| Year |
Citation |
Score |
| 1997 |
Sawaya MR, Prasad R, Wilson SH, Kraut J, Pelletier H. Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry. 36: 11205-15. PMID 9287163 DOI: 10.1021/Bi9703812 |
0.558 |
|
| 1997 |
Chen YQ, Kraut J, Callender R. pH-dependent conformational changes in Escherichia coli dihydrofolate reductase revealed by Raman difference spectroscopy. Biophysical Journal. 72: 936-41. PMID 9017218 DOI: 10.1016/S0006-3495(97)78727-7 |
0.345 |
|
| 1997 |
Sawaya MR, Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 36: 586-603. PMID 9012674 DOI: 10.1021/Bi962337C |
0.596 |
|
| 1996 |
Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J. A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta. Biochemistry. 35: 12762-77. PMID 8841119 DOI: 10.1021/Bi9529566 |
0.571 |
|
| 1996 |
Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J. Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism, processivity, and fidelity. Biochemistry. 35: 12742-61. PMID 8841118 DOI: 10.1021/Bi952955D |
0.562 |
|
| 1996 |
Lee H, Reyes VM, Kraut J. Crystal structures of Escherichia coli dihydrofolate reductase complexed with 5-formyltetrahydrofolate (folinic acid) in two space groups: evidence for enolization of pteridine O4. Biochemistry. 35: 7012-20. PMID 8679526 DOI: 10.1021/Bi960028G |
0.438 |
|
| 1996 |
Beard WA, Osheroff WP, Prasad R, Sawaya MR, Jaju M, Wood TG, Kraut J, Kunkel TA, Wilson SH. Enzyme-DNA interactions required for efficient nucleotide incorporation and discrimination in human DNA polymerase beta. The Journal of Biological Chemistry. 271: 12141-4. PMID 8647805 DOI: 10.1074/Jbc.271.21.12141 |
0.595 |
|
| 1996 |
Miller MA, Geren L, Han GW, Saunders A, Beasley J, Pielak GJ, Durham B, Millett F, Kraut J. Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering. Biochemistry. 35: 667-73. PMID 8547245 DOI: 10.1021/Bi952557A |
0.431 |
|
| 1995 |
Reyes VM, Sawaya MR, Brown KA, Kraut J. Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications. Biochemistry. 34: 2710-23. PMID 7873554 DOI: 10.1021/Bi00008A039 |
0.612 |
|
| 1994 |
Hahm S, Miller MA, Geren L, Kraut J, Durham B, Millett F. Reaction of horse cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Biochemistry. 33: 1473-80. PMID 8312267 DOI: 10.1021/Bi00172A025 |
0.31 |
|
| 1994 |
Miller MA, Liu RQ, Hahm S, Geren L, Hibdon S, Kraut J, Durham B, Millett F. Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Biochemistry. 33: 8686-93. PMID 8038158 DOI: 10.1021/Bi00195A009 |
0.377 |
|
| 1994 |
Chen YQ, Kraut J, Blakley RL, Callender R. Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications. Biochemistry. 33: 7021-6. PMID 8003467 DOI: 10.1021/Bi00189A001 |
0.381 |
|
| 1994 |
Miller MA, Han GW, Kraut J. A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase. Proceedings of the National Academy of Sciences of the United States of America. 91: 11118-22. PMID 7972020 DOI: 10.1073/Pnas.91.23.11118 |
0.425 |
|
| 1994 |
Miller MA, Shaw A, Kraut J. 2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex. Nature Structural Biology. 1: 524-31. PMID 7664080 DOI: 10.1038/Nsb0894-524 |
0.394 |
|
| 1994 |
Sawaya MR, Pelletier H, Kumar A, Wilson SH, Kraut J. Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism. Science (New York, N.Y.). 264: 1930-5. PMID 7516581 DOI: 10.1126/Science.7516581 |
0.561 |
|
| 1994 |
Pelletier H, Sawaya MR, Kumar A, Wilson SH, Kraut J. Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP. Science (New York, N.Y.). 264: 1891-903. PMID 7516580 DOI: 10.1126/Science.7516580 |
0.549 |
|
| 1993 |
