| Year |
Citation |
Score |
| 2013 |
George RC, Lew J, Graves DJ. Interaction of cinnamaldehyde and epicatechin with tau: implications of beneficial effects in modulating Alzheimer's disease pathogenesis. Journal of Alzheimer's Disease : Jad. 36: 21-40. PMID 23531502 DOI: 10.3233/Jad-122113 |
0.627 |
|
| 2009 |
Peterson DW, George RC, Scaramozzino F, LaPointe NE, Anderson RA, Graves DJ, Lew J. Cinnamon extract inhibits tau aggregation associated with Alzheimer's disease in vitro. Journal of Alzheimer's Disease : Jad. 17: 585-97. PMID 19433898 DOI: 10.3233/Jad-2009-1083 |
0.624 |
|
| 2006 |
Scaramozzino F, Peterson DW, Farmer P, Gerig JT, Graves DJ, Lew J. TMAO promotes fibrillization and microtubule assembly activity in the C-terminal repeat region of tau Biochemistry. 45: 3684-3691. PMID 16533051 DOI: 10.1021/Bi052167G |
0.657 |
|
| 2003 |
Bartleson C, Biorn AC, Graves DJ. Mutants of phosphorylase a altered in recognition by protein phosphatase-1 Biochemistry. 42: 3018-3024. PMID 12627967 DOI: 10.1021/Bi027091S |
0.367 |
|
| 2001 |
Bartleson C, Graves DJ. An Inhibitory Segment of the Catalytic Subunit of Phosphorylase Kinase Does Not Act as a Pseudosubstrate Journal of Biological Chemistry. 276: 34560-34566. PMID 11448955 DOI: 10.1074/Jbc.M102308200 |
0.412 |
|
| 2001 |
Biorn AC, Graves DJ. The amino-terminal tail of glycogen phosphorylase is a switch for controlling phosphorylase conformation, activation, and response to ligands Biochemistry. 40: 5181-5189. PMID 11318640 DOI: 10.1021/Bi0020372 |
0.45 |
|
| 2000 |
Biorn AC, Bartleson C, Graves DJ. Site-directed mutants of glycogen phosphorylase are altered in their interaction with phosphorylase kinase Biochemistry. 39: 15887-15894. PMID 11123915 DOI: 10.1021/Bi001755L |
0.432 |
|
| 2000 |
Bartleson C, Luo S, Graves DJ, Martin BL. Arginine to citrulline replacement in substrates of phosphorylase kinase Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1480: 23-28. PMID 11004553 DOI: 10.1016/S0167-4838(00)00100-X |
0.303 |
|
| 1999 |
Graves D, Bartleson C, Biorn A, Pete M. Substrate and inhibitor recognition of protein kinases: what is known about the catalytic subunit of phosphorylase kinase? Pharmacology & Therapeutics. 82: 143-155. PMID 10454193 DOI: 10.1016/S0163-7258(98)00049-7 |
0.432 |
|
| 1999 |
Pete MJ, Liao CX, Bartleson C, Graves DJ. A recombinant form of the catalytic subunit of phosphorylase kinase that is soluble, monomeric, and includes key C-terminal residues Archives of Biochemistry and Biophysics. 367: 104-114. PMID 10375405 DOI: 10.1006/Abbi.1999.1256 |
0.463 |
|
| 1999 |
Yuan J, Huiatt TW, Liao CX, Robson RM, Graves DJ. The effects of mono-ADP-ribosylation on desmin assembly-disassembly: Determination of the chemical features of bound ADP-ribose that prevent desmin filament formation Archives of Biochemistry and Biophysics. 363: 314-322. PMID 10068454 DOI: 10.1006/Abbi.1998.1096 |
0.366 |
|
| 1998 |
Martin BL, Luo S, Kintanar A, Chen M, Graves DJ. Effect of citrulline for arginine replacement on the structure and turnover of phosphopeptide substrates of protein phosphatase-1 Archives of Biochemistry and Biophysics. 359: 179-191. PMID 9808759 DOI: 10.1006/Abbi.1998.0912 |
