Comparative Analyses of the Three-dimensional Structures and Enzymatic Properties of α, β, γ, and δ Isoforms of Ca2+-Calmodulin-dependent Protein Kinase II*
- T. Gaertner, S. Kolodziej, M. Waxham
- Biology, ChemistryJournal of Biological Chemistry
- 26 March 2004
Simulations utilizing this data revealed that the measured differences in CaM binding affinities play a minor role in the autophosphorylation of the enzyme, which is largely dictated by the rate of autoph phosphorylation for each isoform.
Three-dimensional Reconstructions of Calcium/Calmodulin-dependent (CaM) Kinase IIα and Truncated CaM Kinase IIα Reveal a Unique Organization for Its Structural Core and Functional Domains*
- S. Kolodziej, A. Hudmon, M. Waxham, J. K. Stoops
- ChemistryJournal of Biological Chemistry
- 12 May 2000
The clustering of the functional domains provides a favorable arrangement for the autophosphorylation reaction, and the unusual arrangement of the catalytic domain on extended tethers appears to be significant for the remarkable functional diversity of CaM KIIα in cellular regulation.
Comparative analyses of the three-dimensional structures and enzymatic properties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-dependent protein kinase II.
- T. Gaertner, S. Kolodziej, M. Waxham
- BiologyJournal of Biological Chemistry
- 2004
Enzymatic analyses showed that the isoforms were similar in their K(m) for ATP and the peptide substrate syntide, but showed significant differences in their interactions with Ca(2+)-calmodulin as assessed by binding, substrate phosphorylation, and autophosphorylation.
βCaMKII Regulates Actin Assembly and Structure*
- H. Sanabria, M. Swulius, S. Kolodziej, Jun Liu, M. Waxham
- Biology, ChemistryJournal of Biological Chemistry
- 10 April 2009
βCaMKII has a dual functional role; it can sequester monomeric actin to reduce actin polymerization and can also bundle actin filaments, which would impact both the dynamics of actin filament assembly and enhance the rigidity of the filaments once formed, significantly impacting the structure of synapses.
On the Unique Structural Organization of the Saccharomyces cerevisiae Pyruvate Dehydrogenase Complex*
- J. K. Stoops, R. Cheng, L. Reed
- Chemistry, BiologyJournal of Biological Chemistry
- 28 February 1997
Investigation of the structures of the truncated 60-mer core dihydrolipoamide acetyltransferase of the Saccharomyces cerevisiae pyruvate dehydrogenase complex shows that the 12 large openings in the tE2 core permit the entrance of tBP, BP, and BP·;E3 into a large central cavity where the BP component apparently binds near the tip of the t E2 trimer.
The endosome-associated protein Hrs is hexameric and controls cargo sorting as a "master molecule".
- L. Pullan, S. Mullapudi, P. Penczek
- ChemistryStructure
- 1 April 2006
Utility of Butvar support film and methylamine tungstate stain in three-dimensional electron microscopy: agreement between stain and frozen-hydrated reconstructions.
- S. Kolodziej, P. Penczek, J. K. Stoops
- BiologyJournal of Structural Biology
- 1 November 1997
The agreement between the stain and frozen-hydrated reconstructions affords convincing evidence concerning the validity of the structure and the information afforded by the two reconstructions significantly enhances the structural analysis of the molecule.
Three-dimensional structure of the truncated core of the Saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images.
- J. K. Stoops, T. Baker, J. P. Schroeter, S. Kolodziej, X. Niu, L. Reed
- Biology, ChemistryJournal of Biological Chemistry
- 5 December 1992
Structure-Function Relationships of the Saccharomyces cerevisiae Fatty Acid Synthase
- S. Kolodziej, Pawel A. Penczek, J. P. Schroeter, James K. Stoops
- ChemistryJournal of Biological Chemistry
- 8 November 1996
The three-dimensional structure of the Saccharomyces cerevisie fatty acid synthase was computed from electron microscopy of stain images and it is proposed that these six cavities constitute the six equivalent sites of fatty acids synthesis resulting in an extraordinary structure-function relationship with the 42 catalytic sites involved in fatty acid synthesis inside the molecule.
Specific Amyloid β Clearance by a Catalytic Antibody Construct*
- S. Planque, Y. Nishiyama, S. Paul
- BiologyJournal of Biological Chemistry
- 27 February 2015
The specificity and amyloid β (Aβ)-clearing effect of a catabody construct engineered from innate immunity principles is described, which appears to be an innate immune function that could be applied for therapeutic Aβ removal.
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