Vitello LB, Erman JE, Miller MA, Wang J, Kraut J. Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide. Biochemistry. 32: 9807-18. PMID 8396973 DOI: 10.1021/Bi00088A036 |
0.408 |
|
| 1993 |
Erman JE, Vitello LB, Miller MA, Shaw A, Brown KA, Kraut J. Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I. Biochemistry. 32: 9798-806. PMID 8396972 DOI: 10.1021/Bi00088A035 |
0.405 |
|
| 1993 |
McTigue MA, Davies JF, Kaufman BT, Kraut J. Crystal structures of chicken liver dihydrofolate reductase: binary thioNADP+ and ternary thioNADP+.biopterin complexes. Biochemistry. 32: 6855-62. PMID 8334118 DOI: 10.2210/Pdb1Dr3/Pdb |
0.405 |
|
| 1993 |
Brown KA, Howell EE, Kraut J. Long-range structural effects in a second-site revertant of a mutant dihydrofolate reductase. Proceedings of the National Academy of Sciences of the United States of America. 90: 11753-6. PMID 8265622 DOI: 10.1073/Pnas.90.24.11753 |
0.369 |
|
| 1992 |
McTigue MA, Davies JF, Kaufman BT, Kraut J. Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin. Biochemistry. 31: 7264-73. PMID 1510919 DOI: 10.1021/Bi00147A009 |
0.467 |
|
| 1992 |
David CL, Howell EE, Farnum MF, Villafranca JE, Oatley SJ, Kraut J. Structure and function of alternative proton-relay mutants of dihydrofolate reductase. Biochemistry. 31: 9813-22. PMID 1356437 |
0.349 |
|
| 1992 |
Pelletier H, Kraut J. Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science (New York, N.Y.). 258: 1748-55. PMID 1334573 DOI: 10.1126/Science.1334573 |
0.394 |
|
| 1992 |
Brown KA, Kraut J. Exploring the molecular mechanism of dihydrofolate reductase. Faraday Discussions. 217-24. PMID 1290933 DOI: 10.1039/Fd9929300217 |
0.404 |
|
| 1991 |
Bajorath J, Kitson DH, Fitzgerald G, Andzelm J, Kraut J, Hagler AT. Electron redistribution on binding of a substrate to an enzyme: folate and dihydrofolate reductase. Proteins. 9: 217-224. PMID 2006139 DOI: 10.1002/Prot.340090307 |
0.368 |
|
| 1991 |
Bystroff C, Kraut J. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry. 30: 2227-39. PMID 1998681 DOI: 10.2210/Pdb1Dra/Pdb |
0.448 |
|
| 1991 |
Bajorath J, Kitson DH, Kraut J, Hagler AT. The electrostatic potential of Escherichia coli dihydrofolate reductase Proteins: Structure, Function and Genetics. 11: 1-12. PMID 1961697 DOI: 10.1002/Prot.340110102 |
0.365 |
|
| 1991 |
Warren MS, Brown KA, Farnum MF, Howell EE, Kraut J. Investigation of the functional role of tryptophan-22 in Escherichia coli dihydrofolate reductase by site-directed mutagenesis. Biochemistry. 30: 11092-103. PMID 1932031 DOI: 10.1021/Bi00110A011 |
0.423 |
|
| 1991 |
Bajorath J, Kraut J, Li Z, Kitson DH, Hagler AT. Theoretical studies on the dihydrofolate reductase mechanism: Electronic polarization of bound substrates Proceedings of the National Academy of Sciences of the United States of America. 88: 6423-6426. PMID 1862073 DOI: 10.1073/Pnas.88.15.6423 |
0.351 |
|
| 1991 |
Bajorath J, Li Z, Fitzgerald G, Kitson DH, Farnum M, Fine RM, Kraut J, Hagler AT. Changes in the electron density of the cofactor NADPH on binding to E. coli dihydrofolate reductase Proteins: Structure, Function and Genetics. 11: 263-270. PMID 1758881 DOI: 10.1002/Prot.340110405 |
0.39 |
|
| 1991 |
Smulevich G, Miller MA, Kraut J, Spiro TG. Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: Resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase Biochemistry. 30: 9546-9558. PMID 1654102 DOI: 10.1021/Bi00103A023 |
0.346 |
|
| 1990 |
Howell EE, Booth C, Farnum M, Kraut J, Warren MS. A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27----serine Escherichia coli dihydrofolate reductase. Biochemistry. 29: 8561-9. PMID 2271539 DOI: 10.1021/Bi00489A009 |
0.316 |
|
| 1990 |
