Phosphorylase Kinase

Enzymes

Volumn 17, Issue C, 1986, Pages 395-459

  Pickett Gies, Cheryl A ^a   Walsh, Donal A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 77956897434     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6047(08)60435-7     Document Type: Article

References (216)

1. Sutherland, E.W., Recent Prog. Horm. Res. 5 (1950), 441–463.
2. Cori, C.F., Cori, G.T., JBC 158 (1945), 341–345.
3. Burnett, G., Kennedy, E.P., JBC 211 (1954), 969–980.
4. Krebs, E.G., Fischer, E.H., BBA 20 (1956), 150–157.
5. Lipkin, D., Markham, R., Cook, W.H., J. Am. Chem. Soc., 81, 1959, 6075.
6. Robison, G.A., Butcher, R.W., Sutherland, E.W., Cyclic AMP., 1971, Academic Press, New York.
7. Krebs, E.G., Love, D.S., Bratvold, G.E., Trayser, K.A., Meyer, W.L., Fischer, E.H., Biochemistry 3 (1964), 1022–1033.
8. DeLange, R.J., Kemp, R.G., Riley, W.D., Cooper, R.A., Krebs, E.G., JBC 243 (1968), 2200–2208.
9. Walsh, D.A., Perkins, J.P., Krebs, E.G., JBC 243 (1968), 3763–3774.
10. Chan, K.J., Graves, D.J., Cheung, W.Y., (eds.) “Calcium and Cell Function’, 5, 1984, Academic Press, New York, 1–31.
11. Carlson, G.M., Bechtel, P.J., Graves, D.J., Adv. Enzymol. Relat. Areas Mol. Biol. 50 (1979), 41–115.
12. Malencik, D.A., Fischer, E.H., Cheung, W.Y., (eds.) “Calcium and Cell Function’, 2, 1982, Academic Press, New York, 161–188.
13. Hayakawa, T., Perkins, J.P., Walsh, D.A., Krebs, E.G., Biochemistry 12 (1973), 567–573.
14. Cohen, P., EJB 34 (1973), 1–14.
15. Sharma, R.K., Tam, S.W., Waisman, D.M., Wang, J.H., JBC 255 (1980), 11102–11105.
16. Jennissen, H.P., Horl, W.H., Heilmeyer, L.M.G. Jr., Hoppe-Seyler's Z. Physiol. Chem. 354 (1973), 236–237.
17. Jennissen, H.P., Heilmeyer, L.M.G. Jr., Biochemistry 14 (1975), 754–760.
18. Hallenbeck, P.C., Walsh, D.A., JBC 258 (1983), 13493–13501.
19. Gross, S.R., Bromwell, K., ABB 184 (1977), 1–11.
20. Pocinwong, S., Blum, H., Malencik, D., Fischer, E.H., Biochemistry 20 (1981), 7219–7226.
21. Tam, S.W., Sharma, R.K., Wang, J.H., JBC 257 (1982), 14907–14913.
22. Cooper, R.H., Sul, H.S., McCullough, T.E., Walsh, D.A., JBC 255 (1980), 11794–11801.
23. Nikolaropoulos, S., Sotiroudis, T.G., EJB 151 (1985), 467–473.
24. Chrisman, T.D., Jordan, J.E., Exton, J.H., JBC 257 (1982), 10798–10804.
25. Pohlig, G., Wingender-Drissen, R., Becker, J.U., BBRC 114 (1983), 331–338.
26. Wingender-Drissen, R., Becker, J.U., FEBS Lett. 163 (1983), 33–36.
27. Jennissen, H.P., Heilmeyer, L.M.G. Jr., FEBS Lett. 42 (1974), 77–80.
28. Crabb, J.W., Heilmeyer, L.M.G. Jr., JBC 259 (1984), 6346–6350 14314.
29. Reimann, E.M., Titani, K., Ericsson, L.H., Wade, R.D., Fischer, E.H., Walsh, K.A., Biochemistry 23 (1984), 4185–4192.
