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Regulatory Mechanisms of Antiviral S...

Northwestern University.

Regulatory Mechanisms of Antiviral Signaling.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
書名/作者:	Regulatory Mechanisms of Antiviral Signaling.
作者:	Rodriguez, Kenny R.
面頁冊數:	137 p.
附註:	Source: Dissertation Abstracts International, Volume: 77-05(E), Section: B.
Contained By:	Dissertation Abstracts International77-05B(E).
標題:	Cellular biology.
標題:	Molecular biology.
標題:	Biology.
ISBN:	9781339336169
摘要、提要註:	Mammalian cells have the ability to recognize virus infection by initiating a barrier to replication that impacts both innate and adaptive immune responses. The interferon (IFN) antiviral system is triggered upon recognition of non-self RNAs by the cytoplasmic sensors RIG-I, MDA5, and LGP2. The RNA-activated sensors then initiate oligomerization of MAVS, an adaptor that recruits TRAF ubiquitin ligases to activate IKK-family kinases that induce IRF3 and NFkappaB activation.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3741336

Regulatory Mechanisms of Antiviral Signaling.
Rodriguez, Kenny R.

Regulatory Mechanisms of Antiviral Signaling. - 137 p.

Source: Dissertation Abstracts International, Volume: 77-05(E), Section: B.

Thesis (Ph.D.)--Northwestern University, 2015.

Mammalian cells have the ability to recognize virus infection by initiating a barrier to replication that impacts both innate and adaptive immune responses. The interferon (IFN) antiviral system is triggered upon recognition of non-self RNAs by the cytoplasmic sensors RIG-I, MDA5, and LGP2. The RNA-activated sensors then initiate oligomerization of MAVS, an adaptor that recruits TRAF ubiquitin ligases to activate IKK-family kinases that induce IRF3 and NFkappaB activation.

ISBN: 9781339336169Subjects--Topical Terms:

629801
Cellular biology.

Regulatory Mechanisms of Antiviral Signaling.
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100 1 $a Rodriguez, Kenny R. $3 630113
245 1 0 $a Regulatory Mechanisms of Antiviral Signaling.
300 $a 137 p.
500 $a Source: Dissertation Abstracts International, Volume: 77-05(E), Section: B.
500 $a Adviser: Curt M. Horvath.
502 $a Thesis (Ph.D.)--Northwestern University, 2015.
520 $a Mammalian cells have the ability to recognize virus infection by initiating a barrier to replication that impacts both innate and adaptive immune responses. The interferon (IFN) antiviral system is triggered upon recognition of non-self RNAs by the cytoplasmic sensors RIG-I, MDA5, and LGP2. The RNA-activated sensors then initiate oligomerization of MAVS, an adaptor that recruits TRAF ubiquitin ligases to activate IKK-family kinases that induce IRF3 and NFkappaB activation.
520 $a The importance of these proteins is highlighted by the discovery of virus-encoded immune evasion strategies that inhibit IFN production. The IFN antagonist, paramyxovirus V protein, can bind to MDA5 and LGP2 but not RIG-I. Chapter 2 demonstrates MDA5 R806 to be essential for inhibition by diverse V proteins. Complementary substitution to the analogous RIG-I L714 restores V protein recognition. The analogous LGP2 R455 is required for recognition by measles V protein only. These findings indicate that a single amino acid distinguishes MDA5 from RIG-I, and have evolved distinct contact sites for LGP2 interference.
520 $a A body of prior work demonstrate LGP2 as both a positive and negative regulator of RIG-I-like-receptor signaling. This apparent dichotomy complicated efforts to assess the unique consequences of V protein interaction with LGP2. Chapter 3 directly evaluates the impact of LGP2 interference. MDA5 and LGP2 variants unable to be recognized by measles virus and PIV5 V proteins were tested in signaling assays. Results from Chapter 3 indicate that V protein interaction with LGP2 specifically prevents co-activation of MDA5 signaling, and V proteins did not affect LGP2's negative regulatory capacity. These results clarify the unique consequences of LGP2 interference by paramyxovirus V proteins and help resolve the distinct roles of LGP2 in both activation and inhibition of antiviral signaling.
520 $a While mechanisms of LGP2 co-activation are well understood, less is known about the targets for LGP2 interference. In Chapter 4, LGP2 suppresses TRAF proteins and disengages their K63 ubiquitin ligase activity to prevent NFkappaB activation. LGP2 disruption of TRAF-mediated NFkappaB activation by cGAMP, TNFalpha and IL-1beta extends the impact of LGP2 inhibition beyond MAVS-dependent antiviral signaling. In all, I will address questions regarding the negative regulation of the IFN system..
590 $a School code: 0163.
650 4 $a Cellular biology. $3 629801
650 4 $a Molecular biology. $3 182854
650 4 $a Biology. $3 171887
690 $a 0379
690 $a 0307
690 $a 0306
710 2 $a Northwestern University. $b Interdepartmental Biological Sciences Program. $3 630114
773 0 $t Dissertation Abstracts International $g 77-05B(E).
790 $a 0163
791 $a Ph.D.
792 $a 2015
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3741336

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