Authors:
BRADRICK TD
GALDZICKI Z
JONES C
EHRENSTEIN G
Citation: Td. Bradrick et al., CHOLINE LEAKAGE FROM SYNAPTOSOMES PREPARED FROM POSTMORTEM BRAINS OF ALZHEIMERS-DISEASE PATIENTS, Biophysical journal, 74(2), 1998, pp. 91-91
Citation: H. Park et al., A GLUTAMINE 67-]HISTIDINE MUTATION IN HOMOTETRAMERIC R67 DIHYDROFOLATE-REDUCTASE RESULTS IN 4 MUTATIONS PER SINGLE ACTIVE-SITE PORE AND CAUSES SUBSTANTIAL SUBSTRATE AND COFACTOR INHIBITION, Protein engineering, 10(12), 1997, pp. 1415-1424
Authors:
BRADRICK TD
SHATTUCK C
STRADER MB
WICKER C
EISENSTEIN E
HOWELL EE
Citation: Td. Bradrick et al., REDESIGNING THE QUATERNARY STRUCTURE OF R67 DIHYDROFOLATE-REDUCTASE -CREATION OF AN ACTIVE MONOMER FROM A TETRAMERIC PROTEIN BY QUADRUPLICATION OF THE GENE, The Journal of biological chemistry, 271(45), 1996, pp. 28031-28037
Authors:
GEORGHIOU S
BRADRICK TD
PHILIPPETIS A
BEECHEM JM
Citation: S. Georghiou et al., LARGE-AMPLITUDE PICOSECOND ANISOTROPY DECAY OF THE INTRINSIC FLUORESCENCE OF DOUBLE-STRANDED DNA, Biophysical journal, 70(4), 1996, pp. 1909-1922
Citation: Td. Bradrick et al., STOPPED-FLOW FLUOROMETRIC STUDY OF THE INTERACTION OF MELITTIN WITH PHOSPHOLIPID-BILAYERS - IMPORTANCE OF THE PHYSICAL STATE OF THE BILAYERAND THE ACYL-CHAIN LENGTH, Biophysical journal, 70(2), 1996, p.
Citation: Td. Bradrick et al., UNUSUAL BINDING STOICHIOMETRIES AND COOPERATIVITY ARE OBSERVED DURINGBINARY AND TERNARY COMPLEX-FORMATION IN THE SINGLE ACTIVE PORE OF R67DIHYDROFOLATE-REDUCTASE, A D-2 SYMMETRICAL PROTEIN, Biochemistry, 35(35), 1996, pp. 11414-11424
Citation: Td. Bradrick et al., STOPPED-FLOW FLUOROMETRIC STUDY OF THE INTERACTION OF MELITTIN WITH PHOSPHOLIPID-BILAYERS - IMPORTANCE OF THE PHYSICAL STATE OF THE BILAYERAND THE ACYL-CHAIN LENGTH, Biophysical journal, 69(5), 1995, pp. 1999-2010
Authors:
GEORGHIOU S
BEECHEM JM
BRADRICK TD
PHILIPPETIS A
Citation: S. Georghiou et al., CONFORMATIONAL FLEXIBILITY OF NUCLEIC-ACIDS - A PICOSECOND ANISOTROPYSTUDY USING INTRINSIC FLUORESCENCE, Biophysical journal, 66(2), 1994, pp. 10000025-10000025