| Year |
Citation |
Score |
| 2016 |
Lal J, Maccarini M, Fouquet P, Ho NT, Ho C, Makowski L. Modulation of Hemoglobin Dynamics by an Allosteric Effector. Protein Science : a Publication of the Protein Society. PMID 27977887 DOI: 10.1002/Pro.3099 |
0.304 |
|
| 2016 |
Chi CY, Lin CH, Ho MW, Ding JY, Huang WC, Shih HP, Yeh CF, Fung CP, Sun HY, Huang CT, Wu TS, Chang CY, Liu YM, Feng JY, Wu WK, ... ... Ho CM, et al. Clinical manifestations, course, and outcome of patients with neutralizing anti-interferon-γ autoantibodies and disseminated nontuberculous mycobacterial infections. Medicine. 95: e3927. PMID 27336882 DOI: 10.1097/MD.0000000000003927 |
0.392 |
|
| 2015 |
Tam MF, Tam TC, Simplaceanu V, Ho NT, Zou M, Ho C. Sickle Cell Hemoglobin with Mutation at αHis-50 Has Improved Solubility. The Journal of Biological Chemistry. 290: 21762-72. PMID 26187468 DOI: 10.1074/Jbc.M115.658054 |
0.3 |
|
| 2015 |
Yuan Y, Tam MF, Simplaceanu V, Ho C. New look at hemoglobin allostery. Chemical Reviews. 115: 1702-24. PMID 25607981 DOI: 10.1021/Cr500495X |
0.339 |
|
| 2013 |
Fan JS, Zheng Y, Choy WY, Simplaceanu V, Ho NT, Ho C, Yang D. Solution structure and dynamics of human hemoglobin in the carbonmonoxy form. Biochemistry. 52: 5809-20. PMID 23901897 DOI: 10.1021/Bi4005683 |
0.326 |
|
| 2013 |
Tam MF, Rice NW, Maillett DH, Simplaceanu V, Ho NT, Tam TC, Shen TJ, Ho C. Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the αVal-62 or βVal-67 position of the distal heme pocket. The Journal of Biological Chemistry. 288: 25512-21. PMID 23867463 DOI: 10.1074/Jbc.M113.474841 |
0.344 |
|
| 2013 |
Yuan Y, Byrd C, Shen T, Ho NT, Simplaceanu V, Chyi T, Tam S, Ho C. Roles of Amino Acid Residues in Woolly Mammoth Hemoglobin on the Temperature Effect of Oxygen Binding Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.3099 |
0.309 |
|
| 2012 |
Brillet T, Marden MC, Yeh JI, Shen TJ, Ho NT, Kettering R, Du S, Vasseur C, Domingues-Hamdi E, Ho C, Baudin-Creuza V. Interaction of haptoglobin with hemoglobin octamers based on the mutation αAsn78Cys or βGly83Cys. American Journal of Molecular Biology. 2: 1-10. PMID 23847747 DOI: 10.4236/Ajmb.2012.21001 |
0.34 |
|
| 2012 |
Noguchi H, Campbell KL, Ho C, Unzai S, Park SY, Tame JR. Structures of haemoglobin from woolly mammoth in liganded and unliganded states. Acta Crystallographica. Section D, Biological Crystallography. 68: 1441-9. PMID 23090393 DOI: 10.1107/S0907444912029459 |
0.3 |
|
| 2012 |
Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, ... ... Ho C, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371 |
0.513 |
|
| 2011 |
Yuan Y, Shen TJ, Gupta P, Ho NT, Simplaceanu V, Tam TC, Hofreiter M, Cooper A, Campbell KL, Ho C. A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. Biochemistry. 50: 7350-60. PMID 21806075 DOI: 10.1021/Bi200777J |
0.307 |
|
| 2011 |
Hitchens TK, Ye Q, Eytan DF, Janjic JM, Ahrens ET, Ho C. 19F MRI detection of acute allograft rejection with in vivo perfluorocarbon labeling of immune cells. Magnetic Resonance in Medicine. 65: 1144-53. PMID 21305593 DOI: 10.1002/Mrm.22702 |
0.319 |
|
| 2011 |
Yuan Y, Simplaceanu V, Ho NT, Ho C. An Investigation of the Distal Histidyl H-Bonds in Oxyhemoglobin: Effects of Temperature, pH, and Inositol Hexaphosphate Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.1413 |
0.335 |
|
| 2010 |
Yuan Y, Simplaceanu V, Ho NT, Ho C. An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate. Biochemistry. 49: 10606-15. PMID 21077639 DOI: 10.1021/Bi100927P |
0.318 |
|
| 2010 |
Bermejo GA, Strub MP, Ho C, Tjandra N. Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein. Biochemistry. 49: 1893-902. PMID 20141110 DOI: 10.1021/Bi902045P |
0.317 |
|
| 2009 |
Bermejo GA, Strub MP, Ho C, Tjandra N. Determination of the solution-bound conformation of an amino acid binding protein by NMR paramagnetic relaxation enhancement: use of a single flexible paramagnetic probe with improved estimation of its sampling space. Journal of the American Chemical Society. 131: 9532-7. PMID 19583434 DOI: 10.1021/Ja902436G |
0.313 |
|
| 2008 |
Maillett DH, Simplaceanu V, Shen TJ, Ho NT, Olson JS, Ho C. Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin. Biochemistry. 47: 10551-63. PMID 18788751 DOI: 10.1021/Bi800816V |
0.318 |
|
| 2008 |
Song XJ, Simplaceanu V, Ho NT, Ho C. Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin. Biochemistry. 47: 4907-15. PMID 18376851 DOI: 10.1021/Bi7023699 |
0.38 |
|
| 2008 |
