Melanie Cobb - Publications

University of California, Davis, Davis, CA 

63 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
2019 Shen C, Li B, Astudillo L, Deutscher MP, Cobb MH, Capobianco AJ, Lee E, Robbins DJ. The CK1α Activator Pyrvinium Enhances the Catalytic Efficiency (/) of CK1α. Biochemistry. PMID 31820934 DOI: 10.1021/Acs.Biochem.9B00891  0.303
2016 Gallolu Kankanamalage S, Lee AY, Wichaidit C, Lorente-Rodriguez A, Shah AM, Stippec S, Whitehurst AW, Cobb MH. Multistep regulation of autophagy by WNK1. Proceedings of the National Academy of Sciences of the United States of America. PMID 27911840 DOI: 10.1073/pnas.1617649113  0.318
2013 Sengupta S, Lorente-Rodríguez A, Earnest S, Stippec S, Guo X, Trudgian DC, Mirzaei H, Cobb MH. Regulation of OSR1 and the sodium, potassium, two chloride cotransporter by convergent signals. Proceedings of the National Academy of Sciences of the United States of America. 110: 18826-31. PMID 24191005 DOI: 10.1073/Pnas.1318676110  0.326
2009 Chen W, Chen Y, Xu BE, Juang YC, Stippec S, Zhao Y, Cobb MH. Regulation of a third conserved phosphorylation site in SGK1. The Journal of Biological Chemistry. 284: 3453-60. PMID 19068477 DOI: 10.1074/Jbc.M807502200  0.329
2007 Raman M, Chen W, Cobb MH. Differential regulation and properties of MAPKs. Oncogene. 26: 3100-12. PMID 17496909 DOI: 10.1038/sj.onc.1210392  0.325
2006 Heise CJ, Cobb MH. Expression and characterization of MAP kinases in bacteria. Methods (San Diego, Calif.). 40: 209-12. PMID 16908184 DOI: 10.1016/j.ymeth.2006.06.012  0.317
2006 Anselmo AN, Earnest S, Chen W, Juang YC, Kim SC, Zhao Y, Cobb MH. WNK1 and OSR1 regulate the Na+, K+, 2Cl- cotransporter in HeLa cells. Proceedings of the National Academy of Sciences of the United States of America. 103: 10883-8. PMID 16832045 DOI: 10.1073/Pnas.0604607103  0.314
2006 Ranganathan A, Pearson GW, Chrestensen CA, Sturgill TW, Cobb MH. The MAP kinase ERK5 binds to and phosphorylates p90 RSK. Archives of Biochemistry and Biophysics. 449: 8-16. PMID 16626623 DOI: 10.1016/J.Abb.2006.02.023  0.309
2006 Pearson GW, Earnest S, Cobb MH. Cyclic AMP selectively uncouples mitogen-activated protein kinase cascades from activating signals. Molecular and Cellular Biology. 26: 3039-47. PMID 16581779 DOI: 10.1128/MCB.26.8.3039-3047.2006  0.317
2006 Chen Z, Cobb MH. Activation of MEKK1 by Rho GTPases. Methods in Enzymology. 406: 468-78. PMID 16472679 DOI: 10.1016/S0076-6879(06)06035-6  0.329
2005 Xu BE, Stippec S, Lazrak A, Huang CL, Cobb MH. WNK1 activates SGK1 by a phosphatidylinositol 3-kinase-dependent and non-catalytic mechanism. The Journal of Biological Chemistry. 280: 34218-23. PMID 16081417 DOI: 10.1074/jbc.M505735200  0.311
2004 Zhou T, Raman M, Gao Y, Earnest S, Chen Z, Machius M, Cobb MH, Goldsmith EJ. Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K. Structure (London, England : 1993). 12: 1891-900. PMID 15458637 DOI: 10.1016/J.Str.2004.07.021  0.312
2004 Anselmo AN, Cobb MH. Protein kinase function and glutathionylation. The Biochemical Journal. 381: e1-2. PMID 15270699 DOI: 10.1042/BJ20040873  0.3
2004 Whitehurst AW, Robinson FL, Moore MS, Cobb MH. The death effector domain protein PEA-15 prevents nuclear entry of ERK2 by inhibiting required interactions. The Journal of Biological Chemistry. 279: 12840-7. PMID 14707138 DOI: 10.1074/Jbc.M310031200  0.31
2004 Chen W, Yazicioglu M, Cobb MH. Characterization of OSR1, a member of the mammalian Ste20p/germinal center kinase subfamily. The Journal of Biological Chemistry. 279: 11129-36. PMID 14707132 DOI: 10.1074/jbc.M313562200  0.344
2004 Xu BE, Stippec S, Lenertz L, Lee BH, Zhang W, Lee YK, Cobb MH. WNK1 activates ERK5 by an MEKK2/3-dependent mechanism. The Journal of Biological Chemistry. 279: 7826-31. PMID 14681216 DOI: 10.1074/Jbc.M313465200  0.314
2004 Gallagher ED, Gutowski S, Sternweis PC, Cobb MH. RhoA binds to the amino terminus of MEKK1 and regulates its kinase activity. The Journal of Biological Chemistry. 279: 1872-7. PMID 14581471 DOI: 10.1074/Jbc.M309525200  0.311
