| LDR | | 00000nmm u2200205 4500 |
| 001 | | 000000330795 |
| 005 | | 20241104170354 |
| 008 | | 181129s2018 ||| | | | eng d |
| 020 | |
▼a 9780438125650 |
| 035 | |
▼a (MiAaPQ)AAI10902958 |
| 035 | |
▼a (MiAaPQ)umichrackham:001225 |
| 040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 248032 |
| 049 | 1 |
▼f DP |
| 082 | 0 |
▼a 574 |
| 100 | 1 |
▼a Won, Sang Joon. |
| 245 | 10 |
▼a Structure, Function, and Inhibition of Protein Depalmitoylases. |
| 260 | |
▼a [S.l.] :
▼b University of Michigan.,
▼c 2018 |
| 260 | 1 |
▼a Ann Arbor :
▼b ProQuest Dissertations & Theses,
▼c 2018 |
| 300 | |
▼a 144 p. |
| 500 | |
▼a Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B. |
| 500 | |
▼a Adviser: Brent Randall Martin. |
| 502 | 1 |
▼a Thesis (Ph.D.)--University of Michigan, 2018. |
| 520 | |
▼a Proteins are often regulated through the addition of chemical modifications that modulate localization, activity, and interactions. Protein S-palmitoylation describes the attachment of long-chain fatty acids to cysteine residues in proteins to p |
| 590 | |
▼a School code: 0127. |
| 650 | 4 |
▼a Biochemistry. |
| 690 | |
▼a 0487 |
| 710 | 20 |
▼a University of Michigan.
▼b Chemical Biology. |
| 773 | 0 |
▼t Dissertation Abstracts International
▼g 79-12B(E). |
| 773 | |
▼t Dissertation Abstract International |
| 790 | |
▼a 0127 |
| 791 | |
▼a Ph.D. |
| 792 | |
▼a 2018 |
| 793 | |
▼a English |
| 856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T15000467
▼n KERIS |
| 980 | |
▼a 201812
▼f 2019 |
| 990 | |
▼a 관리자
▼b 관리자 |