Davies JF, Delcamp TJ, Prendergast NJ, Ashford VA, Freisheim JH, Kraut J. Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate Biochemistry®. 29: 9467-9479. PMID 2248959 DOI: 10.1021/Bi00492A021 |
0.461 |
|
| 1990 |
Bystroff C, Oatley SJ, Kraut J. Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry. 29: 3263-77. PMID 2185835 DOI: 10.1021/Bi00465A018 |
0.423 |
|
| 1990 |
Smulevich G, Wang Y, Mauro JM, Wang JM, Fishel LA, Kraut J, Spiro TG. Single-crystal resonance Raman spectroscopy of site-directed mutants of cytochrome c peroxidase. Biochemistry. 29: 7174-80. PMID 2169874 DOI: 10.1021/Bi00483A004 |
0.311 |
|
| 1990 |
Wang JM, Mauro M, Edwards SL, Oatley SJ, Fishel LA, Ashford VA, Xuong NH, Kraut J. X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis. Biochemistry. 29: 7160-73. PMID 2169873 DOI: 10.1021/Bi00483A003 |
0.438 |
|
| 1989 |
Terner J, Shifflett J, Mauro M, Fishel L, Kraut J. Resonance Raman spectroscopy of cytochrome c peroxidase intermediates of mutant enzymes obtained through site-directed mutagenesis Journal of Inorganic Biochemistry. 36: 316. DOI: 10.1016/0162-0134(89)84495-2 |
0.349 |
|
| 1989 |
Scholes CP, Liu Y, Fishel LA, Farnum MF, Mauro JM, Kraut J. Recent ENDOR and Pulsed Electron Paramagnetic Resonance Studies of CytochromecPeroxidase - Compound I and Its Site-Directed Mutants Israel Journal of Chemistry. 29: 85-92. DOI: 10.1002/Ijch.198900012 |
0.324 |
|
| 1988 |
Edwards SL, Kraut J, Xuong Nh, Ashford V, Halloran TP, Mills SE. Crystallization and purification of the enzyme anthranilate phosphoribosyl transferase Journal of Molecular Biology. 203: 523-524. PMID 3199444 DOI: 10.1016/0022-2836(88)90020-4 |
0.344 |
|
| 1988 |
Kraut J. How do enzymes work Science. 242: 533-540. PMID 3051385 DOI: 10.1126/Science.3051385 |
0.34 |
|
| 1988 |
Edwards SL, Kraut J, Poulos TL. Crystal structure of nitric oxide inhibited cytochrome c peroxidase Biochemistry. 27: 8074-8081. PMID 2852951 DOI: 10.1021/Bi00421A016 |
0.453 |
|
| 1987 |
Villafranca JE, Howell EE, Oatley SJ, Xuong NH, Kraut J. An engineered disulfide bond in dihydrofolate reductase Biochemistry. 26: 2182-2189. PMID 3304420 DOI: 10.1021/Bi00382A017 |
0.415 |
|
| 1987 |
Edwards SL, Xuong NH, Hamlin RC, Kraut J. Crystal structure of cytochrome c peroxidase compound I Biochemistry. 26: 1503-1511. PMID 3036202 DOI: 10.1021/Bi00380A002 |
0.398 |
|
| 1987 |
Fishel LA, Villafranca JE, Mauro JM, Kraut J. Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I. Biochemistry. 26: 351-360. PMID 3030406 DOI: 10.1021/Bi00376A004 |
0.326 |
|
| 1987 |
Howell EE, Warren MS, Booth CL, Villafranca JE, Kraut J. Construction of an altered proton donation mechanism in Escherichia coli dihydrofolate reductase. Biochemistry. 26: 8591-8. PMID 2894842 DOI: 10.1021/Bi00400A015 |
0.372 |
|
| 1987 |
Edwards S, Anderson D, Kraut J, Xuong NH. Crystal structures of the oxidized intermediate of cytochrome c peroxidase and its decay product Acta Crystallographica Section A. 43. DOI: 10.1107/S0108767387084381 |
0.336 |
|
| 1986 |
London RE, Howell EE, Warren MS, Kraut J, Blakley RL. Nuclear magnetic resonance study of the state of protonation of inhibitors bound to mutant dihydrofolate reductase lacking the active-site carboxyl. Biochemistry. 25: 7229-35. PMID 3542023 DOI: 10.1021/Bi00370A069 |
0.35 |
|
| 1986 |
Howell EE, Villafranca JE, Warren MS, Oatley SJ, Kraut J. Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis. Science (New York, N.Y.). 231: 1123-8. PMID 3511529 DOI: 10.1126/Science.3511529 |
0.42 |
|
| 1986 |
