Year |
Citation |
Score |
2013 |
Fago A, Crumbliss AL, Hendrich MP, Pearce LL, Peterson J, Henkens R, Bonaventura C. Oxygen binding to partially nitrosylated hemoglobin. Biochimica Et Biophysica Acta. 1834: 1894-900. PMID 23624264 DOI: 10.1016/J.Bbapap.2013.04.017 |
0.415 |
|
2013 |
Bonaventura C, Henkens R, Alayash AI, Banerjee S, Crumbliss AL. Molecular controls of the oxygenation and redox reactions of hemoglobin. Antioxidants & Redox Signaling. 18: 2298-313. PMID 23198874 DOI: 10.1089/Ars.2012.4947 |
0.391 |
|
2012 |
Banerjee S, Jia Y, Siburt CJ, Abraham B, Wood F, Bonaventura C, Henkens R, Crumbliss AL, Alayash AI. Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions. Free Radical Biology & Medicine. 53: 1317-26. PMID 22841869 DOI: 10.1016/J.Freeradbiomed.2012.07.023 |
0.429 |
|
2011 |
Bonaventura C, Henkens R, Friedman J, Siburt CJ, Kraiter D, Crumbliss AL. Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins. Biochimica Et Biophysica Acta. 1814: 1261-8. PMID 21745602 DOI: 10.1016/J.Bbapap.2011.06.012 |
0.468 |
|
2010 |
Bonaventura C, Henkens R, De Jesus-Bonilla W, Lopez-Garriga J, Jia Y, Alayash AI, Siburt CJ, Crumbliss AL. Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite. Biochimica Et Biophysica Acta. 1804: 1988-95. PMID 20601225 DOI: 10.1016/J.Bbapap.2010.06.016 |
0.351 |
|
2007 |
Bonaventura C, Henkens R, Alayash AI, Crumbliss AL. Allosteric effects on oxidative and nitrosative reactions of cell-free hemoglobins. Iubmb Life. 59: 498-505. PMID 17701544 DOI: 10.1080/15216540601188546 |
0.361 |
|
2007 |
Remington N, Stevens RD, Wells RS, Holn A, Dhungana S, Taboy CH, Crumbliss AL, Henkens R, Bonaventura C. Genetic diversity of coastal bottlenose dolphins revealed by structurally and functionally diverse hemoglobins. Gene. 398: 123-31. PMID 17604574 DOI: 10.1016/J.Gene.2007.02.050 |
0.479 |
|
2005 |
Bonaventura C, Godette G, Stevens R, Brenowitz M, Henkens R. Overproduction of alpha chains provides a proton-insensitive component to the bluefish hemoglobin system. The Journal of Biological Chemistry. 280: 40509-14. PMID 16166086 DOI: 10.1074/Jbc.M505353200 |
0.369 |
|
2004 |
Bonaventura C, Fago A, Henkens R, Crumbliss AL. Critical redox and allosteric aspects of nitric oxide interactions with hemoglobin. Antioxidants & Redox Signaling. 6: 979-91. PMID 15548895 DOI: 10.1089/Ars.2004.6.979 |
0.359 |
|
2004 |
Bonaventura C, Crumbliss AL, Weber RE. New insights into the proton-dependent oxygen affinity of Root effect haemoglobins. Acta Physiologica Scandinavica. 182: 245-58. PMID 15491404 DOI: 10.1111/J.1365-201X.2004.01359.X |
0.411 |
|
2004 |
Peterson ES, Shinder R, Khan I, Juczszak L, Wang J, Manjula B, Acharya SA, Bonaventura C, Friedman JM. Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways. Biochemistry. 43: 4832-43. PMID 15096052 DOI: 10.1021/Bi035481O |
0.397 |
|
2003 |
Fago A, Crumbliss AL, Peterson J, Pearce LL, Bonaventura C. The case of the missing NO-hemoglobin: spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry. Proceedings of the National Academy of Sciences of the United States of America. 100: 12087-92. PMID 14514887 DOI: 10.1073/Pnas.2032603100 |
0.363 |
|
2003 |
Christensen AB, Colacino JM, Bonaventura C. Functional and biochemical properties of the hemoglobins of the burrowing brittle star Hemipholis elongata say (Echinodermata, Ophiuroidea). The Biological Bulletin. 205: 54-65. PMID 12917222 DOI: 10.2307/1543445 |
0.464 |
|
2002 |
Chen Q, Bonaventura C, Nagel RL, Hirsch RE. Distinct domain responses of R-state human hemoglobins A, C, and S to anions. Blood Cells, Molecules & Diseases. 29: 119-32. PMID 12482413 DOI: 10.1006/Bcmd.2002.0546 |
0.413 |
|
2002 |
Bonaventura C, Godette G, Ferruzzi G, Tesh S, Stevens RD, Henkens R. Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease. Biophysical Chemistry. 98: 165-81. PMID 12128197 DOI: 10.1016/S0301-4622(02)00092-3 |
0.423 |
|
2002 |
Gladwin MT, Wang X, Reiter CD, Yang BK, Vivas EX, Bonaventura C, Schechter AN. S-Nitrosohemoglobin is unstable in the reductive erythrocyte environment and lacks O2/NO-linked allosteric function. The Journal of Biological Chemistry. 277: 27818-28. PMID 12023289 DOI: 10.1074/Jbc.M203236200 |
0.405 |
|
2002 |
Bonaventura C, Taboy CH, Low PS, Stevens RD, Lafon C, Crumbliss AL. Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: implications for interactions of nitric oxide with normal and sickle red blood cells. The Journal of Biological Chemistry. 277: 14557-63. PMID 11834726 DOI: 10.1074/Jbc.M107658200 |
0.336 |
|
2002 |
Juszczak LJ, Manjula B, Bonaventura C, Acharya SA, Friedman JM. UV resonance Raman study of beta93-modified hemoglobin A: chemical modifier-specific effects and added influences of attached poly(ethylene glycol) chains. Biochemistry. 41: 376-85. PMID 11772037 DOI: 10.1021/Bi011212R |
