| Year |
Citation |
Score |
| 2023 |
Wong NR, Sundar R, Kazanis S, Biswas J, Pochapsky TC. Conformational heterogeneity suggests multiple substrate binding modes in CYP106A2. Journal of Inorganic Biochemistry. 241: 112129. PMID 36731370 DOI: 10.1016/j.jinorgbio.2023.112129 |
0.813 |
|
| 2020 |
Pochapsky TC. A dynamic understanding of cytochrome P450 structure and function through solution NMR. Current Opinion in Biotechnology. 69: 35-42. PMID 33360373 DOI: 10.1016/j.copbio.2020.11.007 |
0.34 |
|
| 2019 |
Pochapsky TC, Pochapsky SS. What Your Crystal Structure Will Not Tell You about Enzyme Function. Accounts of Chemical Research. PMID 31034199 DOI: 10.1021/Acs.Accounts.9B00066 |
0.481 |
|
| 2018 |
Wong NR, Liu X, Lloyd H, Colthart AM, Ferrazzoli AE, Cooper DL, Zhuang Y, Esquea P, Futcher J, Pochapsky TM, Matthews JM, Pochapsky TC. A new approach to understanding structure-function relationships in cytochromes P450 by targeting terpene metabolism in the wild. Journal of Inorganic Biochemistry. 188: 96-101. PMID 30170307 DOI: 10.1016/J.Jinorgbio.2018.08.006 |
0.782 |
|
| 2018 |
Asciutto EK, Pochapsky TC. Some Surprising Implications of NMR-directed Simulations of Substrate Recognition and Binding by Cytochrome P450 (CYP101A1). Journal of Molecular Biology. 430: 1295-1310. PMID 29596916 DOI: 10.1016/J.Jmb.2018.03.014 |
0.451 |
|
| 2017 |
Tietz DR, Colthart AM, Sondej Pochapsky S, Pochapsky TC. Substrate recognition by two different P450s: Evidence for conserved roles in a common fold. Scientific Reports. 7: 13581. PMID 29051575 DOI: 10.1038/S41598-017-14011-W |
0.787 |
|
| 2017 |
Deshpande AR, Pochapsky TC, Ringe D. The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase. Chemical Reviews. PMID 28731690 DOI: 10.1021/Acs.Chemrev.7B00117 |
0.373 |
|
| 2017 |
Tietz DR, Podust LM, Sherman DH, Pochapsky TC. Solution conformations and dynamics of substrate-bound cytochrome P450 MycG. Biochemistry. PMID 28488849 DOI: 10.1021/Acs.Biochem.7B00291 |
0.805 |
|
| 2017 |
Pochapsky TC, Wong N, Zhuang Y, Futcher J, Pandelia ME, Teitz DR, Colthart AM. NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450. Biochimica Et Biophysica Acta. PMID 28473297 DOI: 10.1016/J.Bbapap.2017.04.003 |
0.779 |
|
| 2017 |
Deshpande AR, Pochapsky TC, Petsko GA, Ringe D. Dual chemistry catalyzed by human acireductone dioxygenase. Protein Engineering, Design & Selection : Peds. PMID 28062648 DOI: 10.1093/Protein/Gzw078 |
0.375 |
|
| 2016 |
Colthart AM, Tietz DR, Ni Y, Friedman JL, Dang M, Pochapsky TC. Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance. Scientific Reports. 6: 22035. PMID 26911901 DOI: 10.1038/Srep22035 |
0.8 |
|
| 2016 |
Deshpande AR, Wagenpfeil K, Pochapsky TC, Petsko GA, Ringe D. Metal-dependent function of a mammalian acireductone dioxygenase. Biochemistry. PMID 26858196 DOI: 10.1021/Acs.Biochem.5B01319 |
0.392 |
|
| 2015 |
Zhang Y, Zhou N, Shi J, Pochapsky SS, Pochapsky TC, Zhang B, Zhang X, Xu B. Unfolding a molecular trefoil derived from a zwitterionic metallopeptide to form self-assembled nanostructures. Nature Communications. 6: 6165. PMID 25695392 DOI: 10.1038/Ncomms7165 |
0.315 |
|
| 2014 |
Pochapsky TC. Examining how enzymes self-organize in a membrane. Proceedings of the National Academy of Sciences of the United States of America. 111: 3659-60. PMID 24567406 DOI: 10.1073/Pnas.1401325111 |
