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Joseph E. Coleman - Publications

Affiliations: 
Yale University, New Haven, CT 
Area:
protein chemistry, enzymology and DNA-protein interactions
Website:
http://www.yale.edu/opa/arc-ybc/v28.n4/story7.html
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60 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
1997 Coleman JE, Rodgers KK, Junker M, Gardner KH, Bellon SF, Steitz TA. Zinc as a structural and folding element of proteins which interact with DNA Journal of Inorganic Biochemistry. 67: 342. DOI: 10.1016/S0162-0134(97)80209-7  0.469
1995 Gardner KH, Anderson SF, Coleman JE. Solution structure of the Kluyveromyces lactis LAC9 Cd2 Cys6 DNA-binding domain. Nature Structural Biology. 2: 898-905. PMID 7552715 DOI: 10.1038/Nsb1095-898  0.506
1994 Gardner KH, Coleman JE. 113Cd-1H heteroTOCSY: a method for determining metal-protein connectivities. Journal of Biomolecular Nmr. 4: 761-74. PMID 7812152 DOI: 10.1007/Bf00398407  0.461
1992 Anderson SF, Coleman JE. Conformational changes of HIV reverse transcriptase subunits on formation of the heterodimer: correlation with kcat and Km. Biochemistry. 31: 8221-8. PMID 1381960 DOI: 10.1021/Bi00150A015  0.321
1991 Mookhtiar KA, Peluso PS, Muller DK, Dunn JJ, Coleman JE. Processivity of T7 RNA polymerase requires the C-terminal Phe882-Ala883-COO- or "foot". Biochemistry. 30: 6305-13. PMID 2059636 DOI: 10.1021/Bi00239A032  0.349
1991 Fitzgerald DW, Coleman JE. Physicochemical properties of cloned nucleocapsid protein from HIV. Interactions with metal ions. Biochemistry. 30: 5195-201. PMID 2036385 DOI: 10.1021/Bi00235A012  0.393
1991 Pan T, Coleman JE. Sequential assignments of the 1H NMR resonances of Zn(II)2 and 113Cd(II)2 derivatives of the DNA-binding domain of the GAL4 transcription factor reveal a novel structural motif for specific DNA recognition. Biochemistry. 30: 4212-22. PMID 2021614 DOI: 10.1021/Bi00231A016  0.434
1991 Gardner KH, Pan T, Narula S, Rivera E, Coleman JE. Structure of the binuclear metal-binding site in the GAL4 transcription factor. Biochemistry. 30: 11292-302. PMID 1958667 DOI: 10.1021/Bi00111A015  0.543
1991 Vallee BL, Coleman JE, Auld DS. Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains. Proceedings of the National Academy of Sciences of the United States of America. 88: 999-1003. PMID 1846973 DOI: 10.1073/Pnas.88.3.999  0.543
1991 Coleman JE, Pan T, Gardner K. Solution structure of the DNA binding domain of the transcription factor GAL4 as determined by 2d NMR methods. Journal of Inorganic Biochemistry. 43: 509. DOI: 10.1016/0162-0134(91)84486-S  0.476
1990 Pan T, Freedman LP, Coleman JE. Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor. Biochemistry. 29: 9218-25. PMID 2271590 DOI: 10.1021/Bi00491A016  0.399
1990 Kuwahara J, Coleman JE. Role of the zinc(II) ions in the structure of the three-finger DNA binding domain of the Sp1 transcription factor. Biochemistry. 29: 8627-31. PMID 2271546 DOI: 10.1021/Bi00489A019  0.433
1990 Pan T, Coleman JE. The DNA binding domain of GAL4 forms a binuclear metal ion complex. Biochemistry. 29: 2023-9. PMID 2186803 DOI: 10.1021/Bi00464A019  0.409