0.38 |
|
2001 |
Khan I, Dantsker D, Samuni U, Friedman AJ, Bonaventura C, Manjula B, Acharya SA, Friedman JM. Beta 93 modified hemoglobin: kinetic and conformational consequences. Biochemistry. 40: 7581-92. PMID 11412112 DOI: 10.1021/Bi010051O |
0.373 |
|
2000 |
Taboy CH, Faulkner KM, Kraiter D, Bonaventura C, Crumbliss AL. Concentration-dependent effects of anions on the anaerobic oxidation of hemoglobin and myoglobin. The Journal of Biological Chemistry. 275: 39048-54. PMID 10984477 DOI: 10.1074/Jbc.M004547200 |
0.411 |
|
1999 |
Topham R, Tesh S, Westcott A, Cole G, Mercatante D, Kaufman G, Bonaventura C. Disulfide bond reduction: A powerful, chemical probe for the study of structure-function relationships in the hemocyanins. Archives of Biochemistry and Biophysics. 369: 261-6. PMID 10486145 DOI: 10.1006/Abbi.1999.1367 |
0.437 |
|
1999 |
Bonaventura C, Ferruzzi G, Tesh S, Stevens RD. Effects of S-nitrosation on oxygen binding by normal and sickle cell hemoglobin. The Journal of Biological Chemistry. 274: 24742-8. PMID 10455144 DOI: 10.1074/Jbc.274.35.24742 |
0.442 |
|
1999 |
Taboy CH, Bonaventura C, Crumbliss AL. Spectroelectrochemistry of heme proteins: effects of active-site heterogeneity on Nernst plots. Bioelectrochemistry and Bioenergetics (Lausanne, Switzerland). 48: 79-86. PMID 10228573 DOI: 10.1016/S0302-4598(98)00236-0 |
0.39 |
|
1999 |
Bonaventura C, Godette G, Tesh S, Holm DE, Bonaventura J, Crumbliss AL, Pearce LL, Peterson J. Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide. The Journal of Biological Chemistry. 274: 5499-507. PMID 10026163 DOI: 10.1074/Jbc.274.9.5499 |
0.561 |
|
1998 |
Topham R, Tesh S, Cole G, Mercatante D, Westcott A, Bonaventura C. Active-site disruption in native Limulus hemocyanin and its subunits by disulfide-bond reductants: a chemical probe for the study of structure-function relationships in the hemocyanins. Archives of Biochemistry and Biophysics. 352: 103-13. PMID 9521822 DOI: 10.1006/Abbi.1998.0574 |
0.469 |
|
1998 |
Bonaventura C, Tesh S, Faulkner KM, Kraiter D, Crumbliss AL. Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and Deer Lodge beta2(NA2)His --> Arg. Biochemistry. 37: 496-506. PMID 9425070 DOI: 10.1021/Bi971574S |
0.415 |
|
1997 |
Hahn JS, Braun RD, Dewhirst MW, Shan S, Snyder SA, Taube JM, Ong ET, Rosner GL, Dodge RK, Bonaventura J, Bonaventura C, Deangelo J, Meyer RE. Stroma-free human hemoglobin A decreases R3230Ac rat mammary adenocarcinoma blood flow and oxygen partial pressure Radiation Research. 147: 185-194. PMID 9008211 DOI: 10.2307/3579420 |
0.518 |
|
1996 |
Hazes B, Magnus KA, Kalk KH, Bonaventura C, Hol WG. Nitrate binding to Limulus polyphemus subunit type II hemocyanin and its functional implications. Journal of Molecular Biology. 262: 532-41. PMID 8893861 DOI: 10.1006/Jmbi.1996.0533 |
0.49 |
|
1996 |
Holm DE, Godette G, Bonaventura C, Bonaventura J, Boatright MD, Pearce LL, Peterson J. A carbon monoxide irredubicle form of cytochrome c oxidase and other unusual properties of the 'monomeric' shark enzyme Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 114: 345-352. PMID 8840511 DOI: 10.1016/0305-0491(96)00031-4 |
0.586 |
|
1996 |
Swerdlow RD, Ebert RF, Lee P, Bonaventura C, Miller KI. Keyhole limpet hemocyanin: structural and functional characterization of two different subunits and multimers. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 113: 537-48. PMID 8829804 DOI: 10.1016/0305-0491(95)02091-8 |
0.409 |
|
1996 |
Jia L, Bonaventura C, Bonaventura J, Stamler JS. S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control Nature. 380: 221-226. PMID 8637569 DOI: 10.1038/380221A0 |
0.547 |
|
1996 |
Mylvaganam SE, Bonaventura C, Bonaventura J, Getzoff ED. Structural basis for the root effect in haemoglobin. Nature Structural Biology. 3: 275-83. PMID 8605630 DOI: 10.1038/Nsb0396-275 |
0.587 |
|
1995 |
Faulkner KM, Bonaventura C, Crumbliss AL. A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins. The Journal of Biological Chemistry. 270: 13604-12. PMID 7775411 DOI: 10.1074/Jbc.270.23.13604 |
0.429 |
|
1995 |
Holm DE, Godette G, Bonaventura J, Bonaventura C, Peterson J. The site of the redox-linked proton pump in eukaryotic cytochrome c oxidases. Febs Letters. 370: 53-8. PMID 7649304 DOI: 10.1016/0014-5793(95)00791-7 |
0.59 |
|
1994 |
Bonaventura C, Arumugam M, Cashon R, Bonaventura J, Moo-Penn WF. Chloride masks effects of opposing positive charges in Hb A and Hb Hinsdale (beta 139 Asn-->Lys) that can modulate cooperativity as well as oxygen affinity. Journal of Molecular Biology. 239: 561-8. PMID 8006968 DOI: 10.1006/jmbi.1994.1395 |
0.619 |
|
1994 |
Magnus KA, Hazes B, Ton-That H, Bonaventura C, Bonaventura J, Hol WGJ. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences Proteins: Structure, Function and Genetics. 19: 302-309. PMID 7984626 DOI: 10.1002/Prot.340190405 |