0.352 |
|
| 2013 |
Gurry T, Ullman O, Fisher CK, Perovic I, Pochapsky T, Stultz CM. The dynamic structure of α-synuclein multimers Journal of the American Chemical Society. 135: 3865-3872. PMID 23398399 DOI: 10.1021/Ja310518P |
0.73 |
|
| 2012 |
Li S, Tietz DR, Rutaganira FU, Kells PM, Anzai Y, Kato F, Pochapsky TC, Sherman DH, Podust LM. Substrate recognition by the multifunctional cytochrome P450 MycG in mycinamicin hydroxylation and epoxidation reactions. The Journal of Biological Chemistry. 287: 37880-90. PMID 22952225 DOI: 10.1074/Jbc.M112.410340 |
0.812 |
|
| 2012 |
Asciutto EK, Young MJ, Madura J, Pochapsky SS, Pochapsky TC. Solution structural ensembles of substrate-free cytochrome P450(cam). Biochemistry. 51: 3383-93. PMID 22468842 DOI: 10.1021/Bi300007R |
0.476 |
|
| 2011 |
Wang W, Perovic I, Chittuluru J, Kaganovich A, Nguyen LT, Liao J, Auclair JR, Johnson D, Landeru A, Simorellis AK, Ju S, Cookson MR, Asturias FJ, Agar JN, Webb BN, ... ... Pochapsky TC, et al. A soluble α-synuclein construct forms a dynamic tetramer. Proceedings of the National Academy of Sciences of the United States of America. 108: 17797-802. PMID 22006323 DOI: 10.1073/Pnas.1113260108 |
0.753 |
|
| 2011 |
Friedman EJ, Wang HX, Jiang K, Perovic I, Deshpande A, Pochapsky TC, Temple BR, Hicks SN, Harden TK, Jones AM. Acireductone dioxygenase 1 (ARD1) is an effector of the heterotrimeric G protein beta subunit in Arabidopsis. The Journal of Biological Chemistry. 286: 30107-18. PMID 21712381 DOI: 10.1074/Jbc.M111.227256 |
0.72 |
|
| 2011 |
Asciutto EK, Dang M, Pochapsky SS, Madura JD, Pochapsky TC. Experimentally restrained molecular dynamics simulations for characterizing the open states of cytochrome P450cam. Biochemistry. 50: 1664-71. PMID 21265500 DOI: 10.1021/Bi101820D |
0.625 |
|
| 2011 |
Dang M, Pochapsky SS, Pochapsky TC. Spring-loading the active site of cytochrome P450cam. Metallomics : Integrated Biometal Science. 3: 339-43. PMID 21186391 DOI: 10.1039/C0Mt00065E |
0.621 |
|
| 2011 |
Pochapsky T, Perovic I. human alpha synuclein construct Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17665 |
0.671 |
|
| 2010 |
Herbst RW, Perovic I, Martin-Diaconescu V, O'Brien K, Chivers PT, Pochapsky SS, Pochapsky TC, Maroney MJ. Communication between the zinc and nickel sites in dimeric HypA: metal recognition and pH sensing. Journal of the American Chemical Society. 132: 10338-51. PMID 20662514 DOI: 10.1021/Ja1005724 |
0.747 |
|
| 2010 |
Pochapsky TC, Kazanis S, Dang M. Conformational plasticity and structure/function relationships in cytochromes P450. Antioxidants & Redox Signaling. 13: 1273-96. PMID 20446763 DOI: 10.1089/Ars.2010.3109 |
0.819 |
|
| 2009 |
Pochapsky SS, Dang M, OuYang B, Simorellis AK, Pochapsky TC. Redox-dependent dynamics in cytochrome P450cam. Biochemistry. 48: 4254-61. PMID 19366254 DOI: 10.1021/Bi900002K |
0.736 |
|
| 2009 |
Asciutto EK, Madura JD, Pochapsky SS, OuYang B, Pochapsky TC. Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam. Journal of Molecular Biology. 388: 801-14. PMID 19327368 DOI: 10.1016/J.Jmb.2009.03.046 |
0.61 |
|
| 2008 |