Tsai CH, Chen YC, Chen LD, Pan TC, Ho CY, Lai MT, Tsai FJ, Chen WC. A traditional Chinese herbal antilithic formula, Wulingsan, effectively prevents the renal deposition of calcium oxalate crystal in ethylene glycol-fed rats. Urological Research. 36: 17-24. PMID 18040675 DOI: 10.1007/s00240-007-0122-4 |
0.408 |
|
| 2007 |
Sahu SC, Simplaceanu V, Gong Q, Ho NT, Tian F, Prestegard JH, Ho C. Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Biochemistry. 46: 9973-80. PMID 17691822 DOI: 10.1021/Bi700935Z |
0.316 |
|
| 2007 |
Song XJ, Yuan Y, Simplaceanu V, Sahu SC, Ho NT, Ho C. A comparative NMR study of the polypeptide backbone dynamics of hemoglobin in the deoxy and carbonmonoxy forms. Biochemistry. 46: 6795-803. PMID 17497935 DOI: 10.1021/Bi602654U |
0.345 |
|
| 2007 |
Li D, Manjula BN, Ho NT, Simplaceanu V, Ho C, Acharya AS. Molecular aspects of the high oxygen affinity of non-hypertensive hexa pegylated hemoglobin, [(SP-PEG5K)(6)-Hb]. Artificial Cells, Blood Substitutes, and Immobilization Biotechnology. 35: 19-29. PMID 17364468 DOI: 10.1080/10731190600974376 |
0.321 |
|
| 2006 |
Sahu SC, Simplaceanu V, Gong Q, Ho NT, Glushka JG, Prestegard JH, Ho C. Orientation of deoxyhemoglobin at high magnetic fields: structural insights from RDCs in solution. Journal of the American Chemical Society. 128: 6290-1. PMID 16683773 DOI: 10.1021/Ja060023Z |
0.349 |
|
| 2006 |
Kneipp J, Balakrishnan G, Chen R, Shen TJ, Sahu SC, Ho NT, Giovannelli JL, Simplaceanu V, Ho C, Spiro TG. Dynamics of allostery in hemoglobin: roles of the penultimate tyrosine H bonds. Journal of Molecular Biology. 356: 335-53. PMID 16368110 DOI: 10.1016/J.Jmb.2005.11.006 |
0.35 |
|
| 2006 |
Vasseur-Godbillon C, Sahu SC, Domingues E, Fablet C, Giovannelli JL, Tam TC, Ho NT, Ho C, Marden MC, Baudin-Creuza V. Recombinant hemoglobin betaG83C-F41Y. The Febs Journal. 273: 230-41. PMID 16367763 DOI: 10.1111/J.1742-4658.2005.05063.X |
0.313 |
|
| 2005 |
Tam MF, Chen J, Tam TC, Tsai CH, Shen TJ, Simplaceanu V, Feinstein TN, Barrick D, Ho C. Enhanced inhibition of polymerization of sickle cell hemoglobin in the presence of recombinant mutants of human fetal hemoglobin with substitutions at position 43 in the gamma-chain. Biochemistry. 44: 12188-95. PMID 16142917 DOI: 10.1021/Bi050300Z |
0.552 |
|
| 2005 |
Xu Y, Lin Z, Ho C, Yang D. A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C,15N-labeled large proteins. Journal of the American Chemical Society. 127: 11920-1. PMID 16117513 DOI: 10.1021/Ja053539B |
0.318 |
|
| 2005 |
Manjula BN, Tsai AG, Intaglietta M, Tsai CH, Ho C, Smith PK, Perumalsamy K, Kanika ND, Friedman JM, Acharya SA. Conjugation of multiple copies of polyethylene glycol to hemoglobin facilitated through thiolation: influence on hemoglobin structure and function. The Protein Journal. 24: 133-46. PMID 16096719 DOI: 10.1007/S10930-005-7837-2 |
0.455 |
|
| 2005 |
Wiltrout ME, Giovannelli JL, Simplaceanu V, Lukin JA, Ho NT, Ho C. A biophysical investigation of recombinant hemoglobins with aromatic B10 mutations in the distal heme pockets. Biochemistry. 44: 7207-17. PMID 15882059 DOI: 10.1021/Bi048289A |
0.358 |
|
| 2005 |
Lin SS, Chou MY, Ho CC, Kao CT, Tsai CH, Wang L, Yang CC. Study of the viral infections and cytokines associated with recurrent aphthous ulceration. Microbes and Infection / Institut Pasteur. 7: 635-44. PMID 15840465 DOI: 10.1016/j.micinf.2004.12.023 |
0.396 |
|
| 2004 |
Balakrishnan G, Tsai CH, Wu Q, Case MA, Pevsner A, McLendon GL, Ho C, Spiro TG. Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: Time-resolved UV resonance raman evidence for intra-dimer coupling Journal of Molecular Biology. 340: 857-868. PMID 15223326 DOI: 10.1016/J.Jmb.2004.05.013 |
0.55 |
|
| 2004 |
Manjula BN, Tsai AG, Intaglietta M, Tsai CH, Ho C, Malavalli A, Vandegriff KD, Winslow RM, Smith PK, Perumalsamy K, Devi Kanika N, Friedman JM, Acharya SA. WITHDRAWN: PEGylated hemoglobin: Role of surface configuration of PEG for the modulation of hemoglobin vasoactivity. The Journal of Biological Chemistry. PMID 15194702 DOI: 10.1074/jbc.M403468200 |
0.401 |
|
| 2004 |
Srinivasulu S, Manjula BN, Nagel RL, Tsai CH, Ho C, Prabhakaran M, Acharya SA. Hemoglobin Einstein: semisynthetic deletion in the B-helix of the alpha-chain. Protein Science : a Publication of the Protein Society. 13: 1266-75. PMID 15096632 DOI: 10.1110/Ps.03567804 |
0.525 |
|
| 2004 |
Barrick D, Lukin JA, Simplaceanu V, Ho C. Nuclear magnetic resonance spectroscopy in the study of hemoglobin cooperativity. Methods in Enzymology. 379: 28-54. PMID 15051350 DOI: 10.1016/S0076-6879(04)79002-3 |