0.625 |
|
1994 |
Stevens RD, Bonaventura J, Bonaventura C, Fennel TR, Millington DS. Application of electrospray ionization mass spectrometry for analysis of haemoglobin adducts with acrylonitrile. Biochemical Society Transactions. 22: 543-7. PMID 7958363 DOI: 10.1042/Bst0220543 |
0.486 |
|
1994 |
Bonaventura C, Bonaventura J, Stevens R, Millington D. Acrylamide in Polyacrylamide Gels Can Modify Proteins during Electrophoresis Analytical Biochemistry. 222: 44-48. PMID 7856869 DOI: 10.1006/Abio.1994.1451 |
0.57 |
|
1994 |
Bonilla GO, Focesi Júnior A, Bonaventura C, Bonaventura J, Cashon RE. Functional properties of the hemoglobin from the South American snake Mastigodryas bifossatus. Comparative Biochemistry and Physiology. Part a, Physiology. 109: 1085-95. PMID 7828024 DOI: 10.1016/0300-9629(94)90258-5 |
0.647 |
|
1994 |
Faulkner KM, Bonaventura C, Crumbliss AL. A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins Inorganica Chimica Acta. 226: 187-194. DOI: 10.1016/0020-1693(94)04086-9 |
0.406 |
|
1993 |
Hazes B, Magnus KA, Bonaventura C, Bonaventura J, Dauter Z, Kalk KH, Hol WG. Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation. Protein Science : a Publication of the Protein Society. 2: 597-619. PMID 8518732 DOI: 10.1002/Pro.5560020411 |
0.618 |
|
1993 |
Alayash AI, Fratantoni JC, Bonaventura C, Bonaventura J, Cashon RE. Nitric oxide binding to human ferrihemoglobins cross-linked between either alpha or beta subunits. Archives of Biochemistry and Biophysics. 303: 332-8. PMID 8512319 DOI: 10.1006/Abbi.1993.1292 |
0.638 |
|
1993 |
Topham R, Tesh S, Dilzer S, Bonaventura C, Bonaventura J. Active-site heterogeneity in subunits of horseshoe crab hemocyanin (Limulus polyphemus). Journal of Inorganic Biochemistry. 51: 208. DOI: 10.1016/0162-0134(93)85244-3 |
0.537 |
|
1992 |
Bonaventura C, Cashon R, Colacino JM, Hilderman RH. Alteration of hemoglobin function by diadenosine 5',5'''-P1,P4-tetraphosphate and other alarmones. The Journal of Biological Chemistry. 267: 4652-7. PMID 1537848 |
0.382 |
|
1992 |
Alayash AI, Fratantoni JC, Bonaventura C, Bonaventura J, Bucci E. Consequences of chemical modifications on the free radical reactions of human hemoglobin. Archives of Biochemistry and Biophysics. 298: 114-20. PMID 1524419 DOI: 10.1016/0003-9861(92)90101-2 |
0.615 |
|
1992 |
Alayash AI, Ryan BA, Fratantoni JC, Bonaventura J, Bonaventura C. Hemoglobin-based oxygen carriers (HBOCs): structural alterations that affect free radical generation. Biomaterials, Artificial Cells, and Immobilization Biotechnology : Official Journal of the International Society For Artificial Cells and Immobilization Biotechnology. 20: 277-81. PMID 1391442 |
0.527 |
|
1991 |
Boffi A, Bonaventura C, Bonaventura J, Cashon R, Chiancone E. Oxidized dimeric Scapharca inaequivalvis. Co-driven perturbation of the redox equilibrium. The Journal of Biological Chemistry. 266: 17898-903. PMID 1917929 |
0.588 |
|
1991 |
Bonaventura C, Cashon R, Bonaventura J, Perutz M, Fermi G, Shih DTB. Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lysβ66 → Thr) and its isolated β chains Journal of Biological Chemistry. 266: 23033-23040. PMID 1744099 |
0.613 |
|
1989 |
Ogo S, Focesi A, Cashon R, Bonaventura J, Bonaventura C. Interactions of nicotinamide adenine dinucleotides with varied states and forms of hemoglobin. The Journal of Biological Chemistry. 264: 11302-6. PMID 2738066 |
0.63 |
|
1988 |
Topham R, Cooper B, Tesh S, Godette G, Bonaventura C, Bonaventura J. Isolation, purification and characterization of an iron-binding protein from the horseshoe crab (Limulus polyphemus). The Biochemical Journal. 252: 151-7. PMID 3421898 DOI: 10.1042/Bj2520151 |
0.573 |
|
1988 |
Topham RW, Tesh S, Bonaventura C, Bonaventura J. Active-site heterogeneity in Limulus hemocyanin as revealed by reaction with peroxides. Archives of Biochemistry and Biophysics. 261: 299-311. PMID 3355153 DOI: 10.1016/0003-9861(88)90345-1 |
0.596 |
|
1988 |
Johnson BA, Bonaventura C, Bonaventura J. Allostery in Callinectes sapidus hemocyanin: Cooperative oxygen binding and interactions with L-lactate, calcium, and protons Biochemistry. 27: 1995-2001. PMID 2837279 |
0.563 |
|
1988 |
CRUMBLISS AL, GARRISON JM, BOCK CR, SCHAAF A, BONAVENTURA CJ, BONAVENTURA J. ChemInform Abstract: Synthesis and Characterization of Iron(III) Chelating Analogs of Siderophores on Organic Solid Supports. Cheminform. 19. DOI: 10.1002/chin.198805307 |
0.454 |
|
1987 |
Johnson BA, Bonaventura J, Bonaventura C. Determination of l-lactate binding stoichiometry and differences in allosteric interactions of structurally distinct homohexamers from Panulirus interruptus hemocyanin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 916: 376-380. PMID 3689798 DOI: 10.1016/0167-4838(87)90183-X |