30. Grand, R.J., Shenolikar, S., Cohen, P., EJB 113 (1981), 359–367.
31. Burchell, A., Cohen, P.T.W., Cohen, P., FEBS Lett. 67 (1976), 17–22.
32. Pickett-Gies, C.A., Carlsen, R., Angelos, K.L., Walsh, D.A., JBC, 1986 (in press).
33. Lawrence, J.C. Jr., Krsek, J.A., Salsgiver, W.J., Hiken, J.F., Salmons, S., Smith, R.L., Am. J. Physiol. 250 (1986), C84–C89.
34. Schwartz, A., Entman, M.L., Kaniike, K., Lane, L.K., Van Winkle, B., Bornet, E.P., BBA 426 (1976), 57–72.
35. Horl, W.H., Heilmeyer, L.M.G. Jr., Biochemistry 17 (1978), 766–772.
36. Le Peuch, C.J., Le Peuch, D.A., Demaille, G., Ann. N.Y. Acad. Sci. 402 (1982), 549–557.
37. Hessova, Z., Varsanyi, M., Heilmeyer, L.M.G. Jr., EJB 146 (1985), 107–115.
38. Cohen, P., Curr. Top. Cell. Regul. 14 (1978), 117–196.
39. Trempe, M.R., Carlson, G.M., Hainfeld, J.F., Furcinitti, P.S., Wall, J.S., JBC 261 (1986), 2882–2889.
40. Lambooy, P.K., Steiner, R.F., ABB 213 (1982), 551–556.
41. Picton, C., Klee, C.B., Cohen, P., EJB 111 (1980), 553–561.
42. Fitzgerald, T.J., Carlson, G.M., JBC 259 (1984), 3266–3274.
43. Picton, C., Klee, C.B., Cohen, P., Cell Calcium 2 (1981), 281–294.
44. Chan, K.-F.J., Graves, D.J., JBC 257 (1982), 5939–5947.
45. Skuster, J.R., Chan, K.-F.J., Graves, D.J., JBC 255 (1980), 2203–2210.
46. Kee, S.M., Graves, D.J., FP, 44, 1985, 1074.
47. Cohen, P., Burchell, A., Foulkes, J.G., Cohen, P.T.W., Vanaman, T.C., Nairn, A.C., FEBS Lett. 92 (1978), 287–293.
48. Jennissen, H.P., Horl, W.H., Groschel-Stewart, U., Velick, S.F., Heilmeyer, L.M.G. Jr., Shaltiel, S., (eds.) “Metabolic Interconversions of Enzymes’, 1976, Springer-Verlag, Berlin and New York, 19–26.
49. Hayakawa, T., Perkins, J.P., Krebs, E.G., Biochemistry 12 (1973), 574–580.
50. Chan, K.-F.J., Graves, D.J., JBC 257 (1982), 5948–5955.
51. Chan, K.-F.J., Graves, D.J., JBC 257 (1982), 5956–5961.
52. Gulyaeva, N.B., Vul'fson, P.L., Severin, E.S., Biokhimiya 43 (1977), 373–381.
53. King, M.M., Carlson, G.M., Haley, B.E., JBC 257 (1982), 14058–14065.
54. King, M.M., Carlson, G.M., Biochemistry 20 (1981), 4382–4387.
55. King, M.M., Carlson, G.M., FEBS Lett. 140 (1982), 131–134.
56. Fischer, E.H., Alaba, J.O., Brautigan, D.L., Kerrick, W.G.D., Malencik, D.A., Moeschler, H.J., Picton, C., Pocinwong, S., Li, C.H., (eds.) “Versatility of Proteins’, 1978, Academic Press, New York, 133–145.