0.356 |
|
| 2004 |
Lukin JA, Kontaxis G, Simplaceanu V, Yuan Y, Bax A, Ho C. Backbone resonance assignments of human adult hemoglobin in the carbonmonoxy form. Journal of Biomolecular Nmr. 28: 203-4. PMID 14755170 DOI: 10.1023/B:Jnmr.0000013816.64039.6F |
0.358 |
|
| 2003 |
Ho CC, Yang XW, Lee TL, Liao PH, Yang SH, Tsai CH, Chou MY. Activation of p53 signalling in acetylsalicylic acid-induced apoptosis in OC2 human oral cancer cells. European Journal of Clinical Investigation. 33: 875-82. PMID 14511359 |
0.418 |
|
| 2003 |
Acharya SA, Malavalli A, Peterson E, Sun PD, Ho C, Prabhakaran M, Arnone A, Manjula BN, Friedman JM. Probing the conformation of hemoglobin presbyterian in the R-state. Journal of Protein Chemistry. 22: 221-30. PMID 12962322 DOI: 10.1023/A:1025080801951 |
0.324 |
|
| 2003 |
Lukin JA, Ho C. Nuclear magnetic resonance of hemoglobins. Methods in Molecular Medicine. 82: 251-69. PMID 12669648 DOI: 10.1385/1-59259-373-9:251 |
0.319 |
|
| 2003 |
Fablet C, Marden MC, Green BN, Ho C, Pagnier J, Baudin-Creuza V. Stable octameric structure of recombinant hemoglobin alpha(2)beta(2)83 Gly-->Cys. Protein Science : a Publication of the Protein Society. 12: 690-5. PMID 12649426 DOI: 10.1110/Ps.0234403 |
0.31 |
|
| 2003 |
Tsai CH, Simplaceanu V, Ho NT, Shen TJ, Wang D, Spiro TG, Ho C. Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R-->T transition without altering the free energies of oxygenation. Biophysical Chemistry. 100: 131-42. PMID 12646359 DOI: 10.1016/S0301-4622(02)00274-0 |
0.566 |
|
| 2003 |
Lukin JA, Kontaxis G, Simplaceanu V, Yuan Y, Bax A, Ho C. Quaternary structure of hemoglobin in solution. Proceedings of the National Academy of Sciences of the United States of America. 100: 517-20. PMID 12525687 DOI: 10.1073/Pnas.232715799 |
0.32 |
|
| 2002 |
Cheng Y, Shen TJ, Simplaceanu V, Ho C. Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine. Biochemistry. 41: 11901-13. PMID 12269835 DOI: 10.1021/Bi0202880 |
0.398 |
|
| 2002 |
Yuan Y, Simplaceanu V, Lukin JA, Ho C. NMR investigation of the dynamics of tryptophan side-chains in hemoglobins. Journal of Molecular Biology. 321: 863-78. PMID 12206767 DOI: 10.1016/S0022-2836(02)00704-0 |
0.361 |
|
| 2002 |
Tsai CH, Ho C. Recombinant hemoglobins with low oxygen affinity and high cooperativity. Biophysical Chemistry. 98: 15-25. PMID 12128186 DOI: 10.1016/S0301-4622(02)00081-9 |
0.571 |
|
| 2002 |
Chang CK, Simplaceanu V, Ho C. Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces. Biochemistry. 41: 5644-55. PMID 11969426 DOI: 10.1021/Bi011919D |
0.709 |
|
| 2001 |
Tsai CH, Larson SC, Shen TJ, Ho NT, Fisher GW, Tam MF, Ho C. Probing the importance of the amino-terminal sequence of the beta- and gamma-chains to the properties of normal adult and fetal hemoglobins. Biochemistry. 40: 12169-77. PMID 11580292 DOI: 10.1021/Bi0111045 |
0.538 |
|
| 2001 |
Barrick D, Ho NT, Simplaceanu V, Ho C. Distal ligand reactivity and quaternary structure studies of proximally detached hemoglobins. Biochemistry. 40: 3780-95. PMID 11300758 DOI: 10.1021/Bi002165Q |
0.357 |
|
| 2000 |
Tsai CH, Fang TY, Ho NT, Ho C. Novel recombinant hemoglobin, rHb (beta N108Q), with low oxygen affinity, high cooperativity, and stability against autoxidation. Biochemistry. 39: 13719-29. PMID 11076511 DOI: 10.1021/Bi001116A |
0.553 |
|
| 2000 |
Fang TY, Simplaceanu V, Tsai CH, Ho NT, Ho C. An additional H-bond in the alpha 1 beta 2 interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (beta L105W). Biochemistry. 39: 13708-18. PMID 11076510 DOI: 10.1021/Bi001115I |
0.545 |
|
| 2000 |
Lukin JA, Simplaceanu V, Zou M, Ho NT, Ho C. NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 97: 10354-8. PMID 10962034 DOI: 10.1073/Pnas.190254697 |
0.343 |
|
| 2000 |
Simplaceanu V, Lukin JA, Fang TY, Zou M, Ho NT, Ho C. Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin. Biophysical Journal. 79: 1146-54. PMID 10920044 DOI: 10.1016/S0006-3495(00)76368-5 |
0.369 |
|
| 1999 |
Jeong ST, Ho NT, Hendrich MP, Ho C. Recombinant hemoglobin(alpha 29leucine --> phenylalanine, alpha 96valine --> tryptophan, beta 108asparagine --> lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation. Biochemistry. 38: 13433-42. PMID 10529220 DOI: 10.1021/Bi991271T |
0.354 |
|
| 1999 |
Fang TY, Zou M, Simplaceanu V, Ho NT, Ho C. Assessment of roles of surface histidyl residues in the molecular basis of the Bohr effect and of beta 143 histidine in the binding of 2,3-bisphosphoglycerate in human normal adult hemoglobin. Biochemistry. 38: 13423-32. PMID 10529219 DOI: 10.1021/Bi9911379 |