0.662 |
|
1987 |
Ogo SH, Focesi Júnior A, Cashon R, Bonaventura C, Bonaventura J. Fluorescence studies on the binding of reduced nicotinamide adenine dinucleotide phosphate to human hemoglobin A and its variant hemoglobin Providence. Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Medicas E Biologicas. 20: 755-8. PMID 3455253 |
0.595 |
|
1987 |
L. Crumbliss A, Garrison JM, Bock CR, Schaaf A, Bonaventura CJ, Bonaventura J. Synthesis and characterization of iron(llI) chelating analogues of siderophores on organic solid supports Inorganica Chimica Acta. 133: 281-287. DOI: 10.1016/S0020-1693(00)87780-4 |
0.497 |
|
1986 |
Cashon R, Bonaventura C, Bonaventura J, Focesi A. The nicotinamide adenine dinucleotides as allosteric effectors of human hemoglobin. The Journal of Biological Chemistry. 261: 12700-5. PMID 3745207 |
0.643 |
|
1986 |
Fushitani K, Bonaventura J, Bonaventura C. Isolation of polypeptide chains with heme from the extracellular hemoglobin of Amphitrite ornata (Polychaeta, Annelida). Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 84: 137-41. PMID 3720289 DOI: 10.1016/0305-0491(86)90283-X |
0.578 |
|
1985 |
Kempter B, Markl J, Brenowitz M, Bonaventura C, Bonaventura J. Immunological correspondence between arthropod hemocyanin subunits. II. Xiphosuran (Limulus) and spider (Eurypelma, Cupiennius) hemocyanin. Biological Chemistry Hoppe-Seyler. 366: 77-86. PMID 4005039 DOI: 10.1515/Bchm3.1985.366.1.77 |
0.547 |
|
1985 |
Sugihara J, Imamura T, Nagafuchi S, Bonaventura J, Bonaventura C, Cashon R. Hemoglobin Rahere, a human hemoglobin variant with amino acid substitution at the 2,3-diphosphoglycerate binding site. Functional consequences of the alteration and effects of bezafibrate on the oxygen bindings. The Journal of Clinical Investigation. 76: 1169-73. PMID 3930571 DOI: 10.1172/Jci112072 |
0.664 |
|
1985 |
Brunori M, Bickar D, Bonaventura J, Bonaventura C. Kinetics of reduction of cytochrome c oxidase by dithionite and the effect of hydrogen peroxide. The Journal of Biological Chemistry. 260: 7165-7. PMID 2987245 |
0.522 |
|
1985 |
Bickar D, Lehninger A, Brunori M, Bonaventura J, Bonaventura C. Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase. Journal of Inorganic Biochemistry. 23: 365-72. PMID 2410569 DOI: 10.1016/0162-0134(85)85047-9 |
0.605 |
|
1985 |
Terwilliger R, Terwilliger N, Bonaventura C, Bonaventura J, Schabtach E. Structural and functional properties of hemoglobin from the vestimentiferan Pogonophora, Lamellibrachia Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 829: 27-33. DOI: 10.1016/0167-4838(85)90064-0 |
0.62 |
|
1984 |
Brenowitz M, Bonaventura C, Bonaventura J. Comparison of the physical and functional properties of the 48-subunit native molecule and the 24- and 12-subunit dissociation intermediates of Limulus polyphemus hemocyanin. Biochemistry. 23: 879-88. PMID 25856834 DOI: 10.1021/Bi00300A014 |
0.625 |
|
1984 |
Johnson BA, Bonaventura C, Bonaventura J. Allosteric modulation of Callinectes sapidus hemocyanin by binding of L-lactate Biochemistry. 23: 872-878. PMID 25856833 DOI: 10.1021/Bi00300A013 |
0.651 |
|
1984 |
Brenowitz M, Bonaventura C, Bonaventura J. Self-association and oxygen-binding characteristics of the isolated subunits of Limulus polyphemus hemocyanin. Archives of Biochemistry and Biophysics. 230: 238-49. PMID 6712235 DOI: 10.1016/0003-9861(84)90105-X |
0.661 |
|
1984 |
Shih T, Jones RT, Bonaventura J, Bonaventura C, Schneider RG. Involvement of His HC3 (146) beta in the Bohr effect of human hemoglobin. Studies of native and N-ethylmaleimide-treated hemoglobin A and hemoglobin Cowtown (beta 146 His replaced by Leu). The Journal of Biological Chemistry. 259: 967-74. PMID 6693406 |
0.601 |
|
1984 |
Bickar D, Bonaventura J, Bonaventura C, Auer H, Wilson M. Paradoxical effects of methylmercury on the kinetics of cytochrome c oxidase. Biochemistry. 23: 680-4. PMID 6324852 DOI: 10.1021/Bi00299A015 |
0.571 |
|
1984 |
Bonaventura C, Bonaventura J, Hooper IR, Marshall T. Underwater life support based on immobilized oxygen carriers. Applied Biochemistry and Biotechnology. 9: 65-80. PMID 6148039 DOI: 10.1007/Bf02798375 |
0.618 |
|
1984 |
Bickar D, Bonaventura C, Bonaventura J. Carbon monoxide-driven reduction of ferric heme and heme proteins. The Journal of Biological Chemistry. 259: 10777-83. PMID 6088517 |
0.605 |
|
1983 |
Brouwer M, Bonaventura C, Bonaventura J. Metal ion interactions with Limulus polyphemus and Callinectes sapidus hemocyanins: Stoichiometry and structural and functional consequences of calcium(II), cadmium(II), zinc(II), and mercury(II) binding Biochemistry. 22: 4713-4723. PMID 6626526 DOI: 10.1021/Bi00289A016 |
0.626 |
|
1983 |
