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305 citation(s) found for "Wu, Tiffany".

Electrochemical Studies of the Mono-Fe, Fe−Zn, and Fe−Fe Metalloisoforms of Bacteriophage λ Protein Phosphatase
Reiter, Tiffany A., Rusnak, Frank

Biochemistry | January 20, 2004 | Volume: 43 | Issue: 3 | Pages: 782-790

10.1021/bi0356956 | PMID 14730983 Get It

Mn2+ Is a Native Metal Ion Activator for Bacteriophage λ Protein Phosphatase
Reiter, Tiffany A., Reiter, Nicholas J. , Rusnak, Frank

Biochemistry | December 17, 2002 | Volume: 41 | Issue: 51 | Pages: 15404-15409

10.1021/bi026317o | PMID 12484780 Get It

The dynamins: Redundant or distinct functions for an expanding family of related GTPases?
Henley, John R. , Cook, Tiffany , McNiven, Mark A. , Urrutia, Raúl

Proceedings of the National Academy of Sciences | July 26, 2002 | Volume: 94 | Issue: 2 | Pages: 377-384

10.1073/pnas.94.2.377 | PMID 9012790 Get It

In the 7 years since dynamin was first isolated from bovine brain in search of novel microtubule-based motors, our understanding of this enzyme has expanded significantly. We now know that brain dynamin belongs to a family of large GTPases, which mediate vesicle trafficking. Furthermore, this enzymatic activity is markedly increased through association with microtubules, acidic phospholipids, and certain regulatory proteins that contain Src homology 3 (SH3) domains. From functional, genetic, and cellular manipulations, it is now generally accepted that dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event. These observations have confirmed at least one function of dynamin that was predicted from seminal studies on a pleiotropic mutant, shibire ts ( shi ts ) in Drosophila melanogaster. Of equal interest is the finding that there are multiple dynamin gene products, including two that are expressed in a tissue-specific manner, and they share marked homology with a larger family of distinct but related proteins. Therefore, it is attractive to speculate that the different dynamins may participate in related cellular functions, such as distinct endocytic processes and even secretion. In turn, dynamin could play an important role in cell growth, cell spreading, and neurite outgrowth. The purpose of this review is to enumerate on the expansive dynamin literature and to discuss the nomenclature, expression, and putative functions of this growing and interesting family of proteins.
Characterization of Molecular Defects in Isovaleryl-CoA Dehydrogenase in Patients with Isovaleric Acidemia
Mohsen, Al‐Walid , Anderson, Bambi D., Volchenboum, Samuel L. , Battaile, K.P. , Tiffany, Karen, Kim, Jung‐Ja P. , Vockley, Jerry , Roberts, David D.

Biochemistry | July 26, 2002 | Volume: 37 | Issue: 28 | Pages: 10325-10335

10.1021/bi973096r | PMID 9665741 Get It

Structure of Human Isovaleryl-CoA Dehydrogenase at 2.6 Å Resolution:  Structural Basis for Substrate Specificity,
Tiffany, Karen, Roberts, David L., Paschke, Rosemary, Mohsen, Al‐Walid , Vockley, Jerry , Kim, Jung‐Ja P. , Roberts, David Leland , Wang, Ming

Biochemistry | July 26, 2002 | Volume: 36 | Issue: 28 | Pages: 8455-8464

10.1021/bi970422u | PMID 9214289 Get It