Villafranca JE, Howell EE, Oatley SJ, Warren MS, Kraut J. A Structure--Function Study of Dihydrofolate Reductase by Protein Engineering Philosophical Transactions of the Royal Society A. 317: 405-413. DOI: 10.1098/Rsta.1986.0050 |
0.456 |
|
| 1985 |
Poulos TL, Finzel BC, Gunsalus IC, Wagner GC, Kraut J. The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. The Journal of Biological Chemistry. 260: 16122-30. PMID 4066706 |
0.673 |
|
| 1985 |
Matthews DA, Bolin JT, Burridge JM, Filman DJ, Volz KW, Kraut J. Dihydrofolate reductase. The stereochemistry of inhibitor selectivity. The Journal of Biological Chemistry. 260: 392-9. PMID 3880743 |
0.767 |
|
| 1985 |
Matthews DA, Bolin JT, Burridge JM, Filman DJ, Volz KW, Kaufman BT, Beddell CR, Champness JN, Stammers DK, Kraut J. Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim. The Journal of Biological Chemistry. 260: 381-91. PMID 3880742 |
0.786 |
|
| 1984 |
Finzel BC, Poulos TL, Kraut J. Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution. The Journal of Biological Chemistry. 259: 13027-36. PMID 6092361 DOI: 10.2210/Pdb2Cyp/Pdb |
0.709 |
|
| 1983 |
Villafranca JE, Howell EE, Voet DH, Strobel MS, Ogden RC, Abelson JN, Kraut J. Directed mutagenesis of dihydrofolate reductase. Science (New York, N.Y.). 222: 782-8. PMID 6356360 DOI: 10.1126/Science.6356360 |
0.429 |
|
| 1982 |
Volz KW, Matthews DA, Alden RA, Freer ST, Hansch C, Kaufman BT, Kraut J. Crystal structure of avian dihydrofolate reductase containing phenyltriazine and NADPH. The Journal of Biological Chemistry. 257: 2528-36. PMID 7061437 |
0.658 |
|
| 1982 |
Filman DJ, Bolin JT, Matthews DA, Kraut J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis. The Journal of Biological Chemistry. 257: 13663-72. PMID 6815179 |
0.706 |
|
| 1982 |
Bolin JT, Filman DJ, Matthews DA, Hamlin RC, Kraut J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. The Journal of Biological Chemistry. 257: 13650-62. PMID 6815178 DOI: 10.2210/Pdb3Dfr/Pdb |
0.726 |
|
| 1981 |
Kraut J. Molecular geometry of cytochrome c and its peroxidase: a model for biological electron transfer. Biochemical Society Transactions. 9: 197-202. PMID 6268468 DOI: 10.1042/Bst0090197 |
0.379 |
|
| 1978 |
Matthews DA, Alden RA, Bolin JT, Filman DJ, Freer ST, Hamlin R, Hol WG, Kisliuk RL, Pastore EJ, Plante LT, Xuong N, Kraut J. Dihydrofolate reductase from Lactobacillus casei. X-ray structure of the enzyme methotrexate.NADPH complex. The Journal of Biological Chemistry. 253: 6946-54. PMID 29045 |
0.64 |
|
| 1977 |
Matthews DA, Alden RA, Bolin JT, Freer ST, Hamlin R, Xuong N, Kraut J, Poe M, Williams M, Hoogsteen K. Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate. Science (New York, N.Y.). 197: 452-5. PMID 17920 DOI: 10.1126/Science.17920 |
0.695 |
|
| 1976 |
Birktoft JJ, Kraut J, Freer ST. A detailed structural comparison between the charge relay system in chymotrypsinogen and in alpha-chymotrypsin. Biochemistry. 15: 4481-4485. PMID 974071 DOI: 10.1021/Bi00665A023 |
0.403 |
|
| 1975 |
Freer ST, Alden RA, Carter CW, Kraut J. Crystallographic structure refinement of Chromatium high potential iron protein at two Angstroms resolution. The Journal of Biological Chemistry. 250: 46-54. PMID 1141211 |
0.542 |
|
| 1974 |
Carter CW, Kraut J, Freer ST, Nguyen-Huu-Xuong, Alden RA, Bartsch RG. Two-Angstrom crystal structure of oxidized Chromatium high potential iron protein. The Journal of Biological Chemistry. 249: 4212-25. PMID 4855287 DOI: 10.2210/Pdb1Hip/Pdb |
0.623 |
|
| 1974 |
Carter CW, Kraut J. A proposed model for interaction of polypeptides with RNA. Proceedings of the National Academy of Sciences of the United States of America. 71: 283-7. PMID 4521801 DOI: 10.1073/Pnas.71.2.283 |