Brenowitz M, Bonaventura C, Bonaventura J. Assembly and calcium-induced cooperativity of Limulus IV hemocyanin: a model system for analysis of structure-function relationships in the absence of subunit heterogeneity. Biochemistry. 22: 4707-13. PMID 6626525 DOI: 10.1021/Bi00289A015 |
0.623 |
|
1983 |
Brenowitz MD, Bonaventura J, Bonaventura C. Chapter 9.8 Haemocyanins Journal of Chromatography Library. 18: 156-160. DOI: 10.1016/S0301-4770(08)61314-7 |
0.549 |
|
1982 |
Bonaventura J, Bonaventura C, Brouwer M. Effects of heavy metals on the respiratory proteins of marine organisms in relation to environmental pollution Advances in Experimental Medicine and Biology. 148: 75-83. PMID 7124531 DOI: 10.1007/978-1-4615-9281-5_7 |
0.504 |
|
1982 |
Brouwer M, Bonaventura C, Bonaventura J. Heavy metal ion interactions with Callinectes sapidus hemocyanin: Structural and functional changes induced by a variety of heavy metal ions Biochemistry. 21: 2529-2538. PMID 7093201 DOI: 10.1021/Bi00539A037 |
0.652 |
|
1982 |
Brouwer M, Bonaventura C, Bonaventura J. Chloride and pH dependence of cooperative interactions in Limulus polyphemus hemocyanin Progress in Clinical and Biological Research. 81: 231-256. PMID 6289351 |
0.505 |
|
1982 |
Bickar D, Bonaventura J, Bonaventura C. Cytochrome c oxidase binding of hydrogen peroxide. Biochemistry. 21: 2661-6. PMID 6284205 DOI: 10.1021/Bi00540A013 |
0.635 |
|
1981 |
Bonaventura J, Bonaventura C. Preparation of high molecular weight invertebrate hemoglobins. Methods in Enzymology. 76: 43-54. PMID 7329268 DOI: 10.1016/0076-6879(81)76113-5 |
0.597 |
|
1981 |
Bonaventura C, Bonaventura J, Miller KI, Van Holde KE. Hemocyanin of the chambered Nautilus: Structure-function relationships Archives of Biochemistry and Biophysics. 211: 589-598. PMID 7305390 DOI: 10.1016/0003-9861(81)90493-8 |
0.677 |
|
1981 |
Brenowitz M, Bonaventura C, Bonaventura J, Gianazza E. Subunit composition of high molecular weight oligomer: Limulus polyphemus hemocyanin. Archives of Biochemistry and Biophysics. 210: 748-61. PMID 7305358 DOI: 10.1016/0003-9861(81)90242-3 |
0.584 |
|
1981 |
Chiancone E, Ferruzzi G, Bonaventura C, Bonaventura J. Amphitrite ornata erythrocruorin II. Molecular controls of function Bba - Protein Structure. 670: 84-92. PMID 7272332 DOI: 10.1016/0005-2795(81)90052-0 |
0.66 |
|
1981 |
Markl J, Bonaventura C, Bonaventura J. Hemocyanins in spiders, XIII. Kinetics of oxygen dissociation from individual subunits of Eurypelma and Cupiennius hemocyanin. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 362: 429-37. PMID 7239442 DOI: 10.1515/Bchm2.1981.362.1.429 |
0.615 |
|
1981 |
Brouwer M, Bonaventura C, Bonaventura J. Effect of oxygen and allosteric effectors on structural stability of oligomeric hemocyanins of the arthropod, Limulus polyphemus, and the mollusc, Helix pomatia Biochemistry. 20: 1842-1848. PMID 7225359 DOI: 10.1021/Bi00510A020 |
0.663 |
|
1980 |
Bonaventura C, Bonaventura J, Brouwer M. Assembly processes in oligomers containing structurally distinct subunits: respiratory proteins as models. Biophysical Journal. 32: 429-31. PMID 19431381 DOI: 10.1016/S0006-3495(80)84969-1 |
0.641 |
|
1980 |
Bonaventura C, Bonaventura J. Competition in oxygen-linked anion binding to normal and variant human hemoglobins. Hemoglobin. 4: 275-89. PMID 7419423 DOI: 10.3109/03630268008996210 |
0.635 |
|
1980 |
Poyart C, Bursaux E, Arnone A, Bonaventura J, Bonaventura C. Structural and functional studies of hemoglobin Suresnes (arg 141 alpha 2 replaced by His beta 2). Consequences of disrupting an oxygen-linked anion-binding site. The Journal of Biological Chemistry. 255: 9465-73. PMID 7410435 |
0.644 |
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1980 |
Lamy J, Lamy J, Bonaventura J, Bonaventura C. Structure, function, and assembly in the hemocyanin system of the scorpion, Androctonus australis. Biochemistry. 19: 3033-9. PMID 7397116 DOI: 10.1021/Bi00554A031 |
0.521 |
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1980 |
Chiancone E, Brenowitz M, Ascoli F, Bonaventura C, Bonaventura J. Amphitrite ornata erythrocruorin. I. Structural properties and characterization of subunit interactions. Biochimica Et Biophysica Acta. 623: 146-62. PMID 7378469 DOI: 10.1016/0005-2795(80)90017-3 |
0.617 |
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1980 |
Wilson MT, Lalla-Maharajh W, Darley-Usmar V, Bonaventura J, Bonaventura C, Brunori M. Structural and functional properties of cytochrome c oxidases isolated from sharks. The Journal of Biological Chemistry. 255: 2722-8. PMID 6244291 |
0.497 |
|
1980 |
BONAVENTURA J, BONAVENTURA C. Hemocyanins Relationships in Their Structure, Function and Assembly American Zoologist. 20: 7-17. DOI: 10.1093/Icb/20.1.7 |
0.658 |
|
1980 |
