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The presence and involvement of calmodulin in two calcium-dependent processes of Paramecium tetraureliaRauh, James Joseph. January 1982 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1982. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
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Functional domains of neuromodulin and the interaction of calmodulin with target peptides /Chapman, Edwin R., January 1992 (has links)
Thesis (Ph. D.)--University of Washington, 1992. / Vita. Includes bibliographical references (leaves [114]-133).
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Rac1b, a variant of rac1, interacts with calmodulinKhanna, Neha 10 April 2014 (has links)
Rac1b, splice isoform of Rac1, is a member of the Rho family of small GTP-binding proteins that has been found to be up-regulated in the cancers of breast, colon and the lung. Rac1b consists of an additional 19 amino acid insertion [VGETYGKDITSRGKDKPIA] close to the switch II domain, a region important for the interaction of Rac1 with various regulators and effectors. This insertion leads to the intracellular predominance of active GTP-bound form of Rac1b and also renders it ineffective to interact with Rho guanine nucleotide dissociation inhibitors (Rho GDI’s).
Previously, a 14 amino acid region [AVKYLECSALTQRG] essential for calmodulin (CaM) binding has been established in Rac1. A similar region also exists in Rac1b. In the present work, we have determined that as for Rac1, Rac1b also interacts with calmodulin in a calcium dependent manner. We have also demonstrated that Rac1b binds to calmodulin directly. However, the putative CaM binding region in the two proteins differ as the commercially synthesized CaM binding peptide for Rac1 failed to compete with Rac1b for binding to calmodulin.
In addition, using the PAK-CRIB domain in pull down assays that interacts with the GTP-bound form of Rac1b, we have established that CaM plays an important role in the activation of Rac1b. Experiments using W7, the inhibitor for CaM, revealed that activation of Rac1b in the presence of W7 is reduced in response to growth factor agonists such as Heregulin β-1 and EGF. However, it was observed that the addition of W7 has no role in in vitro GDP/GTP binding to Rac1b. Molecular modeling and docking studies were also carried out to predict the possible sites in Rac1b that potentially can interact with CaM.
In summary, the results presented here demonstrate that CaM interacts with Rac1b in a calcium dependent manner. Additionally, CaM plays an important role in the activation of Rac1b thus indicating a role for CaM in cancer progression.
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Cloning and characterization of a calmodulin gene in rice, Oryza sativa /Lee, Shuk-man, January 2000 (has links)
Thesis (M. Phil.)--University of Hong Kong, 2000. / Includes bibliographical references (leaves 94-101).
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Cloning and characterization of a calmodulin gene in rice, Oryza sativaLee, Shuk-man, January 2000 (has links)
Thesis (M.Phil.)--University of Hong Kong, 2000. / Includes bibliographical references (leaves 94-101) Also available in print.
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Identification of binding sites for ophiobolin a in the calmodulin molecule區大綱, Au, Tai-kong. January 1997 (has links)
published_or_final_version / Zoology / Doctoral / Doctor of Philosophy
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Cloning and characterization of a calmodulin gene in rice, Oryza sativaLee, Shuk-man, 李淑雯 January 2000 (has links)
published_or_final_version / Zoology / Master / Master of Philosophy
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KINETIC STUDIES OF CALCIUM BINDING TO CALMODULIN.Tudor, Marcia Ann. January 1983 (has links)
No description available.
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The synthesis and evaluation of some anti-infective agentsAllcock, Robert William January 2000 (has links)
No description available.
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Selenoprotein W : purification and characterization of its interaction with calmodulinBauman, Andrew Thomas 26 November 2003 (has links)
Graduation date: 2004
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