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Dependency of neurotrophin receptor-...

Rochira, Jennifer A.

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Dependency of neurotrophin receptor-interacting melanoma associated antigen protein in bone morphogenetic protein-mediated apoptosis.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Dependency of neurotrophin receptor-interacting melanoma associated antigen protein in bone morphogenetic protein-mediated apoptosis./
Author:	Rochira, Jennifer A.
Description:	205 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-12, Section: B, page: .
Contained By:	Dissertation Abstracts International71-12B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3431394
ISBN:	9781124309736

Dependency of neurotrophin receptor-interacting melanoma associated antigen protein in bone morphogenetic protein-mediated apoptosis.
Rochira, Jennifer A.

Dependency of neurotrophin receptor-interacting melanoma associated antigen protein in bone morphogenetic protein-mediated apoptosis. - 205 p.

Source: Dissertation Abstracts International, Volume: 71-12, Section: B, page: .

Thesis (Ph.D.)--The University of Maine, 2010.

The mitogen-activated protein kinase (MAPK) pathway of bone morphogenetic protein (BMP) signaling has emerged as an alternative BMP pathway to the canonical SMAD pathway. Seminal investigations of neurotrophin receptor-interacting melanoma-associated antigen protein (NRAGE) have shown that it is a required component of the BMP MAPK pathway leading to apoptosis of neural progenitor cells.

ISBN: 9781124309736Subjects--Topical Terms:

1017719
Biology, Molecular.

Dependency of neurotrophin receptor-interacting melanoma associated antigen protein in bone morphogenetic protein-mediated apoptosis.
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020 $a 9781124309736
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040 $a UMI $c UMI
100 1 $a Rochira, Jennifer A. $3 1673264
245 1 0 $a Dependency of neurotrophin receptor-interacting melanoma associated antigen protein in bone morphogenetic protein-mediated apoptosis.
300 $a 205 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-12, Section: B, page: .
500 $a Advisers: Joseph M. Verdi; Samuel T. Hess.
502 $a Thesis (Ph.D.)--The University of Maine, 2010.
520 $a The mitogen-activated protein kinase (MAPK) pathway of bone morphogenetic protein (BMP) signaling has emerged as an alternative BMP pathway to the canonical SMAD pathway. Seminal investigations of neurotrophin receptor-interacting melanoma-associated antigen protein (NRAGE) have shown that it is a required component of the BMP MAPK pathway leading to apoptosis of neural progenitor cells.
520 $a NRAGE is a member of the MAGE family of genes which are responsible for the cell surface expression of tumor-specific peptides and is detected in tumor cells. However, NRAGE does not code for tumor-specific peptides and is expressed in most developmental and adult tissues. It is unlike any other MAGE member in that it possesses a unique repeat domain of amino acids that is only found in human, rat, and mouse homologs. Thus, the overall hypothesis of this thesis is that the NRAGE repeat domain is a pivotal binding domain in the BMP MAPK pathway.
520 $a Pursuant to the hypothesis, the interaction between NRAGE and X-linked inhibitor of apoptosis (XIAP) was specifically investigated to identify the NRAGE binding domain. XIAP is another member in the BMP MAPK pathway that has critical roles in caspase inhibition, receptor signaling, cell division, and ubiquitination of proteins for proteasomal degradation. The goal in identifying the binding domain of NRAGE to XIAP was to develop a small peptide that would affect downstream signaling of the BMP MAPK pathway.
520 $a Using fluorescence resonance energy transfer (FRET), we showed that the repeat domain of NRAGE is the binding domain for XIAP. Based on this data, an oligopeptide was designed after the NRAGE repeat domain and found to inhibit downstream signaling of BMP-induced NF-kappaB activation and apoptosis in P19 neural progenitor cells. FRET analyses showed that NRAGE and XIAP are still binding in the presence of the peptide thus leading to the hypothesis that the peptide is disrupting the dimerization of XIAP in the BMP pathway that is necessary to initiate downstream signaling. NRAGE may be a candidate protein to inhibit for the treatment in certain diseases which may be achievable with the oligopeptide.
590 $a School code: 0113.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Genetics. $3 1017730
690 $a 0307
690 $a 0369
710 2 $a The University of Maine. $3 1029373
773 0 $t Dissertation Abstracts International $g 71-12B.
790 1 0 $a Verdi, Joseph M., $e advisor
790 1 0 $a Hess, Samuel T., $e advisor
790 $a 0113
791 $a Ph.D.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3431394