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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
81

Identification of mutants in genes encoding arabidopsis acyl-coenzyme A binding proteins ACBP3, ACBP4 and ACBP5

Chan, Suk-wah, 陳淑華 January 2004 (has links)
published_or_final_version / abstract / Botany / Master / Master of Philosophy
82

Association of DC-SIGN (CD209) gene polymorphisms with severe acute respiratory syndrome (SARS)

Xu, Meishu., 徐美術. January 2007 (has links)
published_or_final_version / abstract / Pathology / Master / Master of Philosophy
83

Investigating the mechanisms of auxin transport

Parry, Geraint January 2002 (has links)
No description available.
84

Inhibitory role of Smad7 in hepatocarcinogenesis in mice and in vitro. / CUHK electronic theses & dissertations collection

January 2013 (has links)
Wang, Jia. / Thesis (Ph.D.)--Chinese University of Hong Kong, 2013. / Includes bibliographical references (leaves 99-115). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Abstract also in Chinese.
85

CopB from Archaeoglobus fulgidus: a thermophilic Cu2+ transporting CPx-ATPase

Mana Capelli, Sebastian C. 28 April 2003 (has links)
In this work we present the first characterization of a Cu2+-transporting ATPase. The thermophilic bacteria Archaeoglobus fulgidus contains two genes, CopA and CopB, encoding for CPx-ATPases. CopB belongs to the subgroup IB-4 of the CPX-ATPases. These enzymes are characterized by a CPH motif in the 6th transmembrane domain and a His-rich N-terminus metal binding domain (MBD). CopB was heterologously expressed in E. coli. Membranes were prepared and used to measure activity. CopB was active at high temperature (75º C), high ionic strength and pH 5.7. The enzyme was activated by Cu2+, and in to a lesser extent by Ag+ and Cu+. CopB showed a Vmax = 5 µmol/mg/h and a high apparent affinity (K1/2 = 0.28 ± 0.09 μM) for Cu2+. Uptake of 64Cu2+ into everted vesicles was also measured in order to show that Cu2+ is not only activating the enzyme but being transported. Compared with CopB-WT, CopB-T (lacking the N-terminus MBD) did not show any difference in its activation by the different metal ions, demonstrating that the cytoplasmic MBD has no role in the metal selectivity. CopB-T also showed a 40 % decrease in the ATPase activity. CopB-WT and CopB-T presented similar levels of phosphorylation. However, CopB-T exhibited a reduced rate of dephosphorylation (slower transition from the E2P to the E2 conformation). These observations suggest a regulatory role for the cytoplasmic MBD.
86

Association of DC-SIGN (CD209) gene polymorphisms with severe acute respiratory syndrome (SARS) /

Xu, Meishu. January 2007 (has links)
Thesis (M. Phil.)--University of Hong Kong, 2007. / Also available online.
87

Roles of human double-stranded RNA binding proteins TRBP and PACT in RNA interference

Kok, Kin-hang. January 2006 (has links)
Thesis (Ph. D.)--University of Hong Kong, 2007. / Title proper from title frame. Also available in printed format.
88

Association of DC-SIGN (CD209) gene polymorphisms with severe acute respiratory syndrome (SARS)

Xu, Meishu. January 2007 (has links)
Thesis (M. Phil.)--University of Hong Kong, 2007. / Title proper from title frame. Also available in printed format.
89

Osmotic response element binding protein (OREBP) is an essential regulator of urine concentrating mechanism and renal protection

Lam, Ka-man, Amy. January 2004 (has links)
Thesis (Ph. D.)--University of Hong Kong, 2005. / Title proper from title frame. Also available in printed format.
90

Nde1-mediated inhibition of ciliogenesis controls cell cycle re-entry

Kim, Sehyun. January 2009 (has links) (PDF)
Thesis (Ph. D.)--University of Oklahoma. / Bibliography: leaves 118-130.

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