0.575 |
|
| 1974 |
Carter CW, Kraut J, Freer ST, Alden RA. Comparison of oxidation-reduction site geometries in oxidized and reduced Chromatium high potential iron protein and oxidized Peptococcus aerogenes ferredoxin. The Journal of Biological Chemistry. 249: 6339-46. PMID 4417854 |
0.464 |
|
| 1973 |
Salemme FR, Freer ST, Xuong NH, Alden RA, Kraut J. The structure of oxidized cytochrome c2 of Rhodospirillum rubrum Journal of Biological Chemistry. 248: 3910-3921. PMID 4350650 DOI: 10.2210/Pdb1C2C/Pdb |
0.427 |
|
| 1972 |
Robertus JD, Kraut J, Alden RA, Birktoft JJ. Subtilisin; a stereochemical mechanism involving transition-state stabilization. Biochemistry. 11: 4293-303. PMID 5079900 DOI: 10.1021/Bi00773A016 |
0.488 |
|
| 1972 |
Robertus JD, Alden RA, Birktoft JJ, Kraut J, Powers JC, Wilcox PE. An x-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN'. Biochemistry. 11: 2439-49. PMID 5040650 DOI: 10.1021/Bi00763A009 |
0.572 |
|
| 1972 |
Wright CS, Alden RA, Kraut J. Crystal structure of a subtilisin BPN′ complex with N-benzoyl-l-arginine Journal of Molecular Biology. 66. PMID 5038454 DOI: 10.1016/0022-2836(72)90479-2 |
0.425 |
|
| 1972 |
Carter CW, Kraut J, Freer ST, Alden RA, Sieker LC, Adman E, Jensen LH. A comparison of Fe 4 S 4 clusters in high-potential iron protein and in ferredoxin. Proceedings of the National Academy of Sciences of the United States of America. 69: 3526-9. PMID 4509310 DOI: 10.1073/Pnas.69.12.3526 |
0.545 |
|
| 1972 |
Carter CW, Freer ST, Xuong NH, Alden RA, Kraut J. Structure of the iron-sulfur cluster in the Chromatius iron protein at 2.25 Angstrom resolution. Cold Spring Harbor Symposia On Quantitative Biology. 36: 381-5. PMID 4508152 DOI: 10.1101/Sqb.1972.036.01.049 |
0.521 |
|
| 1972 |
Kraut J, Robertus JD, Birktoft JJ, Alden RA, Wilcox PE, Powers JC. The aromatic substrate binding site in subtilisin BPN' and its resemblance to chymotrypsin. Cold Spring Harbor Symposia On Quantitative Biology. 36: 117-23. PMID 4508128 DOI: 10.1101/Sqb.1972.036.01.017 |
0.602 |
|
| 1971 |
Robertus JD, Alden RA, Kraut J. On the identity of subtilisins BPN' and Novo. Biochemical and Biophysical Research Communications. 42: 334-9. PMID 5545520 DOI: 10.1016/0006-291X(71)90107-0 |
0.58 |
|
| 1971 |
Alden RA, Birktoft JJ, Kraut J, Robertus JD, Wright CS. Atomic coordinates for subtilisin BPN' (or Novo). Biochemical and Biophysical Research Communications. 45: 337-44. PMID 5160720 DOI: 10.1016/0006-291X(71)90823-0 |
0.562 |
|
| 1970 |
Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH. Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation. Biochemistry. 9: 1997-2009. PMID 5442169 DOI: 10.1021/Bi00811A022 |
0.585 |
|
| 1970 |
Alden RA, Wright CS, Kraut J. A hydrogen-bond network at the active site of subtilisin BPN' Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 257: 119-124. PMID 4399039 DOI: 10.1098/Rstb.1970.0014 |
0.373 |
|
| 1969 |
Wright CS, Alden RA, Kraut J. Structure of subtilisin BPN′ at 2.5 Å resolution Nature. 221: 235-242. PMID 5763076 DOI: 10.1038/221235A0 |
0.413 |
|
| 1968 |
Alden RA, Kraut J, Traylor TG. Mechanism of single-bond shortening. Evidence from the crystal structures of 1-biapocamphane, 1-binorbornane, and 1-biadamantane Journal of the American Chemical Society. 90: 74-82. DOI: 10.1021/Ja01003A014 |
0.36 |
|
| 1962 |
Stout GH, Alden RA, Kraut J, High DF. Harunganin: A Crystallographic Determination of an Unknown Structure Journal of the American Chemical Society. 84: 2653-2654. DOI: 10.1021/Ja00872A045 |
0.324 |
|
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