1990 Pan T, Coleman JE. GAL4 transcription factor is not a "zinc finger" but forms a Zn(II)2Cys6 binuclear cluster. Proceedings of the National Academy of Sciences of the United States of America. 87: 2077-81. PMID 2107541 DOI: 10.1073/Pnas.87.6.2077  0.398
1989 Roberts WJ, Pan T, Elliott JI, Coleman JE, Williams KR. p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39. Biochemistry. 28: 10043-7. PMID 2695161 DOI: 10.1021/Bi00452A024  0.404
1989 Martin CT, Coleman JE. T7 RNA polymerase does not interact with the 5'-phosphate of the initiating nucleotide. Biochemistry. 28: 2760-2. PMID 2663058 DOI: 10.1021/Bi00433A002  0.581
1989 Giedroc DP, Johnson BA, Armitage IM, Coleman JE. NMR spectroscopy of 113Cd(II)-substituted gene 32 protein. Biochemistry. 28: 2410-8. PMID 2659069 DOI: 10.1021/Bi00432A011  0.578
1989 Pan T, Giedroc DP, Coleman JE. 1H NMR studies of T4 gene 32 protein: effects of zinc removal and reconstitution. Biochemistry. 28: 8828-32. PMID 2605224 DOI: 10.1021/Bi00448A022  0.606
1989 Pan T, King GC, Coleman JE. Comparison of cooperative and isolated site binding of T4 gene 32 protein to ssDNA by 1H NMR. Biochemistry. 28: 8833-9. PMID 2557909 DOI: 10.1021/Bi00448A023  0.358
1989 Muller DK, Martin CT, Coleman JE. T7 RNA polymerase interacts with its promoter from one side of the DNA helix. Biochemistry. 28: 3306-13. PMID 2545254 DOI: 10.1021/Bi00434A028  0.586
1989 Pan T, Coleman JE. Structure and function of the Zn(II) binding site within the DNA-binding domain of the GAL4 transcription factor. Proceedings of the National Academy of Sciences of the United States of America. 86: 3145-9. PMID 2497463 DOI: 10.1073/Pnas.86.9.3145  0.339
1988 Martin CT, Muller DK, Coleman JE. Processivity in early stages of transcription by T7 RNA polymerase. Biochemistry. 27: 3966-74. PMID 3415967 DOI: 10.1021/Bi00411A012  0.584
1988 King GC, Coleman JE. The Ff gene 5 protein-d(pA)40-60 complex: 1H NMR supports a localized base-binding model. Biochemistry. 27: 6947-53. PMID 3264186 DOI: 10.1021/Bi00418A041  0.372
1988 Keating KM, Ghosaini LR, Giedroc DP, Williams KR, Coleman JE, Sturtevant JM. Thermal denaturation of T4 gene 32 protein: effects of zinc removal and substitution. Biochemistry. 27: 5240-5. PMID 3262371 DOI: 10.1021/Bi00414A044  0.614
1988 Muller DK, Martin CT, Coleman JE. Processivity of proteolytically modified forms of T7 RNA polymerase. Biochemistry. 27: 5763-71. PMID 2460133 DOI: 10.1021/Bi00415A055  0.557
1987 King GC, Coleman JE. Two-dimensional 1H NMR of gene 5 protein indicates that only two aromatic rings interact significantly with oligodeoxynucleotide bases. Biochemistry. 26: 2929-37. PMID 3606999 DOI: 10.1021/Bi00384A039  0.344
1987 Giedroc DP, Keating KM, Williams KR, Coleman JE. The function of zinc in gene 32 protein from T4. Biochemistry. 26: 5251-9. PMID 3314985 DOI: 10.1021/Bi00391A007  0.61
1987 Martin CT, Coleman JE. Kinetic analysis of T7 RNA polymerase-promoter interactions with small synthetic promoters. Biochemistry. 26: 2690-6. PMID 3300768 DOI: 10.1021/Bi00384A006  0.564