2003 Chen Z, Raman M, Chen L, Lee SF, Gilman AG, Cobb MH. TAO (thousand-and-one amino acid) protein kinases mediate signaling from carbachol to p38 mitogen-activated protein kinase and ternary complex factors. The Journal of Biological Chemistry. 278: 22278-83. PMID 12665513 DOI: 10.1074/Jbc.M301173200  0.325
2002 Chen W, White MA, Cobb MH. Stimulus-specific requirements for MAP3 kinases in activating the JNK pathway. The Journal of Biological Chemistry. 277: 49105-10. PMID 12351623 DOI: 10.1074/jbc.M204934200  0.319
2002 Pearson GW, Cobb MH. Cell condition-dependent regulation of ERK5 by cAMP. The Journal of Biological Chemistry. 277: 48094-8. PMID 12297510 DOI: 10.1074/jbc.M208535200  0.313
2002 Gallagher ED, Xu S, Moomaw C, Slaughter CA, Cobb MH. Binding of JNK/SAPK to MEKK1 is regulated by phosphorylation. The Journal of Biological Chemistry. 277: 45785-92. PMID 12228228 DOI: 10.1074/jbc.M207702200  0.309
2002 Christerson LB, Gallagher E, Vanderbilt CA, Whitehurst AW, Wells C, Kazempour R, Sternweis PC, Cobb MH. p115 Rho GTPase activating protein interacts with MEKK1. Journal of Cellular Physiology. 192: 200-8. PMID 12115726 DOI: 10.1002/Jcp.10125  0.302
2002 Robinson FL, Whitehurst AW, Raman M, Cobb MH. Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1. The Journal of Biological Chemistry. 277: 14844-52. PMID 11823456 DOI: 10.1074/Jbc.M107776200  0.328
2001 Berman KS, Hutchison M, Avery L, Cobb MH. kin-18, a C. elegans protein kinase involved in feeding. Gene. 279: 137-47. PMID 11733138 DOI: 10.1016/S0378-1119(01)00752-1  0.313
2001 Chen Z, Cobb MH. Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2. The Journal of Biological Chemistry. 276: 16070-5. PMID 11279118 DOI: 10.1074/jbc.M100681200  0.318
2000 Pearson G, Bumeister R, Henry DO, Cobb MH, White MA. Uncoupling Raf1 from MEK1/2 impairs only a subset of cellular responses to Raf activation. The Journal of Biological Chemistry. 275: 37303-6. PMID 11018021 DOI: 10.1074/Jbc.C000570200  0.322
2000 Karandikar M, Xu S, Cobb MH. MEKK1 binds raf-1 and the ERK2 cascade components. The Journal of Biological Chemistry. 275: 40120-7. PMID 10969079 DOI: 10.1074/jbc.M005926200  0.326
2000 Xu B, English JM, Wilsbacher JL, Stippec S, Goldsmith EJ, Cobb MH. WNK1, a novel mammalian serine/threonine protein kinase lacking the catalytic lysine in subdomain II. The Journal of Biological Chemistry. 275: 16795-801. PMID 10828064 DOI: 10.1074/Jbc.275.22.16795  0.309
2000 Nichols A, Camps M, Gillieron C, Chabert C, Brunet A, Wilsbacher J, Cobb M, Pouyssegur J, Shaw JP, Arkinstall S. Substrate recognition domains within extracellular signal-regulated kinase mediate binding and catalytic activation of mitogen-activated protein kinase phosphatase-3. The Journal of Biological Chemistry. 275: 24613-21. PMID 10811804 DOI: 10.1074/Jbc.M001515200  0.403
2000 Chaudhary A, King WG, Mattaliano MD, Frost JA, Diaz B, Morrison DK, Cobb MH, Marshall MS, Brugge JS. Phosphatidylinositol 3-kinase regulates Raf1 through Pak phosphorylation of serine 338. Current Biology : Cb. 10: 551-4. PMID 10801448 DOI: 10.1016/S0960-9822(00)00475-9  0.309
2000 Liou J, Kiefer F, Dang A, Hashimoto A, Cobb MH, Kurosaki T, Weiss A. HPK1 is activated by lymphocyte antigen receptors and negatively regulates AP-1. Immunity. 12: 399-408. PMID 10795738 DOI: 10.1016/S1074-7613(00)80192-2  0.308
1999 Karandikar M, Cobb MH. Scaffolding and protein interactions in MAP kinase modules. Cell Calcium. 26: 219-26. PMID 10643560 DOI: 10.1054/ceca.1999.0074  0.306
1999 Wang J, Frost JA, Cobb MH, Ross EM. Reciprocal signaling between heterotrimeric G proteins and the p21-stimulated protein kinase. The Journal of Biological Chemistry. 274: 31641-7. PMID 10531372 DOI: 10.1074/Jbc.274.44.31641  0.303