0.487 |
|
| 1998 |
Tseng HC, Graves DJ. Natural methylamine osmolytes, trimethylamine N-oxide and betaine, increase tau-induced polymerization of microtubules Biochemical and Biophysical Research Communications. 250: 726-730. PMID 9784413 DOI: 10.1006/Bbrc.1998.9382 |
0.315 |
|
| 1998 |
Imparl-Radosevich J, Deas S, Polansky MM, Baedke DA, Ingebritsen TS, Anderson RA, Graves DJ. Regulation of PTP-1 and insulin receptor kinase by fractions from cinnamon: Implications for cinnamon regulation of insulin signalling Hormone Research. 50: 177-182. PMID 9762007 DOI: 10.1159/000023270 |
0.324 |
|
| 1997 |
Graves DJ, Huiatt TW, Zhou H, Huang HY, Sernett SW, Robson RM, McMahon KK. Regulatory role of arginine-specific mono(ADP-ribosyl)transferase in muscle cells Advances in Experimental Medicine and Biology. 419: 305-313. PMID 9193670 DOI: 10.1007/978-1-4419-8632-0_40 |
0.322 |
|
| 1997 |
Zhou H, Huiatt TW, Robson RM, Sernett SW, Graves DJ. Characterization of ADP-Ribosylation Sites on Desmin and Restoration of Desmin Intermediate Filament Assembly by De-ADP-Ribosylation: Volume334,Number 2 (1996), pages 214–222 Archives of Biochemistry and Biophysics. 338. DOI: 10.1006/Abbi.1996.9826 |
0.301 |
|
| 1996 |
Zhou H, Huiatt TW, Robson RM, Sernett SW, Graves DJ. Characterization of ADP-ribosylation sites on desmin and restoration of desmin intermediate filament assembly by De-ADP-ribosylation Archives of Biochemistry and Biophysics. 334: 214-222. PMID 8900395 DOI: 10.1006/Abbi.1996.0449 |
0.365 |
|
| 1996 |
Songyang Z, Lu KP, Kwon YT, Tsai LH, Filhol O, Cochet C, Brickey DA, Soderling TR, Bartleson C, Graves DJ, DeMaggio AJ, Hoekstra MF, Blenis J, Hunter T, Cantley LC. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. Molecular and Cellular Biology. 16: 6486-93. PMID 8887677 DOI: 10.1128/Mcb.16.11.6486 |
0.557 |
|
| 1996 |
Huang HY, Zhou H, Huiatt TW, Graves DJ. Target proteins for arginine-specific mono(ADP-ribosyl) transferase in membrane fractions from chick skeletal muscle cells Experimental Cell Research. 226: 147-153. PMID 8660950 DOI: 10.1006/Excr.1996.0213 |
0.35 |
|
| 1995 |
Imparl JM, Senshu T, Graves DJ. Studies of calcineurin-calmodulin interaction: Probing the role of arginine residues using peptidylarginine deiminase Archives of Biochemistry and Biophysics. 318: 370-377. PMID 7733665 DOI: 10.1006/Abbi.1995.1242 |
0.4 |
|
| 1995 |
Luo S, Martin BL, Senshu T, Graves DJ. Enzymatic deimination of glycogen phosphorylase and a peptide of the phosphorylation site: Identification of modification and roles in phosphorylation and activity Archives of Biochemistry and Biophysics. 318: 362-369. PMID 7733664 DOI: 10.1006/Abbi.1995.1241 |
0.448 |
|
| 1995 |
Huang CYF, Yuan CJ, Blumenthal DK, Graves DJ. Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase γ-subunit Journal of Biological Chemistry. 270: 7183-7188. PMID 7706257 DOI: 10.1074/Jbc.270.13.7183 |
0.405 |
|
| 1994 |
Huang CY, Yuan CJ, Luo S, Graves DJ. Mutational analyses of the metal ion and substrate binding sites of phosphorylase kinase gamma subunit. Biochemistry. 33: 5877-83. PMID 8180216 DOI: 10.1021/Bi00185A027 |
0.331 |
|
| 1994 |