1986 Giedroc DP, Keating KM, Martin CT, Williams KR, Coleman JE. Zinc metalloproteins involved in replication and transcription. Journal of Inorganic Biochemistry. 28: 155-69. PMID 3543219 DOI: 10.1016/0162-0134(86)80079-4  0.697
1986 Giedroc DP, Keating KM, Williams KR, Konigsberg WH, Coleman JE. Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein. Proceedings of the National Academy of Sciences of the United States of America. 83: 8452-6. PMID 3490667 DOI: 10.1073/Pnas.83.22.8452  0.615
1986 Giedroc DP, Coleman JE. Structural and functional differences between the two intrinsic zinc ions of Escherichia coli RNA polymerase. Biochemistry. 25: 4969-78. PMID 3094579 DOI: 10.1021/Bi00365A037  0.612
1986 King GC, Martin CT, Pham TT, Coleman JE. Transcription by T7 RNA polymerase is not zinc-dependent and is abolished on amidomethylation of cysteine-347. Biochemistry. 25: 36-40. PMID 3082355 DOI: 10.1021/Bi00349A006  0.598
1986 Prigodich RV, Shamoo Y, Williams KR, Chase JW, Konigsberg WH, Coleman JE. 1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis. Biochemistry. 25: 3666-72. PMID 3013293 DOI: 10.1021/Bi00360A029  0.39
1985 Prigodich RV, O'Connor T, Coleman JE. 1H, 113Cd, and 31P NMR of osteocalcin (bovine gamma-carboxyglutamic acid containing protein). Biochemistry. 24: 6291-8. PMID 3878727 DOI: 10.1021/Bi00343A038  0.384
1985 Pham TT, Coleman JE. Cloning, expression, and purification of gene 3 endonuclease from bacteriophage T7. Biochemistry. 24: 5672-7. PMID 2934091 DOI: 10.1021/Bi00341A058  0.359
1984 Prigodich RV, Casas-Finet J, Williams KR, Konigsberg W, Coleman JE. 1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes. Biochemistry. 23: 522-9. PMID 6367821 DOI: 10.1021/Bi00298A019  0.36
1983 Coleman JE, Gettins P. Alkaline phosphatase, solution structure, and mechanism. Advances in Enzymology and Related Areas of Molecular Biology. 55: 381-452. PMID 6312783  0.476
1980 Saffer JD, Coleman JE. Reversible phosphorylation of a nucleosome binding protein that stimulates transcription of nucleosome deoxyribonucleic acid. Biochemistry. 19: 5874-83. PMID 7459345 DOI: 10.1021/Bi00566A033  0.362
1979 Oakley JL, Strothkamp RE, Sarris AH, Coleman JE. T7 RNA polymerase: promoter structure and polymerase binding. Biochemistry. 18: 528-37. PMID 369603 DOI: 10.1021/Bi00570A023  0.367
1977 Oakley JL, Coleman JE. Structure of a promoter for T7 RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. 74: 4266-70. PMID 270669 DOI: 10.1073/Pnas.74.10.4266  0.342
1975 Anderson RA, Nakashima Y, Coleman JE. Chemical modifications of functional residues of fd gene 5 DNA-binding protein. Biochemistry. 14: 907-17. PMID 1125177 DOI: 10.1021/Bi00676A006  0.401
1975 Anderson RA, Coleman JE. Physiochemical properties of DNA binding proteins: gene 32 protein of T4 and Escherichia coli unwinding protein. Biochemistry. 14: 5485-91. PMID 1103969 DOI: 10.1021/Bi00696A017  0.395
1975 Oakley JL, Pascale JA, Coleman JE. T7 RNA polymerase: conformation, functional groups, and promotor binding. Biochemistry. 14: 4684-91. PMID 1101955 DOI: 10.1021/Bi00692A019  0.406
