Year |
Citation |
Score |
1996 |
Braun C, Lindhorst T, Madsen NB, Withers SG. Identification of Asp 549 as the catalytic nucleophile of glycogen-debranching enzyme via trapping of the glycosyl-enzyme intermediate. Biochemistry. 35: 5458-63. PMID 8611536 DOI: 10.1021/Bi9526488 |
0.508 |
|
1995 |
Liu W, Madsen NB, Fan B, Zucker KA, Glew RH, Fry DE. Effects of oligosaccharide binding on glycogen debranching enzyme activity and conformation. Biochemistry. 34: 7056-61. PMID 7766615 DOI: 10.1021/Bi00021A017 |
0.398 |
|
1992 |
Sprang SR, Madsen NB, Withers SG. Multiple phosphate positions in the catalytic site of glycogen phosphorylase: structure of the pyridoxal-5'-pyrophosphate coenzyme-substrate analog. Protein Science : a Publication of the Protein Society. 1: 1100-11. PMID 1304389 DOI: 10.1002/Pro.5560010904 |
0.508 |
|
1991 |
Liu W, Madsen NB, Braun C, Withers SG. Reassessment of the catalytic mechanism of glycogen debranching enzyme. Biochemistry. 30: 1419-24. PMID 1991122 DOI: 10.1021/Bi00219A036 |
0.529 |
|
1991 |
Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB. Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate. Science (New York, N.Y.). 254: 1367-71. PMID 1962195 DOI: 10.1126/Science.1962195 |
0.541 |
|
1989 |
Kornberg HL, Madsen NB. Synthesis of C4-dicarboxylic acids from acetate by a "glyoxylate bypass" of the tricarboxylic acid cycle. 1957. Biochimica Et Biophysica Acta. 1000: 275-7. PMID 2673375 |
0.444 |
|
1988 |
Sprang SR, Acharya KR, Goldsmith EJ, Stuart DI, Varvill K, Fletterick RJ, Madsen NB, Johnson LN. Structural changes in glycogen phosphorylase induced by phosphorylation. Nature. 336: 215-21. PMID 3194008 DOI: 10.1038/336215A0 |
0.395 |
|
1988 |
Scraba DG, Bradley RD, Fitzgerald PM, Madsen NB. Electron microscopy of glycogen degrading enzymes. Febs Letters. 240: 133-8. PMID 3142791 DOI: 10.1016/0014-5793(88)80354-5 |
0.375 |
|
1988 |
Takrama J, Madsen NB. Binding of glycogen, oligosaccharides, and glucose to glycogen debranching enzyme. Biochemistry. 27: 3308-14. PMID 2968814 DOI: 10.1021/Bi00409A028 |
0.404 |
|
1987 |
Monanu MO, Madsen NB. Distinction between substrate- and enzyme-directed effects of modifiers of rabbit liver phosphorylase a phosphatases. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 65: 293-301. PMID 3038147 DOI: 10.1139/O87-038 |
0.411 |
|
1986 |
Madsen NB. 9 Glycogen Phosphorylase Enzymes. 17: 365-394. DOI: 10.1016/S1874-6047(08)60434-5 |
0.387 |
|
1985 |
Withers SG, Madsen NB, Sykes BD. 31P NMR relaxation studies of the activation of the coenzyme phosphate of glycogen phosphorylase. The role of motion of the bound phosphate. Biophysical Journal. 48: 1019-26. PMID 3937556 DOI: 10.1016/S0006-3495(85)83864-9 |
0.572 |
|
1985 |
Withers SG, Madsen NB, Sykes BD. Relaxation of individual transitions in an AX spectrum. Use of interference terms to separate the dipolar and chemical-shift anisotropy contributions to the relaxation of 31P and 19F nuclei in macromolecules Journal of Magnetic Resonance (1969). 61: 545-549. DOI: 10.1016/0022-2364(85)90195-7 |
0.523 |
|
1984 |
Madsen NB, Withers SG. The catalytic mechanism of phosphorylase; novel role of the coenzyme phosphate. Progress in Clinical and Biological Research. 144: 117-26. PMID 6427781 |
0.423 |
|
1984 |
Osterlund BR, Hayakawa K, Madsen NB, James MN. Crystallization of glycogen debranching enzyme. Journal of Molecular Biology. 174: 557-9. PMID 6232392 DOI: 10.1016/0022-2836(84)90336-X |