Zhang W, Pochapsky SS, Pochapsky TC, Jain NU. Solution NMR structure of putidaredoxin-cytochrome P450cam complex via a combined residual dipolar coupling-spin labeling approach suggests a role for Trp106 of putidaredoxin in complex formation. Journal of Molecular Biology. 384: 349-63. PMID 18835276 DOI: 10.1016/J.Jmb.2008.09.037 |
0.617 |
|
| 2008 |
OuYang B, Pochapsky SS, Dang M, Pochapsky TC. A functional proline switch in cytochrome P450cam. Structure (London, England : 1993). 16: 916-23. PMID 18513977 DOI: 10.1016/J.Str.2008.03.011 |
0.687 |
|
| 2008 |
Chai SC, Ju T, Dang M, Goldsmith RB, Maroney MJ, Pochapsky TC. Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724. Biochemistry. 47: 2428-38. PMID 18237192 DOI: 10.1021/Bi7004152 |
0.787 |
|
| 2008 |
Pochapsky SS, Sunshine JC, Pochapsky TC. Completing the circuit: direct-observe 13C,15N double-quantum spectroscopy permits sequential resonance assignments near a paramagnetic center in acireductone dioxygenase. Journal of the American Chemical Society. 130: 2156-7. PMID 18229927 DOI: 10.1021/Ja710187X |
0.419 |
|
| 2008 |
Hamuro Y, Molnar KS, Coales SJ, OuYang B, Simorellis AK, Pochapsky TC. Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam. Journal of Inorganic Biochemistry. 102: 364-70. PMID 18023482 DOI: 10.1016/J.Jinorgbio.2007.10.001 |
0.632 |
|
| 2007 |
Friedman OM, Matsudaira P, Reis AH, Simister N, Correia I, Kew D, Wei JY, Pochapsky T. Substituted organosiloxanes as potential therapeutics for treatment and prevention of neurodegenerative diseases. Journal of Alzheimer's Disease : Jad. 11: 291-300. PMID 17851178 DOI: 10.3233/Jad-2007-11304 |
0.518 |
|
| 2007 |
Mo H, Dai Y, Pochapsky S, Pochapsky T. 1H, 13C and 15N NMR Assignments for a Carbon Monoxide Generating Metalloenzyme from Klebsiella pneumoniae, Acireductone Dioxygenase (ARD) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4313 |
0.674 |
|
| 2007 |
Pochapsky TC, Ju T, Dang M, Beaulieu R, Pagani GM, OuYang B. Nickel in Acireductone Dioxygenase Nickel and Its Surprising Impact in Nature. 2: 473-500. DOI: 10.1002/9780470028131.ch12 |
0.652 |
|
| 2006 |
OuYang B, Pochapsky SS, Pagani GM, Pochapsky TC. Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam. Biochemistry. 45: 14379-88. PMID 17128977 DOI: 10.1021/Bi0617355 |
0.555 |
|
| 2006 |
Ju T, Goldsmith RB, Chai SC, Maroney MJ, Pochapsky SS, Pochapsky TC. One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase. Journal of Molecular Biology. 363: 823-34. PMID 16989860 DOI: 10.1016/J.Jmb.2006.08.060 |
0.748 |
|
| 2006 |
Rui L, Pochapsky SS, Pochapsky TC. Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity. Biochemistry. 45: 3887-97. PMID 16548516 DOI: 10.1021/Bi052318F |
0.383 |
|
| 2006 |
Pochapsky TC, Pochapsky SS, Ju T, Hoefler C, Liang J. A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings. Journal of Biomolecular Nmr. 34: 117-27. PMID 16518698 DOI: 10.1007/S10858-005-5735-8 |
0.746 |
|
| 2005 |
Sauter M, Lorbiecke R, Ouyang B, Pochapsky TC, Rzewuski G. The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine. The Plant Journal : For Cell and Molecular Biology. 44: 718-29. PMID 16297065 DOI: 10.1111/J.1365-313X.2005.02564.X |
0.538 |
|
| 2005 |
Wei JY, Pochapsky TC, Pochapsky SS. Detection of a high-barrier conformational change in the active site of cytochrome P450cam upon binding of putidaredoxin. Journal of the American Chemical Society. 127: 6974-6. PMID 15884940 DOI: 10.1021/Ja051195J |