0.372 |
|
| 1999 |
Tsai CH, Shen TJ, Ho NT, Ho C. Effects of substitutions of lysine and aspartic acid for asparagine at beta 108 and of tryptophan for valine at alpha 96 on the structural and functional properties of human normal adult hemoglobin: roles of alpha 1 beta 1 and alpha 1 beta 2 subunit interfaces in the cooperative oxygenation process. Biochemistry. 38: 8751-61. PMID 10393550 DOI: 10.1021/Bi990286O |
0.543 |
|
| 1999 |
Dodd SJ, Williams M, Suhan JP, Williams DS, Koretsky AP, Ho C. Detection of single mammalian cells by high-resolution magnetic resonance imaging. Biophysical Journal. 76: 103-9. PMID 9876127 DOI: 10.1016/S0006-3495(99)77182-1 |
0.309 |
|
| 1998 |
Puius YA, Zou M, Ho NT, Ho C, Almo SC. Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb(alpha 96Val-->Trp). Biochemistry. 37: 9258-65. PMID 9649306 DOI: 10.1021/Bi9727287 |
0.33 |
|
| 1997 |
Klug CA, Tasaki K, Tjandra N, Ho C, Schaefer J. Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR Biochemistry. 36: 9405-9408. PMID 9235984 DOI: 10.1021/Bi9705016 |
0.312 |
|
| 1997 |
Huang S, Peterson ES, Ho C, Friedman JM. Quaternary structure sensitive tyrosine interactions in hemoglobin: a UV resonance Raman study of the double mutant rHb (beta99Asp-->Asn, alpha42Tyr-->Asp). Biochemistry. 36: 6197-206. PMID 9166792 DOI: 10.1021/Bi970018V |
0.347 |
|
| 1997 |
Yu J, Simplaceanu V, Tjandra NL, Cottam PF, Lukin JA, Ho C. 1H, 13C, and 15N NMR backbone assignments and chemical-shift-derived secondary structure of glutamine-binding protein of Escherichia coli Journal of Biomolecular Nmr. 9: 167-180. PMID 9090131 DOI: 10.1023/A:1018606304131 |
0.354 |
|
| 1997 |
Lukin JA, Gove AP, Talukdar SN, Ho C. Automated probabilistic method for assigning backbone resonances of (13C,15N)-labeled proteins. Journal of Biomolecular Nmr. 9: 151-66. PMID 9090130 DOI: 10.1023/A:1018602220061 |
0.308 |
|
| 1996 |
Sun Z-, Pratt EA, Simplaceanu V, Ho C. A 19F-NMR Study of the Equilibrium Unfolding of Membrane-Associated d-Lactate Dehydrogenase of Escherichia coli† Biochemistry. 35: 16502-16509. PMID 8987983 DOI: 10.1021/Bi9620619 |
0.319 |
|
| 1996 |
Ho C, Willis BF, Shen TJ, Ho NT, Sun DP, Tam MF, Suzuka SM, Fabry ME, Nagel RL. Roles of α114 and β87 amino acid residues in the polymerization of hemoglobin S: Implications for gene therapy Journal of Molecular Biology. 263: 475-485. PMID 8918602 DOI: 10.1006/Jmbi.1996.0590 |
0.32 |
|
| 1996 |
Kim HW, Shen TJ, Ho NT, Zou M, Tam MF, Ho C. Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin. Biochemistry. 35: 6620-7. PMID 8639610 DOI: 10.1021/Bi952518Z |
0.334 |
|
| 1995 |
Kim HW, Shen TJ, Sun DP, Ho NT, Madrid M, Ho C. A novel low oxygen affinity recombinant hemoglobin (alpha96val--> Trp): switching quaternary structure without changing the ligation state. Journal of Molecular Biology. 248: 867-82. PMID 7752247 DOI: 10.1006/Jmbi.1995.0267 |
0.324 |
|
| 1995 |
Fetler BK, Simplaceanu V, Ho C. 1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells Biophysical Journal. 68: 681-693. PMID 7696519 DOI: 10.1016/S0006-3495(95)80229-8 |
0.406 |
|
| 1994 |
Ho C, Perussi JR. Proton nuclear magnetic resonance studies of hemoglobin. Methods in Enzymology. 232: 97-139. PMID 8057888 DOI: 10.1016/0076-6879(94)32046-2 |
0.359 |
|
| 1994 |
Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C. An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR Biochemistry. 33: 8651-8661. PMID 8038154 DOI: 10.1021/Bi00195A005 |
0.33 |
|
| 1994 |
Kim HW, Shen TJ, Sun DP, Ho NT, Madrid M, Tam MF, Zou M, Cottam PF, Ho C. Restoring allosterism with compensatory mutations in hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 91: 11547-51. PMID 7972099 DOI: 10.1073/Pnas.91.24.11547 |
0.338 |
|
| 1993 |
Shen TJ, Ho NT, Simplaceanu V, Zou M, Green BN, Tam MF, Ho C. Production of unmodified human adult hemoglobin in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 90: 8108-12. PMID 8367471 DOI: 10.1073/Pnas.90.17.8108 |
0.336 |
|
| 1993 |
Dowd SR, Sturtevant JM, Simplaceanu V, Ho C. Phosphorus-31-NMR and calorimetric studies of the low-temperature behavior of three fluorine-19-labeled dimyristoylphosphatidylcholines The Journal of Physical Chemistry. 97: 2946-2951. DOI: 10.1021/J100114A020 |
0.539 |
|
| 1993 |
Rule GS, Tjandra N, Simplaceanu V, Ho C. Assignment Strategies for 15N-1H Correlated Spectra of Large Proteins in Solution Journal of Magnetic Resonance, Series B. 102: 126-128. DOI: 10.1006/Jmrb.1993.1074 |