BONAVENTURA C, BONAVENTURA J. Anionic Control of Function in Vertebrate Hemoglobins American Zoologist. 20: 131-138. DOI: 10.1093/Icb/20.1.131 |
0.644 |
|
1980 |
Focesi A, Ogo SH, Bonaventura C, Bonaventura J. Kinetics of oxygen and carbon monoxide binding to the hemoglobins of the water snakes Liophis miliaris and Helicops modestus Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 67: 555-559. DOI: 10.1016/0305-0491(80)90414-9 |
0.657 |
|
1979 |
Terwilliger NB, Terwilliger RC, Applestein M, Bonaventura C, Bonaventura J. Subunit structure and oxygen binding by hemocyanin of the isopod Ligia exotica. Biochemistry. 18: 102-8. PMID 420767 DOI: 10.1021/Bi00568A016 |
0.66 |
|
1979 |
Lamy J, Lamy J, Weill J, Bonaventura J, Bonaventura C, Brenowitz M. Immunological correlates between the multiple hemocyanin subunits of Limulus polyphemus and Techypleus tridentatus. Archives of Biochemistry and Biophysics. 196: 324-39. PMID 90479 DOI: 10.1016/0003-9861(79)90585-X |
0.603 |
|
1979 |
Atha DH, Riggs A, Bonaventura J, Bonaventura C. Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. pH dependence of ligand binding and subunit dissociation equilibria and kinetics. The Journal of Biological Chemistry. 254: 3393-400. PMID 34618 |
0.603 |
|
1978 |
Bonaventura C, Bonaventura J, Brunori M, Wilson M. Functional studies on crosslinked bovine cytochrome c oxidase. Febs Letters. 85: 30-4. PMID 202495 DOI: 10.1016/0014-5793(78)81241-1 |
0.545 |
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1978 |
Brouwer M, Ryan M, Bonaventura J, Bonaventura C. Functional and structural properties of murex fulvescens hemocyanin: Isolation of two different subunits required for reassociation of a molluscan hemocyanin Biochemistry. 17: 2810-2815. PMID 28744 DOI: 10.1021/Bi00607A017 |
0.649 |
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1978 |
Brouwer M, Bonaventura C, Bonaventura J. Analysis of the effect of three different allosteric ligands on oxygen binding by hemocyanin of the shrimp, Penaeus setiferus Biochemistry. 17: 2148-2154. PMID 27208 DOI: 10.1021/Bi00604A019 |
0.653 |
|
1978 |
Bucci E, Salahuddin A, Bonaventura J, Bonaventura C. Characterization of the ionizable groups interacting with anionic allosteric effectors of human hemoglobin Journal of Biological Chemistry. 253: 821-827. PMID 23382 |
0.577 |
|
1978 |
Pandolfelli ER, Bonaventura C, Bonaventura J, Brunori M. Light-Jump Perturbation of Carbon Monoxide Binding by Various Heme Proteins Biophysical Journal. 24: 257. DOI: 10.1016/S0006-3495(78)85369-7 |
0.572 |
|
1978 |
Sekino T, Focesi A, Bonaventura C, Bonaventura J. Functional properties of Aplysia brasiliana myoglobin Comparative Biochemistry and Physiology Part a: Physiology. 61: 223-226. DOI: 10.1016/0300-9629(78)90101-9 |
0.665 |
|
1978 |
Weber SE, Bonaventura J, Sullivan B, Bonaventura C. Oxygen equilibria and ligand-binding kinetics of erythrocruorins from two burrowing polychaetes of different modes of life, Marphysa sanguinea and Diopatra cuprea Journal of Comparative Physiology □ B. 123: 177-184. DOI: 10.1007/Bf00687847 |
0.638 |
|
1977 |
Amiconi G, Bonaventura C, Bonaventura J, Antonini E. Functional properties of normal and sickle cell hemoglobins in polyethylene glycol 6000. Biochimica Et Biophysica Acta. 495: 279-86. PMID 22353 DOI: 10.1016/0005-2795(77)90384-1 |
0.568 |
|
1977 |
Terwilliger RC, Terwilliger NB, Bonaventura C, Bonaventura J. Oxygen binding domains of Helisoma trivolvis hemoglobin. Biochimica Et Biophysica Acta. 494: 416-25. PMID 20975 DOI: 10.1016/0005-2795(77)90171-4 |
0.661 |
|
1977 |
Moo-Penn WF, Bechtel KC, Schmidt RM, Johnson MH, Jue DL, Schmidt DE, Dunlap WM, Opella SJ, Bonaventura J, Bonaventura C. Hemoglobin Raleigh (beta1 valine replaced by acetylalanine). Structural and functional characterization. Biochemistry. 16: 4872-9. PMID 20942 DOI: 10.1021/Bi00641A019 |
0.545 |
|
1977 |
Brouwer M, Bonaventura C, Bonaventura J. Oxygen binding by Limulus polyphemus hemocyanin: Allosteric modulation by chloride ions Biochemistry. 16: 3897-3902. PMID 20133 DOI: 10.1021/Bi00636A027 |
0.652 |
|
1977 |
Bonaventura C, Sullivan B, Bonaventura J, Bourne S. Anion modulation of the negative Bohr effect of haemoglobin from a primitive amphibian. Nature. 265: 474-6. PMID 13309 DOI: 10.1038/265474A0 |
0.651 |
|
1977 |
Weber RE, Mangum C, Steinman H, Bonaventura C, Sullivan B, Bonaventura J. Hemoglobins of two terebellid polychaetes: Enoplobranchus sanguineus and Amphitrite ornata Comparative Biochemistry and Physiology -- Part a: Physiology. 56: 179-187. PMID 11931 DOI: 10.1016/0300-9629(77)90182-7 |
0.597 |
|
1977 |
Weber RE, Sullivan B, Bonaventura J, Bonaventura C. The haemoglobin systems of the bloodworms Glycera dibranchiata and G. americana. Oxygen binding properties of haemolysates and component haemoglobins Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 58: 183-187. DOI: 10.1016/0305-0491(77)90107-9 |