0.621 |
|
| 2004 |
Kostic M, Pochapsky TC. (1)H, (13)C and (15)N chemical shift assignments of an enolase-phosphatase, E1, from Klebsiella oxytoca. Journal of Biomolecular Nmr. 30: 359-60. PMID 15756463 DOI: 10.1007/S10858-005-1128-2 |
0.602 |
|
| 2004 |
Zhang Y, Heinsen MH, Kostic M, Pagani GM, Riera TV, Perovic I, Hedstrom L, Snider BB, Pochapsky TC. Analogs of 1-phosphonooxy-2,2-dihydroxy-3-oxo-5-(methylthio)pentane, an acyclic intermediate in the methionine salvage pathway: a new preparation and characterization of activity with E1 enolase/phosphatase from Klebsiella oxytoca. Bioorganic & Medicinal Chemistry. 12: 3847-55. PMID 15210152 DOI: 10.1016/J.Bmc.2004.05.002 |
0.782 |
|
| 2003 |
Kostic M, Bernhardt R, Pochapsky TC. A conserved histidine in vertebrate-type ferredoxins is critical for redox-dependent dynamics. Biochemistry. 42: 8171-82. PMID 12846566 DOI: 10.1021/Bi034500R |
0.653 |
|
| 2003 |
Pochapsky SS, Pochapsky TC, Wei JW. A model for effector activity in a highly specific biological electron transfer complex: the cytochrome P450(cam)-putidaredoxin couple. Biochemistry. 42: 5649-56. PMID 12741821 DOI: 10.1021/Bi034263S |
0.444 |
|
| 2002 |
Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nature Structural Biology. 9: 966-72. PMID 12402029 DOI: 10.1038/Nsb863 |
0.819 |
|
| 2002 |
Kostic M, Pochapsky SS, Pochapsky TC. Rapid recycle (13)C',(15)N and (13)C,(13)C' heteronuclear and homonuclear multiple quantum coherence detection for resonance assignments in paramagnetic proteins: example of Ni(2+)-containing acireductone dioxygenase. Journal of the American Chemical Society. 124: 9054-5. PMID 12149001 DOI: 10.1021/Ja0268480 |
0.627 |
|
| 2002 |
Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry. 41: 6761-9. PMID 12022880 DOI: 10.1021/Bi012209A |
0.735 |
|
| 2002 |
Kostic M, Pochapsky SS, Obenauer J, Mo H, Pagani GM, Pejchal R, Pochapsky TC. Comparison of functional domains in vertebrate-type ferredoxins. Biochemistry. 41: 5978-89. PMID 11993992 DOI: 10.1021/Bi0200256 |
0.796 |
|
| 2001 |
Dai Y, Pochapsky TC, Abeles RH. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry. 40: 6379-87. PMID 11371200 DOI: 10.1021/Bi010110Y |
0.359 |
|
| 2001 |
Pochapsky TC, Kostic M, Jain N, Pejchal R. Redox-dependent conformational selection in a Cys4Fe2S2 ferredoxin. Biochemistry. 40: 5602-14. PMID 11341825 DOI: 10.1021/Bi0028845 |
0.713 |
|
| 2000 |
Heinsen MJ, Pochapsky TC. Site-selective deuterium labeling of the tetrabutylammonium cation Journal of Labelled Compounds and Radiopharmaceuticals. 43: 473-480. DOI: 10.1002/(Sici)1099-1344(200004)43:5<473::Aid-Jlcr333>3.0.Co;2-S |
0.315 |
|
| 2000 |
Hofstetter C, Pochapsky TC. BF4− as a probe for ion pair solution structure using interionic one- and two-dimensional19F{1H} NOEs Magnetic Resonance in Chemistry. 38: 90-94. DOI: 10.1002/(Sici)1097-458X(200002)38:2<90::Aid-Mrc608>3.0.Co;2-P |
0.581 |
|
| 2000 |
Hofstetter C, Pochapsky TC. BF4- as a probe for ion pair solution structure using interionic one- and two-dimensional 19F{1H} NOEs Magnetic Resonance in Chemistry. 38: 90-94. |
0.53 |
|
| 1999 |