Luo S, Huang CYF, McClelland JF, Graves DJ. A study of protein secondary structure by Fourier transform infrared/photoacoustic spectroscopy and its application for recombinant proteins Analytical Biochemistry. 216: 67-76. PMID 8135368 DOI: 10.1006/Abio.1994.1009 |
0.346 |
|
| 1993 |
Martin BL, Graves DJ. Hydrolysis of trifluoroethyl phosphate as evidence that the serine and tyrosine phosphatase activities of calcineurin share the same specificity determinant Biochemical and Biophysical Research Communications. 194: 150-156. PMID 8392834 DOI: 10.1006/Bbrc.1993.1797 |
0.42 |
|
| 1993 |
Yuan CJ, Huang CYF, Graves DJ. Phosphorylase kinase, a metal ion-dependent dual specificity kinase Journal of Biological Chemistry. 268: 17683-17686. PMID 8349652 |
0.32 |
|
| 1993 |
Huang HY, Graves DJ, Robson RM, Huiatt TW. ADP-ribosylation of the intermediate filament protein desmin and inhibition of desmin assembly in vitro by muscle ADP-ribosyltransferase Biochemical and Biophysical Research Communications. 197: 570-577. PMID 8267592 DOI: 10.1006/Bbrc.1993.2517 |
0.425 |
|
| 1993 |
Huang CYF, Yuan CJ, Livanova NB, Graves DJ. Expression, purification, characterization, and deletion mutations of phosphorylase kinase γ subunit: identification of an inhibitory domain in the γ subunit Molecular and Cellular Biochemistry. 127: 7-18. PMID 7935363 DOI: 10.1007/Bf01076753 |
0.358 |
|
| 1992 |
Kharadia SV, Huiatt TW, Huang HY, Peterson JE, Graves DJ. Effect of an arginine-specific ADP-ribosyltransferase inhibitor on differentiation of embryonic chick skeletal muscle cells in culture. Experimental Cell Research. 201: 33-42. PMID 1612127 DOI: 10.1016/0014-4827(92)90345-9 |
0.337 |
|
| 1991 |
Takrama JF, Graves DJ. Solution conformations of the N-terminal CNBr fragment of glycogen phosphorylase and its interaction with calmodulin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1077: 371-378. PMID 2029536 DOI: 10.1016/0167-4838(91)90553-C |
0.307 |
|
| 1991 |
Kee SM, Yuan CJ, Graves DJ. High-performance liquid chromatographic separation and renaturation of protein kinase subunits: Application to catalytic subunit of phosphorylase kinase Methods in Enzymology. 200: 436-443. PMID 1956330 DOI: 10.1016/0076-6879(91)00160-X |
0.372 |
|
| 1991 |
Wang H, Graves DJ. Calcineurin-catalyzed reaction with phosphite and phosphate esters of tyrosine Biochemistry. 30: 3019-3024. PMID 1848782 DOI: 10.1021/Bi00226A006 |
0.346 |
|
| 1990 |
Kim ES, Graves DJ. Development of a high-performance liquid chromatography assay method and characterization of adenosine diphosphate-ribosylarginine hydrolase in skeletal muscle Analytical Biochemistry. 187: 251-257. PMID 2382826 DOI: 10.1016/0003-2697(90)90452-F |
0.351 |
|
| 1990 |
Martin BL, Wu D, Tabatabai L, Graves DJ. Formation of cyclic imide-like structures upon the treatment of calmodulin and a calmodulin peptide with heat Archives of Biochemistry and Biophysics. 276: 94-101. PMID 2105083 DOI: 10.1016/0003-9861(90)90014-P |
0.354 |
|
| 1990 |
Harris WR, Graves DJ. Kinetic analysis of the separate phosphorylation events in the phosphorylase kinase reaction Archives of Biochemistry and Biophysics. 276: 102-108. PMID 2105076 DOI: 10.1016/0003-9861(90)90015-Q |
