Year |
Citation |
Score |
2016 |
Ptak CP, Ahmed AH, Oswald RE. NMR approaches to functional dynamics of genetically separated iglur domains Neuromethods. 106: 101-118. DOI: 10.1007/978-1-4939-2812-5_8 |
0.36 |
|
2014 |
Ptak CP, Hsieh CL, Lin YP, Maltsev AS, Raman R, Sharma Y, Oswald RE, Chang YF. NMR solution structure of the terminal immunoglobulin-like domain from the leptospira host-interacting outer membrane protein, LigB. Biochemistry. 53: 5249-60. PMID 25068811 DOI: 10.1021/bi500669u |
0.36 |
|
2014 |
Ptak CP, Hsieh CL, Weiland GA, Oswald RE. Role of stoichiometry in the dimer-stabilizing effect of AMPA receptor allosteric modulators. Acs Chemical Biology. 9: 128-33. PMID 24152170 DOI: 10.1021/cb4007166 |
0.36 |
|
2013 |
Ahmed AH, Ptak CP, Fenwick MK, Hsieh CL, Weiland GA, Oswald RE. Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange. The Journal of Biological Chemistry. 288: 27658-66. PMID 23940029 DOI: 10.1074/jbc.M113.495564 |
0.36 |
|
2013 |
Raman R, Ptak CP, Hsieh CL, Oswald RE, Chang YF, Sharma Y. The perturbation of tryptophan fluorescence by phenylalanine to alanine mutations identifies the hydrophobic core in a subset of bacterial Ig-like domains. Biochemistry. 52: 4589-91. PMID 23800025 DOI: 10.1021/bi400128r |
0.36 |
|
2010 |
Ahmed AH, Ptak CP, Oswald RE. Molecular mechanism of flop selectivity and subsite recognition for an AMPA receptor allosteric modulator: structures of GluA2 and GluA3 in complexes with PEPA. Biochemistry. 49: 2843-50. PMID 20199107 DOI: 10.1021/bi1000678 |
0.36 |
|
2009 |
Ptak CP, Ahmed AH, Oswald RE. Probing the allosteric modulator binding site of GluR2 with thiazide derivatives. Biochemistry. 48: 8594-602. PMID 19673491 DOI: 10.1021/bi901127s |
0.36 |
|
2005 |
Ptak CP, Cuello LG, Perozo E. Electrostatic interaction of a K+ channel RCK domain with charged membrane surfaces. Biochemistry. 44: 62-71. PMID 15628846 DOI: 10.1021/bi048390f |
0.36 |
|
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