Hofstetter C, Wilkinson PS, Pochapsky TC. NMR Structure Determination of Ion Pairs Derived from Quinine: A Model for Templating in Asymmetric Phase-Transfer Reductions by BH(4)(-) with Implications for Rational Design of Phase-Transfer Catalysts. The Journal of Organic Chemistry. 64: 8794-8800. PMID 11674781 DOI: 10.1021/Jo990530H |
0.798 |
|
| 1999 |
Mo H, Dai Y, Pochapsky SS, Pochapsky TC. Letter to the editor: 1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae Journal of Biomolecular Nmr. 14: 287-288. PMID 10481280 DOI: 10.1023/A:1008396624784 |
0.673 |
|
| 1999 |
Arico-Muendel CC, Patera A, Pochapsky TC, Kuti M, Wolfson AJ. Solution structure and dynamics of a serpin reactive site loop using interleukin 1β as a presentation scaffold Protein Engineering. 12: 189-202. PMID 10235620 |
0.74 |
|
| 1999 |
Jain NU, Pochapsky TC. A new assignment strategy for the hyperfine-shifted 13C and 15N resonances in Fe2S2 ferredoxins Biochemical and Biophysical Research Communications. 258: 54-59. PMID 10222234 DOI: 10.1006/Bbrc.1999.0583 |
0.575 |
|
| 1999 |
Mo H, Pochapsky SS, Pochapsky TC. A model for the solution structure of oxidized terpredoxin, a Fe2S2 ferredoxin from Pseudomonas Biochemistry. 38: 5666-5675. PMID 10220356 DOI: 10.1021/Bi983063R |
0.739 |
|
| 1999 |
Pochapsky TC, Jain NU, Kuti M, Lyons TA, Heymont J. A refined model for the solution structure of oxidized putidaredoxin. Biochemistry. 38: 4681-90. PMID 10200155 DOI: 10.1021/Bi983030B |
0.813 |
|
| 1999 |
Jain N, Lyons T, Pochapsky T, Kuti M. 13C and Stereospecific 13C and 1H Resonance Assignments for Oxidized Putidaredoxin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4154 |
0.778 |
|
| 1999 |
Hofstetter C, Wilkinson PS, Pochapsky TC. NMR structure determination of ion pairs derived from quinine: A model for templating in asymmetric phase-transfer reductions by BH4- with implications for rational design of phase-transfer catalysts Journal of Organic Chemistry. 64: 8794-8800. DOI: 10.1021/jo990530h |
0.799 |
|
| 1998 |
Pochapsky TC, Kuti M, Kazanis S. The solution structure of a gallium-substituted putidaredoxin mutant: GaPdx C85S Journal of Biomolecular Nmr. 12: 407-415. PMID 9835048 DOI: 10.1023/A:1008354113765 |
0.821 |
|
| 1998 |
Jain NU, Pochapsky TC. Redox dependence of hyperfine-shifted 13C and 15N resonances in putidaredoxin [15] Journal of the American Chemical Society. 120: 12984-12985. DOI: 10.1021/Ja982877S |
0.527 |
|
| 1997 |
Kazanis S, Pochapsky TC. Structural features of the metal binding site and dynamics of gallium putidaredoxin, a diamagnetic derivative of a CyS4Fe2S2 ferredoxin Journal of Biomolecular Nmr. 9: 337-346. PMID 9255940 DOI: 10.1023/A:1018369721091 |
0.822 |
|
| 1997 |
Mo H, Pochapsky TC. Self-diffusion coefficients of paired ions Journal of Physical Chemistry B. 101. DOI: 10.1021/Jp9703115 |
0.632 |
|
| 1997 |
Mo H, Wang A, Wilkinson PS, Pochapsky TC. Closed-shell ion pairs: Cation and aggregate dynamics of tetraalkylammonium salts in a ion-pairing solvent Journal of the American Chemical Society. 119: 11666-11673. DOI: 10.1021/Ja9723139 |
0.773 |
|
| 1997 |
De Araújo AFP, Pochapsky TC. Estimates for the potential accuracy required in realistic protein folding simulations and structure recognition experiments Folding and Design. 2: 135-139. DOI: 10.1016/S1359-0278(97)00018-7 |
0.312 |
|
| 1997 |
