LDR | | 00000nmm u2200205 4500 |
001 | | 000000330005 |
005 | | 20241017162314 |
008 | | 181129s2017 ||| | | | eng d |
020 | |
▼a 9780355591248 |
035 | |
▼a (MiAaPQ)AAI10681654 |
035 | |
▼a (MiAaPQ)umaryland:10908 |
040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 248032 |
049 | 1 |
▼f DP |
082 | 0 |
▼a 615 |
100 | 1 |
▼a Czuba, Lindsay Christine. |
245 | 10 |
▼a Molecular Insight into the Structure, Function, and Regulation of Bile Acid Transport. |
260 | |
▼a [S.l.] :
▼b University of Maryland, Baltimore.,
▼c 2017 |
260 | 1 |
▼a Ann Arbor :
▼b ProQuest Dissertations & Theses,
▼c 2017 |
300 | |
▼a 183 p. |
500 | |
▼a Source: Dissertation Abstracts International, Volume: 79-05(E), Section: B. |
500 | |
▼a Adviser: Peter W. Swaan. |
502 | 1 |
▼a Thesis (Ph.D.)--University of Maryland, Baltimore, 2017. |
506 | |
▼a This item is not available from ProQuest Dissertations & Theses. |
520 | |
▼a The human Apical Sodium-dependent Bile Acid Transporter (SLC10A2), also known as hASBT, plays an integral role in the enterohepatic circulation of bile acid and cholesterol homeostasis. As a member of the solute carrier family of membrane transp |
520 | |
▼a Limiting the development of such therapeutics, is an incomplete understanding of hASBT's structure. Extensive biochemical and mutagenesis studies for hASBT support a seven transmembrane model. Yet conflicting structures have emerged with the elu |
520 | |
▼a In this work we provide novel molecular insight into the structure, function, and regulation of human ASBT. We contrasted the biochemical, inhibitory, and evolutionary attributes of nmAsbt, yfAsbt, and hASBT and identified their critical differe |
520 | |
▼a Additionally, we characterized the role of tyrosine phosphorylation in regulating the functional expression and stability of hASBT. We identified Src family kinases as critical modulators and provide support for hASBT's regulation by phosphatase |
520 | |
▼a Finally, we have optimized the biological sample preparation methods and have significantly increased the purity of hASBT samples. When coupled with mass spectrometry analysis, these methods will identify critical proteoforms of hASBT and facili |
590 | |
▼a School code: 0373. |
650 | 4 |
▼a Pharmaceutical sciences. |
690 | |
▼a 0572 |
710 | 20 |
▼a University of Maryland, Baltimore.
▼b Pharmaceutical Sciences. |
773 | 0 |
▼t Dissertation Abstracts International
▼g 79-05B(E). |
773 | |
▼t Dissertation Abstract International |
790 | |
▼a 0373 |
791 | |
▼a Ph.D. |
792 | |
▼a 2017 |
793 | |
▼a English |
856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T14996722
▼n KERIS |
980 | |
▼a 201812
▼f 2019 |
990 | |
▼a 관리자
▼b 관리자 |