0.649 |
|
1976 |
Bonaventura C, Bonaventura J, Kitto B, Brunori M, Antonini E. Functional consequences of ligand-linked dissociation in hemoglobin from the sea cucumber Molpadia arenicola. Biochimica Et Biophysica Acta. 428: 779-86. PMID 1276182 DOI: 10.1016/0304-4165(76)90209-9 |
0.662 |
|
1976 |
Sullivan B, Bonaventura J, Bonaventura C, Godette G. Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components. The Journal of Biological Chemistry. 251: 7644-8. PMID 1002705 |
0.551 |
|
1976 |
Weber RE, Sullivan B, Bonaventura J, Bonaventura C. The hemoglobin system of the primitive fish, Amia calva: isolation and functional characterization of the individual hemoglobin components. Biochimica Et Biophysica Acta. 434: 18-31. PMID 938661 DOI: 10.1016/0005-2795(76)90031-3 |
0.671 |
|
1976 |
Bonaventura J, Bonaventura C, Sullivan B, Ferruzzi G, McCurdy PR, Fox J, Moo-Penn WF. Hemoglobin Providence. Functional consequences of two alterations of the 2,3 diphosphoglycerate binding site at position β82 Journal of Biological Chemistry. 251: 7563-7571. PMID 12172 |
0.622 |
|
1976 |
Schwantes A, Schwantes ML, Bonaventura C, Sullivan B, Bonaventura J. Hemoglobins of Boa constrictor amarali. Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 54: 447-50. PMID 7424 DOI: 10.1016/0305-0491(76)90119-X |
0.668 |
|
1976 |
Bonaventura C, Sullivan B, Bonaventura J. Spot hemoglobin. Studies on the Root effect hemoglobin of a marine teleost. The Journal of Biological Chemistry. 251: 1871-6. PMID 5433 |
0.588 |
|
1975 |
Sullivan B, Bonaventura J, Bonaventura C, Pennell L, Elliott J, Boyum R, Lambie W. The structure and evolution of parvalbumins. I. Amino acid compositional studies of parvalbumins from four perciform species. Journal of Molecular Evolution. 5: 103-16. PMID 1159797 DOI: 10.1007/Bf01732515 |
0.544 |
|
1975 |
Bonaventura J, Bonaventura C, Amiconi G, Tentori L, Brunori M, Antonini E. Allosteric interactions in non-alpha chains isolated from normal human hemoglobin, fetal hemoglobin, and hemoglobin Abruzzo (beta143 (H21) His replaced by Arg). The Journal of Biological Chemistry. 250: 6278-81. PMID 1158862 |
0.573 |
|
1975 |
Bonaventura C, Bonaventura J, Amiconi G, Tentori L, Brunori M, Antonini E. Hemoglobin Abruzzo (beta143 (H21) His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site. The Journal of Biological Chemistry. 250: 6273-7. PMID 239943 |
0.644 |
|
1975 |
Bonaventura J, Bonaventura C, Sullivan B. Hemoglobins and hemocyanins: comparative aspects of structure and function. The Journal of Experimental Zoology. 194: 155-74. PMID 451 DOI: 10.1002/Jez.1401940110 |
0.591 |
|
1975 |
Bonaventura J, Bonaventura C, Sullivan B, Godette G. Hemoglobin Deer Lodge (beta 2 His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site. The Journal of Biological Chemistry. 250: 9250-5. PMID 393 |
0.645 |
|
1975 |
Mangum CP, Woodin BR, Bonaventura C, Sullivan B, Bonaventura J. The role of coelomic and vascular hemoglobin in the annelid family terebellidae Comparative Biochemistry and Physiology Part a: Physiology. 51: 281-294. DOI: 10.1016/0300-9629(75)90372-2 |
0.632 |
|
1974 |
Bonaventura C, Sullivan B, Bonaventura J. Effect of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus. The Journal of Biological Chemistry. 249: 3768-75. PMID 4833745 |
0.534 |
|
1974 |
Tondo C, Bonaventura J, Bonaventura C, Brunori M, Amiconi G, Antonini E. Functional properties of hemoglobin Pôrto Alegre (alpha2A beta2 9Ser leads to Cys) and the reactivity of its extra cysteinyl residue. Biochimica Et Biophysica Acta. 342: 15-20. PMID 4824922 DOI: 10.1016/0005-2795(74)90101-9 |
0.521 |
|
1974 |
Bonaventura J, Bonaventura C, Brunori M, Giardina B, Antonini E, Bossa F, Wyman J. Functional properties of carboxypeptidase-digested hemoglobins. Journal of Molecular Biology. 82: 499-511. PMID 4817793 DOI: 10.1016/0022-2836(74)90244-7 |
0.618 |
|
1974 |
Bonaventura J, Bonaventura C, Sullivan B. Hemoglobin of the electric Atlantic torpedo, Torpedo nobiliana: a cooperative hemoglobin without Bohr effects. Biochimica Et Biophysica Acta. 371: 147-54. PMID 4429712 DOI: 10.1016/0005-2795(74)90163-9 |
0.679 |
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1974 |
Bonaventura C, Sullivan B, Bonaventura J, Bourne S. CO binding by hemocyanins of Limulus polyphemus, Busycon carica, and Callinectes sapidus. Biochemistry. 13: 4784-9. PMID 4429663 DOI: 10.1021/Bi00720A016 |
0.597 |
|
1974 |
Bonaventura J, Bonaventura C, Sullivan B. Urea tolerance as a molecular adaptation of elasmobranch hemoglobins. Science (New York, N.Y.). 186: 57-9. PMID 4417357 DOI: 10.1126/Science.186.4158.57 |
0.568 |
|
1974 |