Mo H, Pochapsky TC. Intermolecular interactions characterized by nuclear Overhauser effects Progress in Nuclear Magnetic Resonance Spectroscopy. 30: 1-38. DOI: 10.1016/S0079-6565(96)01036-9 |
0.636 |
|
| 1996 |
Pochapsky TC, Lyons T, Kazanis S, Arakaki T, Ratnaswamy G. A structure-based model for cytochrome P450(cam)-putidaredoxin interactions Biochimie. 78: 723-733. PMID 9010601 DOI: 10.1016/S0300-9084(97)82530-8 |
0.792 |
|
| 1996 |
Lyons TA, Ratnaswamy G, Pochapsky TC. Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange Protein Science. 5: 627-639. PMID 8845752 DOI: 10.1002/Pro.5560050407 |
0.805 |
|
| 1995 |
Pochapsky SS, Mo H, Pochapsky TC. Closed-shell ion pair aggregation in non-polar solvents characterized by NMR diffusion measurements Journal of the Chemical Society, Chemical Communications. 2513-2514. DOI: 10.1039/C39950002513 |
0.646 |
|
| 1995 |
Kazanis S, Pochapsky TC, Barnhart TM, Penner-Hahn JE, Mirza UA, Chait BT. Conversion of a Fe2S2 ferredoxin into a Ga3+ rubredoxin Journal of the American Chemical Society. 117: 6625-6626. DOI: 10.1021/Ja00129A040 |
0.743 |
|
| 1994 |
Pochapsky TC, Ratnaswamy G, Patera A. Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin Biochemistry®. 6433-6441. PMID 8204576 DOI: 10.1021/Bi00187A007 |
0.811 |
|
| 1994 |
Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA. An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from pseudomonas Biochemistry®. 6424-6432. PMID 8204575 DOI: 10.1021/Bi00187A006 |
0.804 |
|
| 1994 |
Thériault Y, Pochapsky TC, Dalvit C, Chiu ML, Sligar SG, Wright PE. 1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin. Journal of Biomolecular Nmr. 4: 491-504. PMID 8075538 DOI: 10.1007/Bf00156616 |
0.314 |
|
| 1993 |
Pochapsky TC, Wang AP, Stone PM. Closed-shell ion pair structure and dynamics: Steady-state1H{1H}, 10B{1H}, and11B{1H} nuclear overhauser effects and10B, 11B nuclear relaxation of tetraalkylammonium tetrahydridoborates in ion-pairing and dissociative solvents Journal of the American Chemical Society. 115: 11084-11091. DOI: 10.1021/Ja00077A004 |
0.327 |
|
| 1993 |
Ratnaswamy G, Pochapsky TC. Characterization of hyperfine-shifted1H resonances in oxidized and reduced putidaredoxin, an Fe2S2 ferredoxin fromPseudomonas putida Magnetic Resonance in Chemistry. 31: S73-S77. DOI: 10.1002/Mrc.1260311315 |
0.787 |
|
| 1992 |
Xiao Mei Ye, Pochapsky TC, Pochapsky SS. 1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas Biochemistry. 31: 1961-1968. PMID 1536837 DOI: 10.1021/Bi00122A009 |
0.431 |
|
| 1991 |
Pochapsky TC, Ye XM. 1H NMR identification of a β-sheet structure and description of folding topology in putidaredoxin Biochemistry. 30: 3850-3856. PMID 2018758 DOI: 10.1021/Bi00230A007 |
0.372 |
|
| 1990 |
Lee KB, La Mar GN, Kehres LA, Fujinari EM, Smith KM, Pochapsky TC, Sligar SG. 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5. Biochemistry. 29: 9623-31. PMID 2271605 DOI: 10.1021/Bi00493A017 |
0.357 |
|
| 1990 |
Pochapsky TC, Stone PM. Study of ion pair solution structure using nuclear overhauser effects: interionic 1H{1H} and 11B{1H} NOES in the (CH3CH2CH2CH2)4N+,BH4- ion pair Journal of the American Chemical Society. 112: 6714-6715. DOI: 10.1021/Ja00174A042 |
0.34 |
|
| 1990 |
Pochapsky TC, Sligar SG, McLachlan SJ, La Mar GN. Relationship between heme binding site structure and heme orientations of two ferrocytochrome b5s. A study in prosthetic group recognition Journal of the American Chemical Society. 112: 5258-5263. DOI: 10.1021/Ja00169A038 |