57. Killilea, S.D., Ky, N.M., ABB 221 (1983), 333–342.
58. Sotiroudis, T.G., Nikolaropoulos, S., FEBS Lett. 176 (1984), 421–425.
59. Crabb, J.W., Sotiroudis, T.G., Heilmeyer, L.M.G. Jr., JBC, 1986 (submitted for publication).
60. Carlson, G.M., Graves, D.J., JBC 251 (1976), 7480–7486.
61. Dickneite, G., Jennissen, H.P., Heilmeyer, L.M.G. Jr., FEBS Lett. 87 (1978), 297–302.
62. King, M.M., Carlson, G.M., Biochemistry 20 (1981), 4387–4393.
63. Kilimann, M.W., Heilmeyer, L.M.G. Jr., Biochemistry 21 (1982), 1727–1734.
64. Kilimann, M.W., Heilmeyer, L.M.G. Jr., Biochemistry 21 (1982), 1735–1739.
65. Georgoussi, Z., Heilmeyer, L.M.G. Jr., Biochemistry, 1986 (in press).
66. Hessova, Z., Thieleczek, R., Varsanyi, M., Falkenberg, F.W., Heilmeyer, L.M.G. Jr., JBC 260 (1985), 10111–10117.
67. Grand, R.J., Shenolikar, S., Cohen, P., EJB 113 (1981), 359–367.
68. Heilmeyer, L.M.G. Jr., Groschel-Stewart, U., Jahnke, U., Kilimann, M.W., Kohse, K.P., Varsanyi, M., Adv. Enzyme Regul. 18 (1980), 121–144.