0.588 |
|
| 1992 |
Farghali H, Rossaro L, Gavaler JS, Thiel DHV, Dowd SR, Williams DS, Ho C. 31P-NMR spectroscopy of perifused rat hepatocytes immobilized in agarose threads: application to chemical-induced hepatotoxicity. Biochimica Et Biophysica Acta. 1139: 105-114. PMID 1610910 DOI: 10.1016/0925-4439(92)90089-6 |
0.313 |
|
| 1992 |
Ho C. Proton nuclear magnetic resonance studies on hemoglobin: Cooperative interactions and partially ligated intermediates Advances in Protein Chemistry. 43: 153-312. PMID 1442322 DOI: 10.1016/S0065-3233(08)60555-0 |
0.366 |
|
| 1992 |
Tjandra N, Simplaceanu V, Cottam PF, Ho C. Multidimensional1H and15N NMR investigation of glutamine-binding protein of Escherichia coli Journal of Biomolecular Nmr. 2: 149-160. PMID 1422149 DOI: 10.1007/Bf01875526 |
0.34 |
|
| 1991 |
Ho C. Roles of the β146 histidyl residue in the molecular basis of the bohr effect of hemoglobin: A proton nuclear magnetic resonance study Biochemistry. 30: 1865-1877. PMID 1993201 DOI: 10.1021/Bi00221A020 |
0.374 |
|
| 1991 |
Truong HTN, Pratt EA, Rule GS, Hsue PY, Ho C. Inactive and temperature-sensitive folding mutants generated by tryptophan substitutions in the membrane-bound D-lactate dehydrogenase of Escherichia coli Biochemistry. 30: 10722-10729. PMID 1931992 DOI: 10.1021/Bi00108A017 |
0.593 |
|
| 1990 |
Russu IM, Wu SS, Bupp KA, Ho NT, Ho C. 1H and 31P nuclear magnetic resonance investigation of the interaction between 2,3-diphosphoglycerate and human normal adult hemoglobin Biochemistry. 29: 3785-3792. PMID 2340273 DOI: 10.1021/Bi00467A027 |
0.374 |
|
| 1990 |
Busch MR, Ho CE. Effects of anions on the molecular basis of the Bohr effect of hemoglobin. Biophysical Chemistry. 37: 313-22. PMID 2285794 DOI: 10.1016/0301-4622(90)88031-M |
0.34 |
|
| 1990 |
Peersen OB, Pratt EA, Truong HT, Ho C, Rule GS. Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study. Biochemistry. 29: 3256-62. PMID 2185834 DOI: 10.1021/Bi00465A017 |
0.651 |
|
| 1990 |
Madrid M, Simplaceanu V, Ho NT, Ho C. Effects of chemical exchange and dipole-dipole interactions on the proton relaxation rates of surface histidyl residues in human hemoglobins Journal of Magnetic Resonance (1969). 88: 42-59. DOI: 10.1016/0022-2364(90)90107-K |
0.322 |
|
| 1989 |
Russu IM, Wu SS, Ho NT, Kellogg GW, Ho C. A proton nuclear magnetic resonance investigation of the anion Bohr effect of human normal adult hemoglobin Biochemistry. 28: 5298-5306. PMID 2765535 DOI: 10.1021/Bi00438A057 |
0.333 |
|
| 1989 |
Shen Q, Simplaceanu V, Cottam PF, Wu J, Hong J, Ho C. Molecular genetic, biochemical and nuclear magnetic resonance studies on the role of the tryptophan residues of glutamine-binding protein from Escherichia coli. Journal of Molecular Biology. 210: 859-867. PMID 2693744 DOI: 10.1016/0022-2836(89)90113-7 |
0.343 |
|
| 1989 |
Shen Q, Simplaceanu V, Cottam PF, Ho C. Proton nuclear magnetic resonance studies on glutamine-binding protein from Escherichia coli. Formation of intermolecular and intramolecular hydrogen bonds upon ligand binding. Journal of Molecular Biology. 210: 849-857. PMID 2693743 DOI: 10.1016/0022-2836(89)90112-5 |
0.34 |
|
| 1989 |
Ho C, Pratt EA, Rule GS. Membrane-bound d-lactate dehydrogenase of Escherichia coli: a model for protein interactions in membranes Bba - Reviews On Biomembranes. 988: 173-184. PMID 2655708 DOI: 10.1016/0304-4157(89)90018-X |
0.593 |
|
| 1989 |
Buckel SD, Cottam PF, Simplaceanu V, Ho C. Formation of intermolecular and intramolecular hydrogen bonds in histidine-binding protein J of Salmonella typhimurium upon binding L-histidine. A proton nuclear magnetic resonance study. Journal of Molecular Biology. 208: 477-489. PMID 2552128 DOI: 10.1016/0022-2836(89)90511-1 |
0.353 |
|
| 1988 |
Brindle KM, Rajagopalan B, Williams DS, Detre JA, Simplaceanu E, Ho C, Radda GK. 31P NMR measurements of myocardial pH in vivo. Biochemical and Biophysical Research Communications. 151: 70-7. PMID 3348798 DOI: 10.1016/0006-291X(88)90560-8 |
0.318 |
|
| 1987 |
Russu IM, Ho NT, Ho C. A proton nuclear Overhauser effect investigation of the subunit interfaces in human normal adult hemoglobin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 914: 40-48. PMID 3607061 DOI: 10.1016/0167-4838(87)90159-2 |
0.364 |
|
| 1987 |
Rule GS, Pratt EA, Simplaceanu V, Ho C. Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli Biochemistry. 26: 549-556. PMID 3548821 DOI: 10.1021/Bi00376A029 |
0.655 |
|
| 1986 |