0.341 |
|
| 1990 |
PIRKLE WH, POCHAPSKY TC. ChemInform Abstract: Theory and Design of Chiral Stationary Phases for the Direct Chromatographic Separation of Enantiomers Cheminform. 21. DOI: 10.1002/chin.199021338 |
0.403 |
|
| 1989 |
Pirkle WH, Pochapsky TC. Considerations of chiral recognition relevant to the liquid chromatographic separation of enantiomers Chemical Reviews. 89: 347-362. DOI: 10.1021/Cr00092A006 |
0.477 |
|
| 1988 |
Pirkle WH, Pochapsky TC. Separation of the stereoisomers of a homologeous series of bis-amides on chiral stationary phases Chromatographia. 25: 652-654. DOI: 10.1007/BF02327666 |
0.423 |
|
| 1987 |
Pirkle WH, Alessi DM, Hyun MH, Pochapsky TC. Separation of some enantiomeric di- and tripeptides on chiral stationary phases. Journal of Chromatography. 398: 203-9. PMID 3654838 DOI: 10.1016/S0021-9673(01)96505-7 |
0.432 |
|
| 1987 |
Pirkle WH, Pochapsky TC. Chiral molecular recognition in small bimolecular systems: A spectroscopic investigation into the nature of diastereomeric complexes Journal of the American Chemical Society. 109: 5975-5982. DOI: 10.1021/Ja00254A014 |
0.523 |
|
| 1987 |
Pirkle WH, Mahler GS, Pochapsky TC, Hyun MH. Direct chromatographic separation of enantiomeric diol derivatives Journal of Chromatography A. 388: 307-314. DOI: 10.1016/S0021-9673(01)94492-9 |
0.45 |
|
| 1986 |
Pirkle WH, Pochapsky TC, Mahler GS, Corey DE, Reno DS, Alessi DM. Useful and easily prepared chiral stationary phases for the direct chromatographic separation of the enantiomers of a variety of derivatized amines, amino acids, alcohols, and related compounds Journal of Organic Chemistry. 51: 4991-5000. DOI: 10.1021/Jo00375A045 |
0.476 |
|
| 1986 |
Pirkle WH, Pochapsky TC. Intermolecular proton[proton] nuclear Overhauser effects in diastereomeric complexes: support for a chromatographically derived chiral recognition model Journal of the American Chemical Society. 108: 5627-5628. DOI: 10.1021/Ja00278A045 |
0.536 |
|
| 1986 |
Pirkle WH, Pochapsky TC. Generation of extreme selectivity in chiral recognition Journal of Chromatography A. 369: 175-177. DOI: 10.1016/S0021-9673(00)90111-0 |
0.416 |
|
| 1986 |
Pirkle WH, Pochapsky TC. Preparation of N-(2-naphthyl)-2-amino acids and esters of high enantiomeric purity Journal of Organic Chemistry. 51: 102-105. DOI: 10.1002/Chin.198625201 |
0.488 |
|
| 1986 |
Pirkle WH, Pochapsky TC. A new, easily accessible reciprocal chiral stationary phase for the chromatographic separation of enantiomers Journal of the American Chemical Society. 108: 352-354. |
0.408 |
|
| 1986 |
Pirkle WH, Pochapsky TC. Intermolecular 1H{1H} nuclear overhauser effects in diastereomeric complexes: Support for a chromatographically derived chiral recognition model Journal of the American Chemical Society. 108: 5627-5628. |
0.477 |
|
| 1985 |
Pirkle WH, Pochapsky TC, Mahler GS, Field RE. Chromatographic separation of the enantiomers of 2-carboalkoxyindolines and N-aryl-α-amino esters on chiral stationary phases derived from N-(3,5-dinitrobenzoyl)-α-amino acids Journal of Chromatography A. 348: 89-96. DOI: 10.1016/S0021-9673(01)92442-2 |
0.457 |
|
| Show low-probability matches. |
