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Computational studies of the functio...

Cavalli, Marco.

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Computational studies of the functional states associated with epidermal growth factor receptor activation.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Computational studies of the functional states associated with epidermal growth factor receptor activation./
作者:	Cavalli, Marco.
面頁冊數:	236 p.
附註:	Source: Dissertation Abstracts International, Volume: 72-04, Section: B, page: 2086.
Contained By:	Dissertation Abstracts International72-04B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3440374
ISBN:	9781124476278

Computational studies of the functional states associated with epidermal growth factor receptor activation.
Cavalli, Marco.

Computational studies of the functional states associated with epidermal growth factor receptor activation. - 236 p.

Source: Dissertation Abstracts International, Volume: 72-04, Section: B, page: 2086.

Thesis (Ph.D.)--City University of New York, 2011.

Epidermal growth factor receptors (EGFR) belong to the ErbB family of receptor tyrosine kinases. ErbB signaling is involved in a wide range of biological processes including cell motility, migration and adhesion as well as gene transcription, differentiation, proliferation and apoptosis. ErbB receptors are known to dimerize upon ligand binding. This event is thought to promote intracellular transactivation of the receptors and consequently trigger a number of signaling cascades.

ISBN: 9781124476278Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Computational studies of the functional states associated with epidermal growth factor receptor activation.
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245 1 0 $a Computational studies of the functional states associated with epidermal growth factor receptor activation.
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500 $a Source: Dissertation Abstracts International, Volume: 72-04, Section: B, page: 2086.
500 $a Adviser: Marco Ceruso.
502 $a Thesis (Ph.D.)--City University of New York, 2011.
520 $a Epidermal growth factor receptors (EGFR) belong to the ErbB family of receptor tyrosine kinases. ErbB signaling is involved in a wide range of biological processes including cell motility, migration and adhesion as well as gene transcription, differentiation, proliferation and apoptosis. ErbB receptors are known to dimerize upon ligand binding. This event is thought to promote intracellular transactivation of the receptors and consequently trigger a number of signaling cascades.
520 $a Mutation and over expression of ErbB receptors have been associated with the onset of many human malignancies, making ErbB receptors central targets in cancer therapy research. Most of these mutations are localized in the intracellular tyrosine kinase domain but recently mutations have also been identified in the extracellular region of the receptors.
520 $a EGFRs are present on the cell surface in a tethered conformation (believed to correspond to an auto inhibited state). In this tethered conformation the so called "dimerization arm" (a beta hairpin protruding from the extracellular D2 domain) is masked by intra molecular contacts. Upon ligand binding a dramatic conformational change reorients the extracellular domains exposing the dimerization arm, promoting the dimerization and eventually triggering the signaling cascades.
520 $a The main objective of this thesis is to investigate computationally the conformational events that lead to the extension of the extracellular region of EGFR and to analyze the energetics of the process.
520 $a Most biological processes in the cell occur at time-scales and involve macromolecular assembly sizes that are often beyond the current limits of classical all-atom computational simulation approaches. One possible solution to overcome these time- and size-scale limitations is to move from all-atom to coarse-grained representations of molecules. We have undertaken the development of structural representations that can enable an accurate description of the conformational dynamics and known structural transitions of protein macromolecules. The long-term objective is to be able to elucidate in a realistic environment (including both lipids and whole transmembrane protein receptors) the molecular mechanisms underlying EGFR-mediated transmembrane signaling events.
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790 1 0 $a Ghose, Ranajeet $e committee member
790 1 0 $a Gunner, Marilyn $e committee member
790 1 0 $a Hubbard, Stevan R. $e committee member
790 1 0 $a Lazaridis, Themis $e committee member
790 1 0 $a Rotenberg, Susan A. $e committee member
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