Ho C, Rule GS, Pratt EA. Nuclear magnetic resonance, biochemical, and molecular genetic studies of the membrane-bound d-lactate dehydrogenase of Escherichia coli. Biophysical Journal. 49: 113-5. PMID 19431609 DOI: 10.1016/S0006-3495(86)83615-3 |
0.627 |
|
| 1986 |
Russu IM, Lin AK, Yang CP, Ho C. Molecular basis for the anti-sickling activity of aromatic amino acids and related compounds: a proton nuclear magnetic resonance investigation. Biochemistry. 25: 808-15. PMID 3964645 DOI: 10.1021/Bi00352A012 |
0.367 |
|
| 1986 |
Russu IM, Ho C. Assessment of role of beta 146-histidyl and other histidyl residues in the Bohr effect of human normal adult hemoglobin. Biochemistry. 25: 1706-16. PMID 3707904 DOI: 10.1021/Bi00355A040 |
0.36 |
|
| 1985 |
Wu WG, Dowd SR, Simplaceanu V, Peng ZY, Ho C. 19F NMR investigation of molecular motion and packing in sonicated phospholipid vesicles. Biochemistry. 24: 7153-7161. PMID 4084571 DOI: 10.1021/Bi00346A020 |
0.326 |
|
| 1985 |
Rule GS, Pratt EA, Chin CC, Wold F, Ho C. Overproduction and nucleotide sequence of the respiratory D-lactate dehydrogenase of Escherichia coli. Journal of Bacteriology. 161: 1059-68. PMID 3882663 DOI: 10.1128/Jb.161.3.1059-1068.1985 |
0.594 |
|
| 1984 |
Russu IM, Lin AK, Ferro-Dosch S, Ho C. A proton nuclear magnetic resonance investigation of human hemoglobin A2. Implications on the intermolecular contacts in sickle hemoglobin fibers and on the Bohr effect of human normal adult hemoglobin. Biochimica Et Biophysica Acta. 785: 123-31. PMID 6704402 DOI: 10.1016/0167-4838(84)90136-5 |
0.35 |
|
| 1984 |
Dowd SR, Simplaceanu V, Ho C. Fluorine-19 nuclear magnetic resonance investigation of fluorine-19-labeled phospholipids. 2. A line-shape analysis Biochemistry. 23: 6142-6146. PMID 6525353 DOI: 10.1021/Bi00320A038 |
0.347 |
|
| 1984 |
Post JF, Cook BW, Dowd SR, Lowe IJ, Ho C. Fluorine-19 nuclear magnetic resonance investigation of fluorine-19-labeled phospholipids. 1. A multiple-pulse study. Biochemistry. 23: 6138-41. PMID 6525352 DOI: 10.1021/Bi00320A037 |
0.682 |
|
| 1984 |
Post JF, Cottam PF, Simplaceanu V, Ho C. Fluorine-19 nuclear magnetic resonance study of 5-fluorotryptophan-labeled histidine-binding protein J of Salmonella typhimurium. Journal of Molecular Biology. 179: 729-43. PMID 6389886 DOI: 10.1016/0022-2836(84)90164-5 |
0.673 |
|
| 1983 |
Hunt AG, Simplaceanu V, Hong JS, Ho C. Phosphorus-31 nuclear magnetic resonance investigation of membrane vesicles from Escherichia coli. Biochemistry. 22: 6130-6134. PMID 6318807 DOI: 10.1021/Bi00295A014 |
0.31 |
|
| 1983 |
Russu IM, Ho C. A proton nuclear magnetic resonance investigation of histidyl residues in sickle hemoglobin. Biochemistry. 21: 5044-51. PMID 6291599 DOI: 10.1021/Bi00263A030 |
0.375 |
|
| 1982 |
Ho C, Russu IM. Proton nuclear magnetic resonance investigation of hemoglobins. Methods in Enzymology. 76: 275-312. PMID 7329262 DOI: 10.1016/0076-6879(81)76128-7 |
0.359 |
|
| 1982 |
Takahashi S, Lin AKL, Ho C. A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket Biophysical Journal. 39: 33-40. PMID 7104448 DOI: 10.1016/S0006-3495(82)84487-1 |
0.393 |
|
| 1982 |
Engelsberg M, Dowd SR, Simplaceanu V, Cook BW, Ho C. Nuclear magnetic resonance line-shape analysis of fluorine-19-labeled phospholipids. Biochemistry. 21: 6985-9. PMID 6897614 DOI: 10.1021/Bi00269A056 |
0.353 |
|
| 1982 |
Russu IM, Ho NT, Ho C. A proton nuclear magnetic resonance investigation of histidyl residues in human normal adult hemoglobin Biochemistry. 21: 5031-5043. PMID 6291598 DOI: 10.1021/Bi00263A029 |
0.374 |
|
| 1980 |
Russu IM, Ho NT, Ho C. Role of the beta 146 histidyl residue in the alkaline Bohr effect of hemoglobin. Biochemistry. 19: 1043-52. PMID 7356961 DOI: 10.1021/Bi00546A033 |
0.312 |
|
| 1980 |
Ho C, Giza YH, Takahashi S, Ugen KE, Cottam PF, Dowd SR. A proton nuclear magnetic resonance investigation of histidine-binding protein J of Salmonella typhimurium: a model for transport of L-histidine across cytoplasmic membrane Journal of Supramolecular and Cellular Biochemistry. 13: 131-145. PMID 7017276 DOI: 10.1002/Jss.400130202 |
0.354 |
|
| 1980 |
Takahashi S, Lin KLCA, Ho C. Proton nuclear magnetic resonance studies of hemoglobins M Boston (alpha 58E7 His leads to Tyr) and M Milwaukee (beta 67E11 Val leads to Glu): spectral assignments of hyperfine-shifted proton resonances and of proximal histidine (E7) NH resonances to the alpha and beta chains of normal human adult hemoglobin. Biochemistry. 19: 5196-5202. PMID 6255985 DOI: 10.1021/Bi00564A007 |
0.352 |
|
| 1979 |
