Zobrazeno 1 - 10
of 146
pro vyhledávání: '"Franklyn G. Prendergast"'
Publikováno v:
The Journal of Physiology. 592:2381-2388
Ideas about personalized medicine are underpinned in part by evolutionary biology's Modern Synthesis. In this essay we link personalized medicine to the efforts of the early statistical investigators who quantified the heritability of human phenotype
Autor:
Franklyn G. Prendergast, William Kirk, Elena Atanasova, Janet Yao, William S. Wessels, Thomas Wesley Allen
Publikováno v:
Journal of fluorescence. 27(3)
A novel version of the well-known and commercially successful Green Fluorescent Protein (GFP) variant known as EGFP, with an introduced E222H mutation, was produced in this laboratory. Given the current state of hypotheses about the role of glutamate
Autor:
Allan Hallquist, Carl Rogaston Willis, Michael R. Chernick, Linda D. Bosserman, Franklyn G Prendergast, James Rutledge, Mathieu Perree, Howard D. Homesley, Martin Fleisher, Dirk C. Davidson, Matthew Burrell, Roy S. Herbst, Audrey Garrett, Manuel Penalver, Swapnil Rajurkar, Misagh Karimi, Steven Strickland, Emery M. Salom, Karl Rogers, Cary A. Presant, Anastasios Raptis
Publikováno v:
Cancer Research. 72:3901-3905
A drug-induced apoptosis assay, termed the microculture-kinetic (MiCK) assay, has been developed. Blinded clinical trials have shown higher response rates and longer survival in groups of patients with acute myelocytic leukemia and epithelial ovarian
Autor:
Gwen Lomberk, Angela Mathison, Adrienne Grzenda, Jin-San Zhang, Thomas Wesley Allen, Ezequiel Calvo, Navtej S. Buttar, Juan L. Iovanna, Ye Zheng, Franklyn G. Prendergast, Gaurang S. Daftary, Raul Urrutia, Daniel D. Billadeau, R. Gada
Publikováno v:
The Journal of Biological Chemistry
Background: KLF16 is the least characterized family member of recently described metabolic regulators. Results: We extensively characterize mechanisms of DNA binding and chromatin coupling used by KLF16 to regulate metabolic gene expression. Conclusi
Autor:
Lucy Malinina, Franklyn G. Prendergast, Julian G. Molotkovsky, Dinshaw J. Patel, Ravi Kanth Kamlekar, Yong-Guang Gao, Rhoderick E. Brown, Dhirendra K. Simanshu, Sergei Yu Venyaminov, Roopa Kenoth
Publikováno v:
Biochemistry. 50:5163-5171
Characterization of protein stability and folding intermediates can provide insights into normal folding mechanisms as well as pathological conditions involving protein aggregation (e.g. Alzheimer’s disease). A partially unfolded state of special i
Autor:
Yong-Guang Gao, Rhoderick E. Brown, Roopa Kenoth, Franklyn G. Prendergast, Dinshaw J. Patel, Julian G. Molotkovsky, Ravi Kanth Kamlekar, William S. Wessels, Sergei Yu Venyaminov, Lucy Malinina
Publikováno v:
Biophysical Journal. 99(8):2626-2635
Human glycolipid transfer protein (GLTP) serves as the GLTP-fold prototype, a novel, to our knowledge, peripheral amphitropic fold and structurally unique lipid binding motif that defines the GLTP superfamily. Despite conservation of all three intrin
Publikováno v:
Microscopy Today. 18:8-13
Scanning electron microscopy (SEM) can produce striking three-dimensional images of biological cells and tissues with submicron resolution of surface morphology. Such cell surfaces are often complex blends of folds, extrusions, and pockets that may b
Autor:
Dinshaw J. Patel, Rhoderick E. Brown, H. Robert Bergen, Linda M. Benson, Roopa Kenoth, Helen M. Pike, Franklyn G. Prendergast, Lucy Malinina, Dhirendra K. Simanshu, Julian G. Molotkovsky, Sergei Yu Venyaminov, Ravi Kanth Kamlekar
Publikováno v:
Journal of Biological Chemistry. 285:13066-13078
HET-C2 is a fungal protein that transfers glycosphingolipids between membranes and has limited sequence homology with human glycolipid transfer protein (GLTP). The human GLTP fold is unique among lipid binding/transfer proteins, defining the GLTP sup
Autor:
Elena Atanasova, Nenad Juranić, Franklyn G. Prendergast, Emanuel E. Strehler, Adelaida G. Filoteo, John T. Penniston, Slobodan Macura
Publikováno v:
Journal of Biological Chemistry. 285:4015-4024
Using solution NMR spectroscopy, we obtained the structure of Ca(2+)-calmodulin (holoCaM) in complex with peptide C28 from the binding domain of the plasma membrane Ca(2+)-ATPase (PMCA) pump isoform 4b. This provides the first atomic resolution insig
Publikováno v:
Journal of Inorganic Biochemistry. 103:1415-1418
Molecular tuning to calcium-binding in the EF-hand motif of holo-calmodulin was studied in solution by NMR h3JNC′ H-bond couplings. In the N-terminus lobe of holo-calmodulin, the glutamate crucial for Ca2+ coordination has network of H-bonds weaker