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LDR00000nmm u2200205 4500
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008181129s2018 ||| | | | eng d
020 ▼a 9780438362758
035 ▼a (MiAaPQ)AAI10843263
035 ▼a (MiAaPQ)purdue:23100
040 ▼a MiAaPQ ▼c MiAaPQ ▼d 248032
0491 ▼f DP
0820 ▼a 580
1001 ▼a Wang, Zhe.
24510 ▼a Functional Analysis of ER Localized Ubac2 and Ubac2- Interacting Proteins From Arabidopsis.
260 ▼a [S.l.] : ▼b Purdue University., ▼c 2018
260 1 ▼a Ann Arbor : ▼b ProQuest Dissertations & Theses, ▼c 2018
300 ▼a 187 p.
500 ▼a Source: Dissertation Abstracts International, Volume: 80-01(E), Section: B.
500 ▼a Adviser: Zhixiang Chen.
5021 ▼a Thesis (Ph.D.)--Purdue University, 2018.
520 ▼a Selective autophagy targets specific cargo by autophagy receptors through interaction with ATG8 (autophagy-related protein 8)/MAP1LC3 (microtubule associated protein 1 light chain 3) for degradation in the vacuole. Here, we report the identifica
520 ▼a Further analysis shows that ubac2 also plays a role in Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI). PTI is initiated upon recognition of PAMPs by pattern recognition receptors (PRRs), which is then transmitted through a
520 ▼a Using yeast two-hybrid screening, we found that ubac2 interacts with three unknown proteins weakly which were demonstrated to interact with ER body component NAI2 strongly later, thus these three unknown proteins were named NAIP. ER body is one
590 ▼a School code: 0183.
650 4 ▼a Plant sciences.
690 ▼a 0479
71020 ▼a Purdue University. ▼b Botany and Plant Pathology.
7730 ▼t Dissertation Abstracts International ▼g 80-01B(E).
773 ▼t Dissertation Abstract International
790 ▼a 0183
791 ▼a Ph.D.
792 ▼a 2018
793 ▼a English
85640 ▼u http://www.riss.kr/pdu/ddodLink.do?id=T14999916 ▼n KERIS
980 ▼a 201812 ▼f 2019
990 ▼a 관리자 ▼b 관리자