0.414 |
|
| 1989 |
Chen LR, Yuan CJ, Somasekhar G, Wejksnora P, Peterson JE, Myers AM, Graves L, Cohen PT, da Cruz e Silva EF, Graves DJ. Expression and characterization of the tau subunit of phosphorylase kinase. Biochemical and Biophysical Research Communications. 161: 746-53. PMID 2735920 DOI: 10.1016/0006-291X(89)92663-6 |
0.413 |
|
| 1989 |
Yuan CJ, Graves DJ. Ca2+-independent interaction of the γ subunit of phosphorylase kinase with dansyl-calmodulin Archives of Biochemistry and Biophysics. 274: 317-326. PMID 2508559 DOI: 10.1016/0003-9861(89)90445-1 |
0.335 |
|
| 1988 |
Soman G, Graves DJ. Endogenous ADP-ribosylation in skeletal muscle membranes Archives of Biochemistry and Biophysics. 260: 56-66. PMID 3124754 DOI: 10.1016/0003-9861(88)90424-9 |
0.33 |
|
| 1987 |
Chang YC, Scott RD, Graves DJ. Function of pyridoxal 5′-phosphate in glycogen phosphorylase: A model study using 6-fluoro-5′-deoxypyridoxal- and 5′-deoxypyridoxal-reconstituted enzymes Biochemistry. 26: 360-367. PMID 3828313 |
0.318 |
|
| 1987 |
Bollen M, Kee SM, Graves DJ, Soderling TR. Substrate specificity of phosphorylase kinase: effects of heparin and calcium. Archives of Biochemistry and Biophysics. 254: 437-47. PMID 3107473 DOI: 10.1016/0003-9861(87)90122-6 |
0.62 |
|
| 1986 |
Chang YC, Soman G, Graves DJ. Identification of an enzymatic activity that hydrolyzes protein-bound ADP-ribose in skeletal muscle Biochemical and Biophysical Research Communications. 139: 932-939. PMID 3768008 DOI: 10.1016/S0006-291X(86)80267-4 |
0.362 |
|
| 1986 |
Graves DJ. Function of pyridoxal 5′-phosphate in glycogen phosphorylase:19F NMR and kinetic studias of phosphorylase reconstituted with 6-fluoropyridoxal and 6-fluoropyridoxal phosphate Biochemistry. 25: 1932-1939. PMID 3707920 DOI: 10.1021/Bi00356A015 |
0.368 |
|
| 1986 |
Harris WR, Miller JF, Graves DJ. Purification and characterization of a glycogen phosphorylase analog missing the amino-terminal segment Archives of Biochemistry and Biophysics. 250: 446-455. PMID 3096212 DOI: 10.1016/0003-9861(86)90748-4 |
0.372 |
|
| 1986 |
Soman G, Graves DJ. Chemical modification of rabbit skeletal muscle phosphorylase kinase with phenylglyoxal Archives of Biochemistry and Biophysics. 248: 341-352. PMID 3089165 DOI: 10.1016/0003-9861(86)90430-3 |
0.48 |
|
| 1986 |
Soman G, Narayanan J, Martin BL, Graves DJ. Use of substituted (benzylidineamino)guanidines in the study of guanidino group specific ADP-ribosyltransferase Biochemistry. 25: 4113-4119. PMID 3017413 DOI: 10.1021/Bi00362A019 |
0.305 |
|
| 1985 |
Scott RD, Chang YC, Graves DJ, Metzler DE. Studies of 6-fluoropyridoxal and 6-fluoropyridoxamine 5'-phosphates in cytosolic aspartate aminotransferase. Biochemistry. 24: 7668-81. PMID 4092032 DOI: 10.1021/Bi00347A026 |
0.371 |
|
| 1984 |
Graves DJ, Soman G, Hurst MO, Chang YC. Involvement of guanidino groups in anion-binding sites and in enzyme-catalyzed covalent modification reactions Current Topics in Cellular Regulation. 24: 181-188. PMID 6499519 DOI: 10.1016/B978-0-12-152824-9.50024-1 |
0.324 |
|
| 1984 |
