Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Victor F, Waingeh"'
Publikováno v:
Chemical Papers. 75:1937-1948
Experimental studies have shown that many glycolytic enzymes bind cytoskeletal proteins reversibly including lactate dehydrogenase (LDH) and that the interaction may be electrostatic in nature. LDH is particularly interesting because different isofor
Publikováno v:
Open Journal of Physical Chemistry. :122-131
The conformations of four β-amino acids in a model peptide environment were investigated using Hartree-Fock (HF) and density functional theory (DFT) methods in gas phase and with solvation. Initial structures were obtained by varying dihedral angles
Publikováno v:
Open Journal of Biophysics. :285-290
Development of new antimalarial drugs continues to be of great importance due to the resistance of the malaria parasite to currently used drugs. Glycolytic enzymes have emerged as potential targets for the development of new drugs due to the reliance
Autor:
Victor F. Waingeh, Kristine L. Carlson, Elizabeth Spanbauer Schmidt, Eric N. Njabon, Kathryn A. Thomasson, Neville Y. Forlemu
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:2813-2827
The association of glycolytic enzymes with F-actin is proposed to be one mechanism by which these enzymes are compartmentalized, and, as a result, may possibly play important roles for: regulation of the glycolytic pathway, potential substrate channe
Publikováno v:
Biopolymers. 73:533-541
Brownian dynamics simulations of computer models of GAPDH mutants interacting with F-actin emphasized the electrostatic nature of such interactions, and confirmed the importance of four previously identified lysine residues on the GAPDH structure in
Publikováno v:
Biopolymers. 70:456-470
Previous Brownian dynamics (BD) simulations identified specific basic residues on fructose-1,6-bisphophate aldolase (aldolase) (I. V. Ouporov et al., Biophysical Journal, 1999, Vol. 76, pp. 17–27) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH
Publikováno v:
Journal of Molecular Recognition. 15:423-431
Previous Brownian dynamics (BD) simulations (Ouporov IG, Knull HR and Thomasson KA 1999. Biophys. J. 76: 17-27) of complex formation between rabbit aldolase and F-actin have identified three lysine residues (K288, K293 and K341) on aldolase and acidi
Autor:
Neville Y, Forlemu, Eric N, Njabon, Kristine L, Carlson, Elizabeth S, Schmidt, Victor F, Waingeh, Kathryn A, Thomasson
Publikováno v:
Proteins. 79(10)
The association of glycolytic enzymes with F-actin is proposed to be one mechanism by which these enzymes are compartmentalized, and, as a result, may possibly play important roles for: regulation of the glycolytic pathway, potential substrate channe
Autor:
Neville Y. Forlemu, Stephen L. Lowe, Igor V. Ouporov, Kathryn A. Thomasson, Victor F. Waingeh
Publikováno v:
Biopolymers. 85(1)
Interactions of the glycolytic enzyme, fructose-1,6-bisphosphate aldolase (aldolase), with F-actin may be one mechanism for the colocalization of glycolytic enzymes. Examination of these interactions in different animal species tests this hypothesis
Autor:
Carol D. Gustafson, Evguenii I. Kozliak, Kathryn A. Thomasson, Victor F. Waingeh, Harvey R. Knull, Stephen L. Lowe
Publikováno v:
Biophysical journal. 90(4)
Interaction of glycolytic enzymes with F-actin is suggested to be a mechanism for compartmentation of the glycolytic pathway. Earlier work demonstrates that muscle F-actin strongly binds glycolytic enzymes, allowing for the general conclusion that