Viggiano G, Ho NT, Ho C. Proton nuclear magnetic resonance and biochemical studies of oxygenation of human adult hemoglobin in deuterium oxide Biochemistry. 18: 5238-5247. PMID 497180 DOI: 10.1021/Bi00590A031 |
0.363 |
|
| 1979 |
Viggiano G, Ho C. Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 76: 3673-3677. PMID 291032 DOI: 10.1073/Pnas.76.8.3673 |
0.369 |
|
| 1979 |
Sturtevant JM, Ho C, Reimann A. Thermotropic behavior of some fluorodimyristoylphosphatidylcholines. Proceedings of the National Academy of Sciences of the United States of America. 76: 2239-43. PMID 287065 DOI: 10.1073/pnas.76.5.2239 |
0.422 |
|
| 1978 |
Ho C, Fung LW, Wiechelman KJ. NMR of hemoproteins and iron-sulfur proteins. Methods in Enzymology. 54: 192-223. PMID 732571 DOI: 10.1016/S0076-6879(78)54016-0 |
0.349 |
|
| 1978 |
Johnson ME, Scholler DM, Hoffman BM, Ho C. Tertiary structure variability within the quaternary states of hemoglobin: a spin label study. Biochimica Et Biophysica Acta. 535: 193-205. PMID 678549 DOI: 10.1016/0005-2795(78)90085-5 |
0.303 |
|
| 1978 |
Viggiano G, Wiechelman KJ, Chervenick PA, Ho C. Proton nuclear magnetic resonance studies of hemoglobins Osler (beta145HC2 Tyr replaced by Asp) and McKee Rocks (beta145HC2 Tyr replaced by term): an assignment for an important tertiary structural probe in hemoglobin. Biochemistry. 17: 795-799. PMID 629932 DOI: 10.1021/Bi00598A007 |
0.386 |
|
| 1978 |
Wiechelman KJ, Fox J, McCurdy PR, Ho C. Proton nuclear magnetic resonance studies of hemoglobin Providence (beta82EF6 Lys replaced by Asn or Asp): a residue involved in anion binding. Biochemistry. 17: 791-795. PMID 629931 DOI: 10.1021/Bi00598A006 |
0.405 |
|
| 1978 |
Gent MPN, Cottam PF, Ho C. Fluorine-19 nuclear magnetic resonance studies of Escherichia coli membranes Proceedings of the National Academy of Sciences of the United States of America. 75: 630-634. PMID 345274 DOI: 10.1073/Pnas.75.2.630 |
0.32 |
|
| 1978 |
Perutz MF, Sanders JK, Chenery DH, Noble RW, Pennelly RR, Fung LW, Ho C, Giannini I, Pörschke D, Winkler H. Interactions between the quaternary structure of the globin and the spin state of the heme in ferric mixed spin derivatives of hemoglobin. Biochemistry. 17: 3640-52. PMID 210800 DOI: 10.1021/Bi00610A034 |
0.557 |
|
| 1977 |
Weatherall DJ, Clegg JB, Callender ST, Wells RM, Gale RE, Huehns ER, Perutz MF, Viggiano G, Ho C. Haemoglobin Radcliffe (alpha2beta299(Gi)Ala): a high oxygen-affinity variant causing familial polycythaemia. British Journal of Haematology. 35: 177-91. PMID 857849 DOI: 10.1111/J.1365-2141.1977.Tb00575.X |
0.318 |
|
| 1977 |
Fung LW, Minton AP, Lindstrom TR, Pisciotta AV, Ho C. Proton nuclear magnetic resonance studies of hemoglobin M Milwaukee and their implications concerning the mechanism of cooperative oxygenation of hemoglobin. Biochemistry. 16: 1452-62. PMID 849426 DOI: 10.1021/Bi00626A033 |
0.369 |
|
| 1977 |
Johnson ME, Fung LW, Ho C. Magnetic field and temperature induced line broadening in the hyperfine-shifted proton resonances of myoglobin and hemoglobin. Journal of the American Chemical Society. 99: 1245-50. PMID 833399 DOI: 10.1021/Ja00446A041 |
0.307 |
|
| 1977 |
Robertson DE, Kroon PA, Ho C. Nuclear magnetic resonance and fluorescence studies of substrate-induced conformational changes of histidine-binding protein J of Salmonella typhimurium. Biochemistry. 16: 1443-1451. PMID 321019 DOI: 10.1021/Bi00626A032 |
0.35 |
|
| 1977 |
Johnson ME, Fung LW-, Ho C. Magnetic Field And Temperature Induced Line Broadening In The Hyperfine-Shifted Proton Resonances Of Myoglobin And Hemoglobin Cheminform. 8. DOI: 10.1002/Chin.197719052 |
0.307 |
|
| 1976 |
Wiechelman KJ, Fairbanks VF, Ho C. Proton nuclear magnetic resonance studies of hemoglobin Malmö: implications of mutations at homologous positions of the alpha and beta chains. Biochemistry. 15: 1414-1420. PMID 1259945 DOI: 10.1021/Bi00652A010 |
0.392 |
|
| 1976 |
Fung LW, Minton AP, Ho C. Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 73: 1581-5. PMID 1064027 DOI: 10.1073/Pnas.73.5.1581 |
0.371 |
|
| 1976 |
Asakura T, Adachi K, Wiley JS, Fung LW, Ho C, Kilmartin JV, Perutz MF. Structure and function of haemoglobin Philly (Tyr C1 (35) β→Phe) Journal of Molecular Biology. 104: 185-195. PMID 957431 DOI: 10.1016/0022-2836(76)90008-5 |
0.363 |
|
| 1975 |
Fung LW, Ho C. A proton nuclear magnetic resonance study of the quaternary structure of human homoglobins in water. Biochemistry. 14: 2526-35. PMID 1138870 DOI: 10.1021/Bi00682A036 |
0.397 |
|
| 1975 |
