| Year |
Citation |
Score |
| 2015 |
Deng G, Shen J, Yin M, McManus J, Mathieu M, Gee P, He T, Shi C, Bedel O, McLean LR, Le-Strat F, Zhang Y, Marquette JP, Gao Q, Zhang B, ... ... Licht S, et al. Selective inhibition of mutant isocitrate dehydrogenase 1 (IDH1) via disruption of a metal binding network by an allosteric small molecule. The Journal of Biological Chemistry. 290: 762-74. PMID 25391653 DOI: 10.1074/Jbc.M114.608497 |
0.329 |
|
| 2014 |
Lin WC, Licht S. Poly(ethylene glycol) as a scaffold for high-affinity open-channel blockers of the mouse nicotinic acetylcholine receptor. Plos One. 9: e112088. PMID 25386750 DOI: 10.1371/Journal.Pone.0112088 |
0.401 |
|
| 2014 |
Deng G, Licht S, Shen J, Yin M, McManus J, Gee P, He T, Gao G, Zhang B, Mathieu M, Rak A, Bedel O, Shi C, Gross S, Hoffmann D, et al. Abstract 4746: Selective inhibition of mutant IDH1 via small molecule binding to the dimer interface Cancer Research. 74: 4746-4746. DOI: 10.1158/1538-7445.Am2014-4746 |
0.318 |
|
| 2012 |
Choi KH, Licht S. ATP-sensitive potassium channels exhibit variance in the number of open channels below the limit predicted for identical and independent gating. Plos One. 7: e37399. PMID 22666353 DOI: 10.1371/Journal.Pone.0037399 |
0.363 |
|
| 2009 |
Tantama M, Licht S. Functional equivalence of the nicotinic acetylcholine receptor transmitter binding sites in the open state. Biochimica Et Biophysica Acta. 1788: 936-44. PMID 19366595 DOI: 10.1016/J.Bbamem.2009.01.009 |
0.707 |
|
| 2008 |
Farbman ME, Gershenson A, Licht S. Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA. Biochemistry. 47: 13497-505. PMID 19053261 DOI: 10.1021/Bi801140Y |
0.365 |
|
| 2008 |
Tantama M, Licht S. Use of calculated cation-pi binding energies to predict relative strengths of nicotinic acetylcholine receptor agonists. Acs Chemical Biology. 3: 693-702. PMID 19032090 DOI: 10.1021/Cb800189Y |
0.702 |
|
| 2008 |
Tantama M, Lin WC, Licht S. An activity-based protein profiling probe for the nicotinic acetylcholine receptor. Journal of the American Chemical Society. 130: 15766-7. PMID 18975901 DOI: 10.1021/Ja805868X |
0.711 |
|
| 2008 |
Jennings LD, Lun DS, Médard M, Licht S. ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis. Biochemistry. 47: 11536-46. PMID 18839965 DOI: 10.1021/Bi801101P |
0.307 |
|
| 2008 |
Jennings LD, Bohon J, Chance MR, Licht S. The ClpP N-terminus coordinates substrate access with protease active site reactivity. Biochemistry. 47: 11031-40. PMID 18816064 DOI: 10.1021/Bi8010169 |
0.334 |
|
| 2008 |
Lin WC, Licht S. Polymer-based open-channel blockers for the acetylcholine receptor: the effect of spacer length on blockade kinetics. Biochemistry. 47: 9163-73. PMID 18690702 DOI: 10.1021/Bi800737J |
0.389 |
|
| 2008 |
Choi KH, Tantama M, Licht S. Testing for violations of microscopic reversibility in ATP-sensitive potassium channel gating. The Journal of Physical Chemistry. B. 112: 10314-21. PMID 18661924 DOI: 10.1021/Jp712088V |
0.68 |
|
| 2008 |
Licht S, Lee I. Resolving individual steps in the operation of ATP-dependent proteolytic molecular machines: from conformational changes to substrate translocation and processivity. Biochemistry. 47: 3595-605. PMID 18311925 DOI: 10.1021/Bi800025G |
0.358 |
|
| 2005 |
Mitra A, Tascione R, Auerbach A, Licht S. Plasticity of acetylcholine receptor gating motions via rate-energy relationships. Biophysical Journal. 89: 3071-8. PMID 16113115 DOI: 10.1529/Biophysj.105.068783 |
0.649 |
|
| 2003 |
Licht SS, Sonnleitner A, Weiss S, Schultz PG. A rugged energy landscape mechanism for trapping of transmembrane receptors during endocytosis. Biochemistry. 42: 2916-25. PMID 12627957 DOI: 10.1021/Bi026059V |
0.466 |
|
| 1999 |
Licht SS, Lawrence CC, Stubbe J. Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: the importance of entropy in catalysis. Biochemistry. 38: 1234-42. PMID 9930983 DOI: 10.1021/Bi981886A |
0.536 |
|
| 1999 |
Licht SS, Booker S, Stubbe J. Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation. Biochemistry. 38: 1221-33. PMID 9930982 DOI: 10.1021/Bi981885I |
0.646 |
|
| 1999 |
Licht SS, Lawrence CC, Stubbe J. Class II ribonucleotide reductases catalyze carbon-cobalt bond reformation on every turnover Journal of the American Chemical Society. 121: X. DOI: 10.1021/Ja9913840 |
0.539 |
|
| 1996 |
Licht S, Gerfen GJ, Stubbe J. Thiyl radicals in ribonucleotide reductases. Science (New York, N.Y.). 271: 477-81. PMID 8560260 DOI: 10.1126/Science.271.5248.477 |
0.513 |
|
| 1996 |
Gerfen GJ, Licht S, Willems JP, Hoffman BM, Stubbe J. Electron paramagnetic resonance investigations of a kinetically competent intermediate formed in ribonucleotide reduction: Evidence for a thiyl radical-cob(II)alamin interaction Journal of the American Chemical Society. 118: 8192-8197. DOI: 10.1021/Ja960363S |
0.48 |
|
| 1994 |
Booker S, Licht S, Broderick J, Stubbe J. Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cysteine residues in ribonucleotide reduction. Biochemistry. 33: 12676-85. PMID 7918494 DOI: 10.1021/Bi00208A019 |
0.69 |
|
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