1973 Taylor JS, Lau CY, Applebury ML, Coleman JE. Escherichia coli Co(II) alkaline phosphatase. Absorption, circular dichroism, and magnetic circular dichroism of the d-d electronic transitions. The Journal of Biological Chemistry. 248: 6216-20. PMID 4580054  0.608
1972 Taylor JS, Coleman JE. Nitrogen ligands at the active site of alkaline phosphatase. Proceedings of the National Academy of Sciences of the United States of America. 69: 859-62. PMID 4337243 DOI: 10.1073/Pnas.69.4.859  0.329
1970 Taylor JS, Mushak P, Coleman JE. Electron spin resonance studies of carbonic anhydrase: transition metal ions and spin-labeled sulfonamides. Proceedings of the National Academy of Sciences of the United States of America. 67: 1410-6. PMID 4320976 DOI: 10.1073/Pnas.67.3.1410  0.353
1970 Applebury ML, Johnson BP, Coleman JE. Phosphate binding to alkaline phosphatase. Metal ion dependence. The Journal of Biological Chemistry. 245: 4968-76. PMID 4319108  0.615
1969 Applebury ML, Coleman JE. Escherichia coli co (II) alkaline phsophatase. The Journal of Biological Chemistry. 244: 709-18. PMID 4889861  0.623
1969 Applebury ML, Coleman JE. Escherichia coli alkaline phosphatase. Metal binding, protein conformation, and quaternary structure. The Journal of Biological Chemistry. 244: 308-18. PMID 4886432  0.638
1966 Coleman JE, Pulido P, Vallee BL. Organic modifications of metallocarboxypeptidases. Biochemistry. 5: 2019-26. PMID 5963445 DOI: 10.1021/Bi00870A033  0.396
1965 Coleman JE. Human carbonic anhydrase. Protein conformation and metal ion binding. Biochemistry. 4: 2644-55. PMID 4956423 DOI: 10.1021/Bi00888A014  0.325
1964 COLEMAN JE, VALLEE BL. METALLOCARBOXYPEPTIDASE-INHIBITOR COMPLEXES. Biochemistry. 3: 1874-9. PMID 14269303 DOI: 10.1021/Bi00900A014  0.424
1963 VALLEE BL, RIORDAN JF, COLEMAN JE. Carboxypeptidase A: approaches to the chemical nature of the active center and the mechanisms of action. Proceedings of the National Academy of Sciences of the United States of America. 49: 109-16. PMID 13995911 DOI: 10.1073/Pnas.49.1.109  0.497
1962 COLEMAN JE, VALLEE BL. Metallocarboxypeptidasesubstrate complexes. Biochemistry. 1: 1083-92. PMID 14022245 DOI: 10.1021/Bi00912A019  0.43
1962 COLEMAN JE, VALLEE BL. Apocarboxypeptidase-substrate complexes. The Journal of Biological Chemistry. 237: 3430-6. PMID 14022244  0.369
1962 Coleman JE, Vallee BL, Bent P. Metallbindende Gruppen der Carboxypeptidase A und ihr Einfluß auf die Aktivität Angewandte Chemie. 74: 34-34. DOI: 10.1002/ange.19620740121  0.32
1961 VALLEE BL, WILLIAMS RJ, COLEMAN JE. Nitrogen and sulphur at the active centre of carboxypeptidase A. Nature. 190: 633-4. PMID 13779804 DOI: 10.1038/190633A0  0.418
1961 COLEMAN JE, VALLEE BL. Metallocarboxypeptidases: stability constants and enzymatic characteristics. The Journal of Biological Chemistry. 236: 2244-9. PMID 13694603  0.347
1960 COLEMAN JE, VALLEE BL. Metallocarboxypeptidases. The Journal of Biological Chemistry. 235: 390-5. PMID 13811155  0.386
1960 COLEMAN JE, ALLAN BJ, VALLEE BL. Protein spherulites. Science (New York, N.Y.). 131: 350-2. PMID 13811154  0.378
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