69. Kilimann, M., Heilmeyer, L.M.G. Jr., EJB 73 (1977), 191–197.
70. Kohse, K.P., Heilmeyer, L.M.G. Jr., EJB 117 (1981), 507–513.
71. J.T. Stull, M.H. Nunnally, C.H. Michnoff (1986). This volume, Chapter 4.
72. Wang, J.H., Stull, J.T., Huang, T.-S., Krebs, E.G., JBC 251 (1976), 4521–4527.
73. Carlson, G.M., Graves, D.J., JBC 251 (1976), 7480–7486.
74. Graves, D.J., Hayakawa, T., Horvitz, R.A., Beckman, E., Krebs, E.G., Biochemistry 12 (1973), 580–585.
75. Sul, H.S., Dirden, B., Angelos, K.L., Hallenbeck, P., Walsh, D.A., Methods in Enzymology 99 (1983), 250–259.
76. Jennissen, H.P., Petersen-Von Gehr, J.K.H., Botzet, G., EJB 147 (1985), 619–630.
77. Clerch, L.B., Huijing, F., BBA 268 (1972), 654–662.
78. Kim, G., Graves, D.J., Biochemistry 12 (1973), 2090–2095.
79. Singh, T.J., Akatsuka, A., Huang, K.-P., ABB 218 (1982), 360–368.
80. Villar-Palasi, C., Wei, S.H., PNAS 67 (1970), 345–350.
81. Tabatabai, L.B., Graves, D.J., JBC 253 (1978), 2196–2202.
82. Meyer, W.L., Fischer, E.H., Krebs, E.G., Biochemistry 3 (1964), 1033–1039.
83. Cheng, A., Fitzgerald, T.J., Carlson, G.M., JBC 260 (1985), 2535–2542.
84. Hayes, J.S., Mayer, S.E., Am. J. Physiol. 240 (1981), E340–E349.
85. Ramachandran, C., Angelos, K.L., Walsh, D.A., JBC 257 (1982), 1448–1457.
86. King, M.M., Carlson, G.M., ABB 209 (1981), 517–523.
87. King, M.M., Carlson, G.M., JBC 256 (1981), 11058–11064.
88. Hallenbeck, P., Walsh, D.A., JBC 261 (1986), 5442–5449.
89. Stull, J.T., England, P.J., Brostrom, C.O., Krebs, E.G., Cold Spring Harbor Symp. Quant. Biol. 37 (1972), 263–265.
90. Tessmar, G., Graves, D.J., BBRC 50 (1973), 1–7.
91. Krebs, E.G., Kent, A.B., Fischer, E.H., JBC 231 (1958), 73–83.
92. Shizuta, Y., Khandelwal, R.L., Maller, J.L., Vandenheede, J.R., Krebs, E.G., JBC 252 (1977), 3408–3413.
93. Nolan, C., Novoa, W.B., Krebs, E.G., Fischer, E.H., Biochemistry 3 (1964), 542–551.
94. Tessmar, G.W., Skuster, J.R., Tabatabai, L.B., Graves, D.J., JBC 252 (1977), 5666–5671.
95. Graves, D.J., Methods in Enzymology 99 (1983), 268–278.
96. Viriya, J., Graves, D.J., BBRC 87 (1979), 17–24.
97. Chan, K.-F.J., Hurst, M.V., Graves, D.J., JBC 257 (1982), 3655–3659.
98. Kemp, B.E., John, M.J., Cold Spring Harbor Conf. Cell Proliferation 8 (1981), 331–342.
99. Soderling, T.R., Srivastava, A.K., Bass, M.A., Khatra, B., PNAS 76 (1979), 2536–2540.
100. Walsh, D.A., Perkins, J.P., Broström, C.O., Ho, E.S., Krebs, E.G., JBC 246 (1971), 1968–1976.
101. King, M.M., Fitzgerald, T.J., Carlson, G.M., JBC 258 (1983), 9925–9930.
102. De Paoli-Roach, A.A., Roach, P.J., Larner, J., JBC 254 (1979), 4212–4219.
103. Walsh, K.X., Millikin, D.M., Schlender, K.K., Reimann, E.M., JBC 254 (1979), 6611–6616.
104. Akatsuka, A., Singh, T.J., Huang, K.-P., JBC 259 (1984), 7878–7883.
105. Stull, J.T., Broström, C.O., Krebs, E.G., JBC 247 (1972), 5272–5274.
106. Perry, S.V., Cole, H.A., BJ 141 (1974), 733–743.
107. Moir, A.J.G., Cole, H.A., Perry, S.V., BJ 161 (1977), 371–382.
108. Louis, P.J.St., Sulakhe, P.V., Eur. J. Pharmacol. 43 (1977), 277–280.
109. De Paoli-Roach, A.A., Bingham, E.W., Roach, P.J., ABB 212 (1981), 229–236.
110. Singh, T.J., Akatsuka, A., Huang, K.-P., FEBS Lett. 159 (1983), 217–220.
111. Soderling, T.R., Sheorain, V.S., Ericsson, L.H., FEBS Lett. 106 (1979), 181–184.
112. K.L. Angelos, D.A. Walsh (unpublished observation).
113. Meyer, F., Heilmeyer, L.M.G. Jr., Haschke, R.H., Fischer, E.H., JBC 245 (1970), 6642–6648.
114. Jennissen, H.P., Horl, W.H., Groschel-Stewart, U., Velick, S.F., Heilmeyer, L.M.G. Jr., Shaltiel, S., (eds.) “Metabolic Interconversion of Enzymes’, 1975, Springer-Verlag, Berlin and New York, 19–26.
115. Dombradi, V.K., Silberman, S.R., Lee, E.Y.C., Caswell, A.H., Brandt, N.R., ABB 230 (1984), 615–630.
116. Flockhart, D.A., Freist, W., Hoppe, J., Lincoln, T.M., Corbin, J.D., EJB 140 (1984), 289–295.
117. Livanova, N.B., Silonova, G.V., Solovyeva, N.V., Andreeva, I.E., Ostrovskaya, M.V., Poglazov, B.F., Biochem. Int. 7 (1983), 95–105.
