| LDR | | 00000nmm u2200205 4500 |
| 001 | | 000000330183 |
| 005 | | 20241025142914 |
| 008 | | 181129s2018 ||| | | | eng d |
| 020 | |
▼a 9780355907193 |
| 035 | |
▼a (MiAaPQ)AAI10748842 |
| 035 | |
▼a (MiAaPQ)duke:14475 |
| 040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 248032 |
| 049 | 1 |
▼f DP |
| 082 | 0 |
▼a 574 |
| 100 | 1 |
▼a Tarbet, Heather Jean. |
| 245 | 10 |
▼a O-GlcNAc-Mediated Protein-Protein Interactions in Cell Signaling. |
| 260 | |
▼a [S.l.] :
▼b Duke University.,
▼c 2018 |
| 260 | 1 |
▼a Ann Arbor :
▼b ProQuest Dissertations & Theses,
▼c 2018 |
| 300 | |
▼a 139 p. |
| 500 | |
▼a Source: Dissertation Abstracts International, Volume: 79-09(E), Section: B. |
| 500 | |
▼a Adviser: Michael S. Boyce. |
| 502 | 1 |
▼a Thesis (Ph.D.)--Duke University, 2018. |
| 506 | |
▼a This item is not available from ProQuest Dissertations & Theses. |
| 520 | |
▼a Protein modification by O-linked beta-N-acetylglucosamine (O-GlcNAc) is an essential signaling mechanism that affects diverse processes such as cell cycle, metabolism, and death. Aberrant signaling has been implicated in numerous human diseases |
| 520 | |
▼a Despite the extensive number of OGT and OGA substrates identified, including IFs, the substrate specificity of both of these enzymes remains an open question due to the lack of consensus sequence among O-GlcNAc modified proteins. A prevailing ge |
| 590 | |
▼a School code: 0066. |
| 650 | 4 |
▼a Biochemistry. |
| 690 | |
▼a 0487 |
| 710 | 20 |
▼a Duke University.
▼b Biochemistry. |
| 773 | 0 |
▼t Dissertation Abstracts International
▼g 79-09B(E). |
| 773 | |
▼t Dissertation Abstract International |
| 790 | |
▼a 0066 |
| 791 | |
▼a Ph.D. |
| 792 | |
▼a 2018 |
| 793 | |
▼a English |
| 856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T14997012
▼n KERIS |
| 980 | |
▼a 201812
▼f 2019 |
| 990 | |
▼a 관리자
▼b 관리자 |