Soman G, Mickelson JR, Louis CF, Graves DJ. NAD: Guanidino group specific mono ADP-ribosyltransferase activity in skeletal muscle Biochemical and Biophysical Research Communications. 120: 973-980. PMID 6329192 DOI: 10.1016/S0006-291X(84)80202-8 |
0.377 |
|
| 1984 |
Soman G, Miller JF, Graves DJ. [41] Use of guanylhydrazones as substrates for guanidine-specific mono-ADP-ribosyltransferases Methods in Enzymology. 106: 403-410. PMID 6092832 DOI: 10.1016/0076-6879(84)06043-2 |
0.302 |
|
| 1983 |
Jesse Chan KF, Graves DJ. [28] Separation of the subunits of muscle phosphorylase kinase Methods in Enzymology. 99: 259-267. PMID 6645976 DOI: 10.1016/0076-6879(83)99061-4 |
0.438 |
|
| 1983 |
Chang YC, McCalmont T, Graves DJ. Functions of the 5′-phosphoryl group of pyridoxal 5′-phosphate in phosphorylase: A study using pyridoxal-reconstituted enzyme as a model system Biochemistry. 22: 4987-4993. PMID 6639940 DOI: 10.1021/Bi00290A017 |
0.43 |
|
| 1983 |
Soman G, Chang YC, Graves DJ. Effect of oxyanions of the early transition metals on rabbit skeletal muscle phosphorylase Biochemistry. 22: 4994-5000. PMID 6416293 DOI: 10.1021/Bi00290A018 |
0.391 |
|
| 1983 |
Graves DJ. Use of peptide substrates to study the specificity of phosphorylase kinase phosphorylation. Methods in Enzymology. 99: 268-78. PMID 6358786 DOI: 10.1016/0076-6879(83)99062-6 |
0.417 |
|
| 1983 |
Soman G, Tomer KB, Graves DJ. Assay of mono ADP-ribosyltransferase activity by using guanylhydrazones Analytical Biochemistry. 134: 101-110. PMID 6318594 DOI: 10.1016/0003-2697(83)90269-5 |
0.321 |
|
| 1982 |
Kobayashi M, Graves DJ. Rabbit liver phosphorylase: Improvement of the purification procedure and assay of the inactive b form Analytical Biochemistry. 122: 94-99. PMID 6808862 DOI: 10.1016/0003-2697(82)90256-1 |
0.376 |
|
| 1982 |
Yan SCB, Graves DJ. Inactivation and reactivation of phosphoprotein phosphatase Molecular and Cellular Biochemistry. 42: 21-29. PMID 6278282 DOI: 10.1007/Bf00223535 |
0.36 |
|
| 1981 |
Miller JF, Graves DJ. Effect of 1,2-dimethoxyethane on potato phosphorylase for polysaccharide specificity Biochemical and Biophysical Research Communications. 99: 1377-1383. PMID 7259781 DOI: 10.1016/0006-291X(81)90771-3 |
0.385 |
|
| 1981 |
Miller JF, Seybold MC, Graves DJ. Use of arginine compounds to examine the role of an essential arginine in the mechanism of glycogen phosphorylase Biochemistry. 20: 4579-4584. PMID 6794599 DOI: 10.1021/Bi00519A010 |
0.409 |
|
| 1981 |
Uhing RJ, Lentz SR, Graves DJ. Effects of 1,2-dimethoxyethane on the catalytic and coenzyme properties of glycogen phosphorylase. Biochemistry. 20: 2537-44. PMID 6786337 DOI: 10.1021/Bi00512A027 |
0.442 |
|
| 1980 |
Graves DJ, Martensen TM. [13] The use of alternative substrates to study enzyme-catalyzed chemical modification Methods in Enzymology. 64: 325-340. DOI: 10.1016/S0076-6879(80)64015-4 |
0.371 |
|
| 1979 |
Viriya J, Graves DJ. Phosphorylation of synthetic peptide analogs of the phosphorylatable site of phosphorylase b with phosphorylase kinase Biochemical and Biophysical Research Communications. 87: 17-24. PMID 454396 DOI: 10.1016/0006-291X(79)91641-3 |
0.368 |
|
| 1979 |