118. Huang, T.S., Bylund, D.B., Stull, J.T., Krebs, E.G., FEBS Lett. 42 (1974), 249–252.
119. Heilmeyer, L.M.G. Jr., Meyer, F., Haschke, R.H., Fischer, E.H., JBC 245 (1970), 6649–6656.
120. Gergely, P., Vereb, G., Bot, G., Arch. Biochem. Biophys. Acad. Sci. Hung., 10, 1975, 153.
121. Burger, D., Cox, J.A., Fischer, E.H., Stein, E.A., BBRC 105 (1982), 632–637.
122. Burger, D., Stein, E.A., Cox, J.A., JBC 258 (1983), 14733–14739.
123. Cohen, P., EJB 111 (1980), 563–574.
124. Brostrom, C.O., Hunkeler, F.L., Krebs, E.G., JBC 246 (1971), 1961–1967.
125. Ozawa, E., Hosoi, K., Ebashi, S., J. Biochem. (Tokyo) 61 (1967), 531–533.
126. Ebashi, S., Makoto, E., Ohtsuki, I., Q. Rev. Biophys. 2 (1969), 351–384.
127. Drummond, G.E., Harwood, J.P., Powell, C.A., JBC 244 (1969), 4235–4240.
128. Stull, J.T., Mayer, S.E., JBC 246 (1971), 5716–5723.
129. Vandenheede, J.R., De Wulf, H., Merlevede, W., EJB 101 (1979), 51–58.
130. Keppens, S., Vandenheede, J.R., De Wulf, H., BBA 496 (1977), 448–457.
131. Cherrington, A.D., Hundley, R.F., Dolgin, S., Exton, J.H., J. Cyclic Nucleotide Res. 3 (1977), 263–271.
132. Hutson, N.J., Brumley, F.T., Assimacopoulos, F.D., Harper, S.C., Exton, J.H., JBC 251 (1976), 5200–5208.
133. Cohen, S.M., Burt, C.T., PNAS 74 (1977), 4271–4275.
134. Heilmeyer, L.M.G. Jr., Jahnke, U., Kilimann, M.W., Kohse, K.P., Sperling, J.E., Cold Spring Harbor Conf. Cell Proliferation 8 (1981), 321–329.
135. De Paoli-Roach, A.A., Gibbs, J.B., Roach, P.J., FEBS Lett. 105 (1979), 321–324.
136. Shenolikar, S., Cohen, P.T.W., Cohen, P., Nairn, A.C., Perry, S.V., EJB 100 (1979), 329–337.
137. Wilkinson, J., EJB 103 (1980), 179–188.
138. Potter, J.D., Johnson, J.D., Dedman, J.R., Schreiber, W.E., Mandel, F., Jackson, R.L., Means, A.R., Wasserman, R.H., Corradino, R.A., Carafoli, E., Kretsinger, R.H., MacLennan, D.H., Siegel, F.L., (eds.) “Calcium Binding Proteins and Calcium Functions’, 1977, Elsevter/North-Holland, New York, 239–250.
139. Leavis, P.C., Kraft, E.L., ABB 186 (1978), 411–415.
140. Sigel, P., Pette, D., J. Histochem. Cytochem. 17 (1969), 225–237.
141. Pette, D., Acta Histochem. Suppl. 14 (1975), 47–68.
142. Yoshikawa, K., Usui, H., Imazu, M., Takeda, M., Ebashi, S., EJB 136 (1983), 413–419.
143. Wanson, J.-C., Drochmans, P., J. Cell Biol. 54 (1972), 206–224.
144. DiMauro, S., Trojaborg, W., Gambetti, P., Rowland, L.P., ABB 144 (1971), 413–422.
145. Bergamini, C., Buc, H., Morange, M., FEBS Lett. 81 (1977), 166–172.
146. Reddy, N.B., Oliver, K.L., Festoff, B.W., Engel, W.K., BBA 540 (1978), 371–378.
147. Kasvinsky, P.J., Madsen, N.B., Sygusch, J., Fletterick, R.J., JBC 253 (1978), 3343–3351.
148. Madsen, N.B., Kasvinsky, P.J., Fletterick, R.J., JBC 253 (1978), 9097–9101.
149. Steiner, R.F., Marshall, L., BBA 707 (1982), 38–45.
150. Preiss, J., Walsh, D.A., Ginsberg, V., (eds.) “Biology of Carbohydrates’, 1, 1981, Wiley, New York, 199–314.
151. Busby, S.J.W., Gadian, D.G., Griffiths, J.R., Radda, G.K., Richards, R.E., EJB 63 (1976), 23–31.
152. Srivastava, A.K., Khatra, B.S., Soderling, T.R., ABB 205 (1980), 291–296.
153. Gergely, P., Vereb, G., Bot, G., BBA 429 (1976), 809–816.
154. Fischer, E.H., Krebs, E.G., FP 25 (1966), 1511–1520.
155. Entman, M.L., Kaniike, K., Goldstein, M.A., Nelson, T.E., Bornet, E.P., Futch, T.W., Schwartz, A., JBC 251 (1976), 3140–3146.