0.358 |
|
1983 |
Madsen NB, Shechosky S, Fletterick RJ. Site-site interactions in glycogen phosphorylase b probed by ligands specific for each site. Biochemistry. 22: 4460-5. PMID 6414512 DOI: 10.1021/Bi00288A017 |
0.383 |
|
1982 |
Withers SG, Madsen NB, Sprang SR, Fletterick RJ. Catalytic site of glycogen phosphorylase: structural changes during activation and mechanistic implications. Biochemistry. 21: 5372-82. PMID 7171564 DOI: 10.1021/Bi00264A039 |
0.508 |
|
1982 |
Sprang S, Fletterick R, Stern M, Yang D, Madsen N, Sturtevant J. Analysis of an allosteric binding site: the nucleoside inhibitor site of phosphorylase alpha Biochemistry. 21: 2036-2048. PMID 7093228 DOI: 10.1021/Bi00538A010 |
0.316 |
|
1982 |
Withers SG, Madsen NB, Sykes BD. Covalently activated glycogen phosphorylase: a phosphorus-31 nuclear magnetic resonance and ultracentrifugation analysis. Biochemistry. 21: 6716-22. PMID 6818986 DOI: 10.1021/Bi00269A016 |
0.639 |
|
1982 |
Sprang SR, Goldsmith EJ, Fletterick RJ, Withers SG, Madsen NB. Catalytic site of glycogen phosphorylase: structure of the T state and specificity for alpha-D-glucose. Biochemistry. 21: 5364-71. PMID 6816272 DOI: 10.1021/Bi00264A038 |
0.485 |
|
1982 |
Withers SG, Shechosky S, Madsen NB. Pyridoxal phosphate is not the acid catalyst in the glycogen phosphorylase catalytic mechanism. Biochemical and Biophysical Research Communications. 108: 322-8. PMID 6816229 DOI: 10.1016/0006-291X(82)91869-1 |
0.511 |
|
1981 |
Kasvinsky PJ, Fletterick RJ, Madsen NB. Regulation of the dephosphorylation of glycogen phosphorylase a and synthase b by glucose and caffeine in isolated hepatocytes. Canadian Journal of Biochemistry. 59: 387-95. PMID 6794883 DOI: 10.1139/O81-054 |
0.371 |
|
1981 |
Withers SG, Madsen NB, Sykes BD, Takagi M, Shimomura S, Fukui T. Evidence for direct phosphate-phosphate interaction between pyridoxal phosphate and substrate in the glycogen phosphorylase catalytic mechanism. The Journal of Biological Chemistry. 256: 10759-62. PMID 6793586 |
0.561 |
|
1981 |
Withers SG, Madsen NB, Sykes BD. Active form of pyridoxal phosphate in glycogen phosphorylase. Phosphorus-31 nuclear magentic resonance investigation. Biochemistry. 20: 1748-56. PMID 6784759 DOI: 10.1021/Bi00510A007 |
0.656 |
|
1980 |
Withers SG, Madsen NB. Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form. Biochemical and Biophysical Research Communications. 97: 513-9. PMID 6781495 DOI: 10.1016/0006-291X(80)90293-4 |
0.528 |
|
1979 |
Withers SG, Sykes BD, Madsen NB, Kasvinsky PJ. Identical structural changes induced in glycogen phosphorylase by two nonexclusive allosteric inhibitors. Biochemistry. 18: 5342-8. PMID 518839 DOI: 10.1021/Bi00591A013 |
0.556 |
|
1979 |
Fletterick RJ, Sprang S, Madsen NB. Analysis of the surface topography of glycogen phosphorylase a: implications for metabolic interconversion and regulatory mechanisms. Canadian Journal of Biochemistry. 57: 789-97. PMID 476522 DOI: 10.1139/O79-098 |
0.386 |
|
1979 |
Withers SG, Yang DS, Madsen NB, Fletterick RJ. A systematic approach to isomorphous replacement using a series of simple charged mercurials. Biochemical and Biophysical Research Communications. 86: 1044-50. PMID 435308 DOI: 10.1016/0006-291X(79)90222-5 |
0.448 |
|
1977 |
Li EC, Fletterick RJ, Sygusch J, Madsen NB. An essential arginine residue in the active-site pocket of glycogen phosporylase. Canadian Journal of Biochemistry. 55: 465-73. PMID 870152 DOI: 10.1139/O77-065 |