Chiancone E, Anderson NM, Antonini E, Bonaventura J, Bonaventura C, Brunori M, Spagnuolo C. Effect of heme and non-heme ligands on subunit dissociation of normal and carboxypeptidase-digested hemoglobin. Gel filtration and flash photolysis studies. The Journal of Biological Chemistry. 249: 5689-94. PMID 4413057 |
0.569 |
|
1974 |
Sullivan B, Bonaventura J, Bonaventura C. Functional differences in the multiple hemocyanins of the horseshoe crab, Limulus polyphemus L. Proceedings of the National Academy of Sciences of the United States of America. 71: 2558-62. PMID 4210212 DOI: 10.1073/Pnas.71.6.2558 |
0.67 |
|
1974 |
Chiancone E, Norne JE, Bonaventura J, Bonaventura C, Forsén S. Nuclear magnetic resonance quadrupole relaxation study of chloride binding to hemoglobin abruzzo (α2Aβ2143 His → Arg) Biochimica Et Biophysica Acta (Bba) - Protein Structure. 336: 403-406. DOI: 10.1016/0005-2795(74)90421-8 |
0.631 |
|
1974 |
Bonaventura J, Bonaventura C, Amiconi G, Antonini E, Brunori M. Functional properties of hemoglobin leiden (α2Aβ26 or7 Glu deleted) Archives of Biochemistry and Biophysics. 161: 328-332. DOI: 10.1016/0003-9861(74)90268-9 |
0.629 |
|
1973 |
Bonaventura C, Bonaventura J, Antonini E, Brunori M, Wyman J. Carbon monoxide binding by simple heme proteins under photodissociating conditions. Biochemistry. 12: 3424-8. PMID 4731186 DOI: 10.1021/Bi00742A010 |
0.578 |
|
1973 |
Brunori M, Bonaventura J, Bonaventura C, Giardina B, Bossa F, Antonini E. Hemoglobins from trout: structural and functional properties. Molecular and Cellular Biochemistry. 1: 189-96. PMID 4585092 DOI: 10.1007/Bf01659329 |
0.562 |
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1973 |
Wilson MT, Brunori M, Bonaventura J, Bonaventura C. Effect of steady illumination on the binding of carbon monoxide by carboxymethylated cytochrome c Biochemical Journal. 131: 863-865. PMID 4352917 DOI: 10.1042/Bj1310863 |
0.588 |
|
1972 |
Bonaventura J, Bonaventura C, Giardina B, Antonini E, Brunori M, Wyman J. Partial restoration of normal functional properties in carboxypeptidase A-digested hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 69: 2174-8. PMID 4506087 DOI: 10.1073/Pnas.69.8.2174 |
0.667 |
|
1972 |
Brunori M, Bonaventura J, Bonaventura C, Antonini E, Wyman J. Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions. Proceedings of the National Academy of Sciences of the United States of America. 69: 868-71. PMID 4502938 DOI: 10.1073/Pnas.69.4.868 |
0.598 |
|
1969 |
Bonaventura C, Myers J. Fluorescence and oxygen evolution from Chlorella pyrenoidosa. Biochimica Et Biophysica Acta. 189: 366-83. PMID 5370012 DOI: 10.1016/0005-2728(69)90168-6 |
0.577 |
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Low-probability matches (unlikely to be authored by this person) |
1971 |
Bonaventura C, Kindergan M. Kinetic and spectral resolution of two components of delayed emission from Chlorella pyrenoidosa. Biochimica Et Biophysica Acta. 234: 249-65. PMID 5566609 DOI: 10.1016/0005-2728(71)90080-6 |
0.265 |
|
2008 |
Rittschof D, Bonaventura C, Wilker JJ, Van Dover CL. Oxidative iron species and ocean challenges: a perspective. Biofouling. 24: 173-5. PMID 18348007 DOI: 10.1080/08927010801958952 |
0.265 |
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2002 |
Taboy CH, Bonaventura C, Crumbliss AL. Anaerobic oxidations of myoglobin and hemoglobin by spectroelectrochemistry. Methods in Enzymology. 353: 187-209. PMID 12078494 DOI: 10.1016/S0076-6879(02)53048-2 |
0.264 |
|
2013 |
Abdellaoui S, Noiriel A, Henkens R, Bonaventura C, Blum LJ, Doumèche B. A 96-well electrochemical method for the screening of enzymatic activities. Analytical Chemistry. 85: 3690-7. PMID 23461701 DOI: 10.1021/Ac303777R |
0.25 |
|
1997 |
Bonaventura C, Johnson FM. Healthy environments for healthy people: bioremediation today and tomorrow. Environmental Health Perspectives. 105: 5-20. PMID 9114274 DOI: 10.1289/Ehp.97105S15 |
0.237 |
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2013 |
Abdellaoui S, Bekhouche M, Noiriel A, Henkens R, Bonaventura C, Blum LJ, Doumèche B. Rapid electrochemical screening of NAD-dependent dehydrogenases in a 96-well format. Chemical Communications (Cambridge, England). 49: 5781-3. PMID 23689734 DOI: 10.1039/C3Cc42065E |
0.225 |
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1999 |
Bonaventura C. NIEHS workshop: unique marine/freshwater models for environmental health research. Environmental Health Perspectives. 107: 89-92. PMID 9876116 DOI: 10.1289/Ehp.9910789 |
0.178 |
|
2016 |
Aymard C, Bonaventura C, Henkens R, Mousty C, Hecquet L, Charmantray F, Blum LJ, Doumèche B. High-Throughput Electrochemical Screening Assay for Free and Immobilized Oxidases: Electrochemiluminescence and Intermittent Pulse Amperometry Chemelectrochem. 4: 957-966. DOI: 10.1002/CELC.201600647 |
0.084 |
|
Hide low-probability matches. |