156. Entman, M.L., Bornet, E.P., Van Winkle, W.B., Goldstein, M.A., Schwartz, A., J. Mol. Cell. Cardiol. 9 (1977), 515–528.
157. Kayikawa, N., Kishimoto, A., Shiota, M., Nishizuka, Y., Methods in Enzymology 102 (1983), 279–290.
158. Mayer, S.E., Krebs, E.G., JBC 245 (1970), 3153–3160.
159. Pickett-Gies, C.A., Walsh, D.A., JBC 260 (1985), 2046–2056.
160. Kilimann, M.W., Schnackerz, K.D., Heilmeyer, L.M.G. Jr., Biochemistry 23 (1984), 112–117.
161. Cooper, R.H., Sul, H.S., Walsh, D.A., JBC 256 (1981), 8030–8038.
162. Pickett-Gies, C.A., Carlsen, R., Anderson, L.J., Angelos, K.L., Walsh, D.A., JBC, 261, 1986 (in press).
163. Lincoln, T.M., Corbin, J.D., PNAS 74 (1977), 3239–3243.
164. Cohen, P., FEBS Lett. 119 (1980), 301–306.
165. Waisman, D.M., Singh, T.J., Wang, J.H., JBC 253 (1978), 3387–3390.
166. Singh, T.J., Akatsuka, A., Huang, K.-P., JBC 257 (1982), 13379–13384.
167. Singh, T.J., Akatsuka, A., Huang, K.P., JBC 259 (1984), 12857–12864.
168. Kishimoto, A., Takai, Y., Nishizuka, Y., JBC 252 (1977), 7449–7452.
169. Takai, Y., Kishimoto, A., Iwasa, Y., Kawahara, Y., Mori, T., Nishizuka, Y., JBC 254 (1979), 3692–3695.
170. Cook, P.F., Neville, M.E., Vrana, K.E., Hartl, F.T., Roskoski, R.R., Biochemistry 21 (1982), 5794–5799.
171. Singh, T.J., Wang, J.H., JBC 252 (1977), 625–632.
172. Cohen, P., Watson, D.C., Dixon, G.H., EJB 51 (1975), 79–92.
173. Sul, H.S., Cooper, R.H., Whitehouse, S., Walsh, D.A., JBC 257 (1982), 3484–3490.
174. Cox, D.E., Edström, R.D., JBC 257 (1982), 12728–12733.
175. Singh, T.J., Huang, K.-P., BBRC 130 (1985), 1308–1313.
176. Yeaman, S.J., Cohen, P., Watson, D.C., Dixon, G.H., BJ 162 (1977), 411–421.
177. Cheng, H.-C., Kemp, B.E., Pearson, R.B., Smith, A.J., Misconi, L., Van Patten, S.M., Walsh, D.A., JBC 261 (1986), 989–992.
178. Sul, H.S., Walsh, D.A., JBC 257 (1982), 10324–10328.
179. Ganapathi, M.K., Lee, E.Y.C., ABB 233 (1984), 19–31.
180. Ramachandran, C., Pickett-Gies, C.A., Goris, J., Waelkens, E., Merlevede, W., Walsh, D.A., Adv. Protein Phosphatases 2 (1985), 355–374.
181. Ramachandran, C., Goris, J., Waelkens, E., Merlevede, W., Walsh, D.A., JBC, 261, 1986 (in press).
182. Cohen, P., Antoniw, J.F., FEBS Lett. 34 (1973), 43–47.
183. Stewart, A.A., Hemmings, B.A., Cohen, P., Goris, J., Merlevede, W., EJB 115 (1981), 197–205.
184. Ganapathi, M.K., Silberman, S.R., Paris, H., Lee, E.Y.C., JBC 256 (1981), 3213–3217.
185. Jurgensen, S., Shacter, E., Huang, C.Y., Chock, P.B., Yang, S.D., Vandenheede, J.R., Merlevede, W., JBC 259 (1984), 5864–5870.
