF/cofilin family (Ono, 2007). These small molecular mass proteins regulate actin dynamics in a variety of ways. Various in-vitro studies have shown that ADF/cofilin accelerate actin monomer dissociation from pointed ends which adds in to the monomer pool of actin (Bamburg, 1999; Carlier et al., 1999; Pollard et al., 2000). ADF/cofilin also exhibit weak actin filament severing activity which generates new barbed ends and facilitate rapid increase in filament assembly at the leading edge (Maciver et al., 1991; Ono, 2003). These activities have recently been shown to depend on the concentration of ADF/cofilin proteins (Andrianantoandro and Pollard 2006).	en
dc.format.extent	12271563 bytes
dc.format.mimetype	application/pdf
dc.language.iso	en	en
dc.relation.ispartofseries	CSIR-CDRI Thesis No.- T-36	en
dc.subject	Eukaryotes	en
dc.subject	Metazoans	en
dc.title	Functional and Structural characterization of ADF/cofilin homologue from Leishmania donovani.	en
dc.type	Thesis	en