Fung LW, Lin KL, Ho C. High-resolution proton nuclear magnetic resonance studies of sickle cell hemoglobin. Biochemistry. 14: 3424-30. PMID 238591 DOI: 10.1021/Bi00686A021 |
0.37 |
|
| 1974 |
Johnson ME, Ho C. Effects of ligands and organic phosphates on functional properties of human adult hemoglobin Biochemistry. 13: 3653-3661. PMID 4851759 DOI: 10.1021/Bi00715A005 |
0.323 |
|
| 1974 |
Wiechelman KJ, Charache S, Ho C. Nuclear magnetic resonance studies of hemoglobin Chesapeake: an alpha1beta2 mutant. Biochemistry. 13: 4772-4777. PMID 4429661 DOI: 10.1021/Bi00720A014 |
0.329 |
|
| 1973 |
Kreishman GP, Robertson DE, Ho C. PMR studies of the substrate induced conformational change of glutamine binding protein from E. coli. Biochemical and Biophysical Research Communications. 53: 18-23. PMID 4582370 DOI: 10.1016/0006-291X(73)91394-6 |
0.351 |
|
| 1972 |
Lindstrom TR, Ho C. Functional Nonequivalence of α and β Hemes in Human Adult Hemoglobin Proceedings of the National Academy of Sciences of the United States of America. 69: 1707-1710. PMID 4505648 DOI: 10.1073/Pnas.69.7.1707 |
0.328 |
|
| 1972 |
Lindstrom TR, Ho C, Pisciotta AV. Nuclear Magnetic Resonance Studies of Haemoglobin M Milwaukee Nature. 237: 263-264. PMID 4504457 DOI: 10.1038/Newbio237263A0 |
0.322 |
|
| 1971 |
Davis DG, Lindstrom TR, Mock NH, Baldassare JJ, Charache S, Jones RT, Ho C. Nuclear magnetic resonance studies of hemoglobins. VI. Heme proton spectra of human deoxyhemoglobins and their relevance to the nature of co-operative oxygenation of hemoglobin. Journal of Molecular Biology. 60: 101-11. PMID 5572098 DOI: 10.1016/0022-2836(71)90450-5 |
0.322 |
|
| 1971 |
Kurland RJ, Little RG, Davis DG, Ho C. Proton magnetic resonance study of high- and low-spin hemin derivatives. Biochemistry. 10: 2237-46. PMID 5114986 DOI: 10.1021/Bi00788A009 |
0.313 |
|
| 1970 |
Davis DG, Mock NH, Lindstrom TR, Charache S, Ho C. Nuclear magnetic resonance studies of hemoglobiss. V. The heme proton spectra of human deoxyhemoglobins A, F, Zurich, and Chesapeake. Biochemical and Biophysical Research Communications. 40: 343-9. PMID 5482264 DOI: 10.1016/0006-291X(70)91015-6 |
0.358 |
|
| 1970 |
Ho C, Davis DG, Mock NH, Lindstrom TR, Charache S. Nuclear magnetic resonance studies of hemoglobin. IV. The structure-function relationship of human adult hemoglobins A and Chesapeake and its implication to the nature of oxygenation of hemoglobin. Biochemical and Biophysical Research Communications. 38: 779-86. PMID 5443718 DOI: 10.1016/0006-291X(70)90649-2 |
0.352 |
|
| 1970 |
Ho C, Baldassare JJ, Charache S. Electron paramagnetic resonance studies of spin-labeled hemoglobins and their implications to the nature of cooperative oxygen binding to hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 66: 722-9. PMID 4316679 DOI: 10.1073/Pnas.66.3.722 |
0.389 |
|
| 1969 |
Ho C, Magnuson JA, Wilson JB, Magnuson NS, Kurland RJ. Phosphorus nuclear magnetic resonance studies of phosphoproteins and phosphorylated molecules. II. Chemical nature of phosphorus atoms in alpha S-casein B and phosvitin. Biochemistry. 8: 2074-2082. PMID 5814938 DOI: 10.1021/Bi00833A044 |
0.304 |
|
| 1969 |
Davis DG, Mock NL, Laman VR, Ho C. Nuclear magnetic resonance studies of hemoglobins. Journal of Molecular Biology. 40: 311-3. PMID 5391787 DOI: 10.1016/0022-2836(69)90480-X |
0.321 |
|
| 1969 |
Davis DG, Charache S, Ho C. Nuclear magnetic resonance studies of hemoglobins. 3. Evidence for the nonequivalence of alpha- and beta-hains in azide derivativeof methemoglobins. Proceedings of the National Academy of Sciences of the United States of America. 63: 1403-9. PMID 5260944 DOI: 10.1073/Pnas.63.4.1403 |
0.335 |
|
| 1968 |
Kurland RJ, Davis DG, Ho C. Paramagnetic proton nuclear magnetic resonance shifts of metmyoglobin, methemoglobin, and hemin derivatives. Journal of the American Chemical Society. 90: 2700-1. PMID 5651073 DOI: 10.1021/Ja01012A048 |
0.332 |
|
| 1965 |
HO C, WAUGH DF. INTERACTIONS OF BOVINE CASEINS WITH DIVALENT CATIONS. Journal of the American Chemical Society. 87: 889-92. PMID 14284618 DOI: 10.1021/Ja01082A033 |
0.576 |
|
| 1965 |
Ho C, Waugh DF. Interactions of bovine alpha-s-casein with small ions. Journal of the American Chemical Society. 87: 110-7. PMID 5826969 DOI: 10.1021/Ja01079A020 |
0.581 |
|
| 1963 |
HO C, STURTEVANT JM. THE KINETICS OF THE HYDRATION OF CARBON DIOXIDE AT 25 DEGREES. The Journal of Biological Chemistry. 238: 3499-501. PMID 14085408 |
0.399 |
|
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