0.427 |
|
1977 |
Fletterick RJ, Madsen NB. X-rays reveal phosphorylase architecture Trends in Biochemical Sciences. 2: 145-148. DOI: 10.1016/0968-0004(77)90361-9 |
0.389 |
|
1976 |
Fletterick RJ, Sygusch J, Murray N, Madsen NB. Low-resolution structure of the glycogen phosphorylase alpha monomer and comparison with phosphorylase beta. Journal of Molecular Biology. 103: 1-13. PMID 957422 DOI: 10.1016/0022-2836(76)90048-6 |
0.311 |
|
1976 |
Madsen NB, Avramovic-Zikic O, Lue PF, Honikel KO. Studies on allosteric phenomena in glycogen phosphorylase b. Molecular and Cellular Biochemistry. 11: 35-50. PMID 775316 DOI: 10.1007/Bf01792832 |
0.39 |
|
1970 |
Engers HD, Bridger WA, Madsen NB. Kinetic mechanism of phosphorylase a. II. Isotope exchange studies at equilibrium. Canadian Journal of Biochemistry. 48: 755-8. PMID 5534922 DOI: 10.1139/O70-118 |
0.37 |
|
1970 |
Engers HD, Bridger WA, Madsen NB. Isotope exchange at equilibrium as a test for homotropic cooperativity of allosteric enzymes. Biochemistry. 9: 3281-4. PMID 4992393 DOI: 10.1021/Bi00818A023 |
0.329 |
|
1970 |
Zarkadas CG, Smillie LB, Madsen NB. The sulfhydryl groups of muscle phosphorylase. V. The reactive sulfhydryl peptides. Canadian Journal of Biochemistry. 48: 763-76. PMID 4934391 DOI: 10.1139/O70-120 |
0.308 |
|
1970 |
Engers HD, Shechosky S, Madsen NB. Kinetic mechanism of phosphorylase a. I. Initial velocity studies. Canadian Journal of Biochemistry. 48: 746-54. PMID 4397708 DOI: 10.1139/O70-117 |
0.384 |
|
1958 |
MADSEN NB, CORI CF. The binding of glycogen and phosphorylase. The Journal of Biological Chemistry. 233: 1251-6. PMID 13610823 |
0.492 |
|
1958 |
KORNBERG HL, MADSEN NB. The metabolism of C2 compounds in microorganisms. 3. Synthesis of malate from acetate via the glyoxylate cycle. The Biochemical Journal. 68: 549-57. PMID 13522658 |
0.431 |
|
1957 |
KORNBERG HL, MADSEN NB. Synthesis of C4-dicarboxylic acids from acetate by a glyoxylate bypass of the tricarboxylic acid cycle. Biochimica Et Biophysica Acta. 24: 651-3. PMID 13436500 |
0.444 |
|
1957 |
MADSEN NB, CORI CF. The binding of adenylic acid by muscle phosphorylase. The Journal of Biological Chemistry. 224: 899-908. PMID 13405919 |
0.508 |
|
1956 |
CORI CF, MADSEN NB. The interaction of muscle phosphorylase with p-chloromercuribenzoate. I. Inhibition of activity and effect on the molecular weight. The Journal of Biological Chemistry. 223: 1055-65. PMID 13385253 |
0.5 |
|
1955 |
MADSEN NB, CORI CF. The inhibition of muscle phosphorylase by p-chloromercuribenzoate. Biochimica Et Biophysica Acta. 18: 156-7. PMID 13260267 DOI: 10.1016/0006-3002(55)90032-9 |
0.482 |
|
1954 |
MADSEN NB, CORI CF. The interaction of phosphorylase with protamine. Biochimica Et Biophysica Acta. 15: 516-25. PMID 13230100 DOI: 10.1016/0006-3002(54)90009-8 |
0.543 |
|
1953 |
MADSEN NB, TUBA J. [The role of alkaline phosphatase in intestinal absorption. I. The kinetics of phosphatase action on various substrates]. Canadian Journal of Medical Sciences. 31: 1-7. PMID 13019657 DOI: 10.1139/Cjms53-001 |
0.391 |
|
1952 |
TAYLOR JD, MADSEN NB, TUBA J. The effects of some dietary derived lipids and fat soluble vitamins on rat serum tributyrinase and alkaline phosphatase. Canadian Journal of Medical Sciences. 30: 308-13. PMID 14954491 DOI: 10.1139/Cjms52-039 |
0.303 |
|
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