Carlson GM, Bechtel PJ, Graves DJ. Chemical and regulatory properties of phosphorylase kinase and cyclic AMP-dependent protein kinase Advances in Enzymology and Related Areas of Molecular Biology. 50: 41-115. PMID 227235 DOI: 10.1002/9780470122952.Ch2 |
0.36 |
|
| 1977 |
Parrish RF, Uhing RJ, Graves DJ. Effect of phosphate analogues on the activity of pyridoxal reconstituted glycogen phosphorylase. Biochemistry. 16: 4824-31. PMID 911792 DOI: 10.1021/Bi00641A011 |
0.415 |
|
| 1977 |
Kemp BE, Graves DJ, Benjamini E, Krebs EG. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase. The Journal of Biological Chemistry. 252: 4888-94. PMID 194899 |
0.52 |
|
| 1976 |
Carlson GM, Graves DJ. Site of action and biphasic effect of neutral salts in the phosphorylase kinase reaction Biochemistry. 15: 4476-4481. PMID 974070 DOI: 10.1021/Bi00665A022 |
0.423 |
|
| 1976 |
Parrish RF, Graves DJ. Irreversible inhibition of phosphorylase phosphatase by fluorophosphate Biochemical and Biophysical Research Communications. 70: 1290-1296. PMID 182164 DOI: 10.1016/0006-291X(76)91042-1 |
0.405 |
|
| 1975 |
Carty TJ, Tu JI, Graves DJ. Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties Journal of Biological Chemistry. 250: 4980-4985. PMID 1150650 |
0.33 |
|
| 1975 |
Graves DJ, Carlson GM, Skuster JR, Parrish RF, Carty TJ, Tessmer GW. Pyridoxal phosphate dependent conformational states of glycogen phosphorylase as probed by interconverting enzymes Journal of Biological Chemistry. 250: 2254-2258. PMID 163824 |
0.343 |
|
| 1973 |
Tu JI, Graves DJ. Inhibition of the phosphorylase kinase catalyzed reaction by glucose-6-P Biochemical and Biophysical Research Communications. 53: 59-65. PMID 4741557 DOI: 10.1016/0006-291X(73)91400-9 |
0.388 |
|
| 1973 |
Kimi G, Graves DJ. On the hysteretic response of rabbit skeletal muscle phosphorylase kinase Biochemistry. 12: 2090-2095. PMID 4735880 DOI: 10.1021/Bi00735A011 |
0.45 |
|
| 1973 |
Tu JI, Graves DJ. Association dissociation properties of sodium borohydride reduced phosphorylase b Journal of Biological Chemistry. 248: 4617-4622. PMID 4718737 |
0.335 |
|
| 1973 |
Anderson RA, Graves DJ. Chemistry of the adenosine monophosphate site of rabbit muscle glycogen phosphorylase. I. Hydrophobic nature and affinity labeling of the allosteric site Biochemistry. 12: 1895-1900. PMID 4704477 DOI: 10.1021/Bi00734A009 |
0.373 |
|
| 1973 |
Graves DJ, Hayakawa T, Horvitz RA, Beckman E, Krebs EG. Studies on the subunit structure of trypsin-activated phosphorylase kinase. Biochemistry. 12: 580-5. PMID 4691509 DOI: 10.1021/Bi00728A003 |
0.579 |
|
| 1973 |
Tessmer G, Graves DJ. The phosphorylase kinase reaction on a peptide derived from glycogen phosphorylase Biochemical and Biophysical Research Communications. 50: 1-7. PMID 4683623 DOI: 10.1016/0006-291X(73)91054-1 |
0.431 |
|
| 1973 |
Anderson RA, Parrish RF, Graves DJ. Chemistry of the adenosine monophosphate site of rabbit muscle glycogen phosphorylase. II. Properties of 8-[m-(m-fluorosulfonylbenzamido)benzylthio]adenine-modified phosphorylase Biochemistry. 12: 1901-1906. PMID 4350104 DOI: 10.1021/Bi00734A010 |
0.435 |
|
| 1972 |
Graves DJ, Wang JH. 15 α-Glucan Phosphorylases-Chemical and Physical Basis of Catalysis and Regulation Enzymes. 7: 435-482. DOI: 10.1016/S1874-6047(08)60459-X |