186. Vandenheede, J.R., Yang, S.D., Merlevede, W., JBC 256 (1981), 5894–5900.
187. Ingebritsen, T.S., Cohen, P., EJB 132 (1983), 255–261.
188. Ingebritsen, T.S., Foulkes, Z.G., Cohen, P., EJB 132 (1983), 263–274.
189. Ingebritsen, T.S., Blair, J., Guy, P., Witters, L., Hardie, D.C., EJB 132 (1983), 275–281.
190. Pato, M.D., Adelstein, R.S., Crouch, D., Safer, B., Ingebritsen, T.S., Cohen, P., EJB 132 (1983), 283–287.
191. Stewart, A., Ingebritsen, T.S., Cohen, P., EJB 132 (1983), 289–295.
192. Pelech, S., Cohen, P., Fisher, M.Z., Pogson, C., El-Maghrabi, R., Pilkus, S.J., EJB 145 (1984), 39–45.
193. Ingebritsen, T.S., Stewart, A.A., Cohen, P., EJB 132 (1983), 297–307.
194. DiSalvo, J., Merlevede, W., Advances in Protein Phosphatases, 1, 1985, Leuven Press.
195. DiSalvo, J., Merlevede, W., Advances in Protein Phosphatases, 2, 1985, Leuven Press.
196. Tsuchiya, M., Tanigawa, Y., Ushiroyama, T., Matsuura, R., Shimoyama, M., EJB 147 (1985), 33–40.
197. Williamson, J.R., Cooper, R.H., Hoek, J.B., BBA 639 (1981), 243–295.
198. Assimacopoulos-Jeannet, F.D., Blackmore, P.F., Exton, J.H., JBC 252 (1977), 2662–2669.
199. Gross, S.R., Johnson, R.M., J. Pharmacol. Exp. Ther. 214 (1980), 37–44.
200. Posner, J.B., Stern, R.S., Krebs, E.G., JBC 240 (1985), 982–985.
201. Danforth, W.H., Helmreich, E., JBC 239 (1964), 3133–3138.
202. Danforth, W.H., Lyon, J.B., JBC 239 (1964), 4047–4050.
203. Friesen, A.J., Allen, G., Valadares, J.R., Science 155 (1967), 1108–1109.
204. Friesen, A.J., Oliver, N., Allen, G., Am. J. Physiol. 217 (1969), 445–450.
205. Dobson, J.G., Mayer, S.E., Circ. Res. 33 (1973), 412–420.
206. Dobson, J.G., Ross, J., Mayer, S.E., Circ. Res. 39 (1976), 388–395.
207. Hammermeister, K.E., Yunis, A., Krebs, E.G., JBC 240 (1965), 986–991.
208. Namm, D.H., Mayer, S.E., Mol. Pharmacol. 4 (1968), 61–69.
209. Namm, D.H., Mayer, S.E., Maltbie, M., Mol. Pharmacol. 4 (1968), 522–530.
210. Mayer, S.E., Namm, D.H., Rice, L., Circ. Res. 26 (1970), 225–233.
211. Barovsky, K., Gross, S.R., J. Pharmacol. Exp. Ther. 217 (1981), 326–332.
212. Yeaman, S.J., Cohen, P., EJB 51 (1975), 93–104.
213. McCullough, T.E., Walsh, D.A., JBC 254 (1979), 7345–7352.
214. Sul, H.S., Cooper, R.H., McCullough, T.E., Pickett-Gies, C.A., Angelos, K.L., Walsh, D.A., Cold Spring Harbor Conf. Cell Proliferation 8 (1981), 343–355.
215. Angelos, K.L., Ramachandran, C., Walsh, D.A., JBC, 1986 (in press.).
216. Carlsen, R.C., Larson, D.B., Walsh, D.A., Can. J. Pharmacol. Physiol. 63 (1985), 958–965.