0.61 |
|
| 1970 |
Huang CY, Graves DJ. Correlation between subunit interactions and enzymatic activity of phosphorylase a. Method for determining equilibrium constants from initial rate measurements Biochemistry. 9: 660-671. PMID 5461220 DOI: 10.1021/Bi00805A028 |
0.397 |
|
| 1970 |
Chao J, Graves DJ. pH dependence of the kinetic parameters of maltodextrin phosphorylase Biochemical and Biophysical Research Communications. 40: 1398-1403. PMID 4933689 DOI: 10.1016/0006-291X(70)90022-7 |
0.314 |
|
| 1969 |
Chao J, Johnson GF, Graves DJ. Kinetic mechanism of maltodextrin phosphorylase Biochemistry. 8: 1459-1466. PMID 4897523 DOI: 10.1021/Bi00832A022 |
0.331 |
|
| 1969 |
Assaf SA, Graves DJ. Structural and catalytic properties of lobster muscle glycogen phosphorylase Journal of Biological Chemistry. 244: 5544-5555. DOI: 10.31274/Rtd-180813-396 |
0.393 |
|
| 1968 |
Philip G, Graves DJ. Dinitrophenylation of glycogen phosphorylase. I. Preparation and properties of active dinitrophenyl derivatives Biochemistry. 7: 2093-2101. PMID 5660040 DOI: 10.1021/Bi00846A011 |
0.367 |
|
| 1968 |
Johnson GF, Philip G, Graves DJ. Dinitrophenylation of glycogen phosphorylase. II. Circular dichroism of the modified enzyme Biochemistry. 7: 2101-2105. DOI: 10.1021/Bi00846A012 |
0.304 |
|
| 1967 |
Sealock RW, Graves DJ. Effect of salt solutions on glycogen phosphorylase. a possible role of the phosphoryl group in phosphorylase a Biochemistry. 6: 201-207. PMID 4291566 DOI: 10.1021/Bi00853A032 |
0.431 |
|
| 1966 |
Johnson GF, Graves DJ. Circular dichroism and optical rotatory dispersion of glycogen phosphorylase Biochemistry. 5: 2906-2911. PMID 5961878 DOI: 10.1021/Bi00873A019 |
0.34 |
|
| 1965 |
Wang JH, Shonka ML, Graves DJ. The effect of glucose on the sedimentation and catalytic activity of glycogen phosphorylase Biochemical and Biophysical Research Communications. 18: 131-135. PMID 14265745 DOI: 10.1016/0006-291X(65)90895-8 |
0.687 |
|
| 1965 |
Wang JH, Shonka ML, Graves DJ. Influence of Carbohydrates on Phosphorylase Structure and Activity. I. Activation by Preincubation with Glycogen* Biochemistry. 4: 2296-2301. DOI: 10.1021/Bi00887A006 |
0.66 |
|
| 1965 |
Graves DJ, Sealock RW, Wang JH. Cold Inactivation of Glycogen Phosphorylase* Biochemistry. 4: 290-296. DOI: 10.1021/Bi00878A017 |
0.643 |
|
| 1964 |
Wang JH, Graves DJ. The relationship of the dissociation to the catalytic activity of glycogen phosphorylase A Biochemistry. 3: 1437-1445. PMID 14231906 DOI: 10.1021/Bi00898A008 |
0.685 |
|
| 1960 |
GRAVES DJ, FISCHER EH, KREBS EG. Specificity studies on muscle phosphorylase phosphatase. The Journal of Biological Chemistry. 235: 805-9. PMID 13829077 |
0.437 |
|
| 1959 |
KREBS EG, GRAVES DJ, FISCHER EH. Factors affecting the activity of muscle phosphorylase b kinase. The Journal of Biological Chemistry. 234: 2867-73. PMID 14411853 |
0.504 |
|
| 1959 |
FISCHER EH, GRAVES DJ, CRITTENDEN ER, KREBS EG. Structure of the site phosphorylated in the phosphorylase b to a reaction. The Journal of Biological Chemistry. 234: 1698-704. PMID 13672948 |
0.475 |
|
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