1999 Chen Z, Hutchison M, Cobb MH. Isolation of the protein kinase TAO2 and identification of its mitogen-activated protein kinase/extracellular signal-regulated kinase kinase binding domain. The Journal of Biological Chemistry. 274: 28803-7. PMID 10497253 DOI: 10.1074/jbc.274.40.28803  0.314
1998 Robinson MJ, Stippec SA, Goldsmith E, White MA, Cobb MH. A constitutively active and nuclear form of the MAP kinase ERK2 is sufficient for neurite outgrowth and cell transformation. Current Biology : Cb. 8: 1141-50. PMID 9799732 DOI: 10.1016/S0960-9822(07)00485-X  0.33
1998 Hutchison M, Berman KS, Cobb MH. Isolation of TAO1, a protein kinase that activates MEKs in stress-activated protein kinase cascades. The Journal of Biological Chemistry. 273: 28625-32. PMID 9786855 DOI: 10.1074/jbc.273.44.28625  0.32
1998 Dang A, Frost JA, Cobb MH. The MEK1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases ERK1 and ERK2 in mammalian cells. The Journal of Biological Chemistry. 273: 19909-13. PMID 9677429 DOI: 10.1074/jbc.273.31.19909  0.316
1997 Xu S, Cobb MH. MEKK1 binds directly to the c-Jun N-terminal kinases/stress-activated protein kinases. The Journal of Biological Chemistry. 272: 32056-60. PMID 9405400 DOI: 10.1074/jbc.272.51.32056  0.332
1997 Frost JA, Steen H, Shapiro P, Lewis T, Ahn N, Shaw PE, Cobb MH. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. The Embo Journal. 16: 6426-38. PMID 9351825 DOI: 10.1093/Emboj/16.21.6426  0.31
1997 Xu S, Khoo S, Dang A, Witt S, Do V, Zhen E, Schaefer EM, Cobb MH. Differential regulation of mitogen-activated protein/ERK kinase (MEK)1 and MEK2 and activation by a Ras-independent mechanism. Molecular Endocrinology (Baltimore, Md.). 11: 1618-25. PMID 9328344 DOI: 10.1210/mend.11.11.0010  0.331
1997 Khokhlatchev A, Xu S, English J, Wu P, Schaefer E, Cobb MH. Reconstitution of mitogen-activated protein kinase phosphorylation cascades in bacteria. Efficient synthesis of active protein kinases. The Journal of Biological Chemistry. 272: 11057-62. PMID 9110999 DOI: 10.1074/jbc.272.17.11057  0.318
1996 Cobb MH, Xu S, Cheng M, Ebert D, Robbins D, Goldsmith E, Robinson M. Structural analysis of the MAP kinase ERK2 and studies of MAP kinase regulatory pathways. Advances in Pharmacology (San Diego, Calif.). 36: 49-65. PMID 8783554 DOI: 10.1016/S1054-3589(08)60576-1  0.326
1996 Frost JA, Xu S, Hutchison MR, Marcus S, Cobb MH. Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members. Molecular and Cellular Biology. 16: 3707-13. PMID 8668187 DOI: 10.1128/Mcb.16.7.3707  0.333
1996 Cheng M, Zhen E, Robinson MJ, Ebert D, Goldsmith E, Cobb MH. Characterization of a protein kinase that phosphorylates serine 189 of the mitogen-activated protein kinase homolog ERK3. The Journal of Biological Chemistry. 271: 12057-62. PMID 8662649 DOI: 10.1074/Jbc.271.20.12057  0.315
1996 Cheng M, Boulton TG, Cobb MH. ERK3 is a constitutively nuclear protein kinase. The Journal of Biological Chemistry. 271: 8951-8. PMID 8621539 DOI: 10.1074/jbc.271.15.8951  0.319
1995 Xu S, Robbins D, Frost J, Dang A, Lange-Carter C, Cobb MH. MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase. Proceedings of the National Academy of Sciences of the United States of America. 92: 6808-12. PMID 7624324 DOI: 10.1073/pnas.92.15.6808  0.334
1995 Marcus S, Polverino A, Chang E, Robbins D, Cobb MH, Wigler MH. Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe. Proceedings of the National Academy of Sciences of the United States of America. 92: 6180-4. PMID 7597098 DOI: 10.1073/Pnas.92.13.6180  0.304
1995 Polverino A, Frost J, Yang P, Hutchison M, Neiman AM, Cobb MH, Marcus S. Activation of mitogen-activated protein kinase cascades by p21-activated protein kinases in cell-free extracts of Xenopus oocytes. The Journal of Biological Chemistry. 270: 26067-70. PMID 7592806 DOI: 10.1074/Jbc.270.44.26067  0.313
1995 English JM, Vanderbilt CA, Xu S, Marcus S, Cobb MH. Isolation of MEK5 and differential expression of alternatively spliced forms. The Journal of Biological Chemistry. 270: 28897-902. PMID 7499418 DOI: 10.1074/Jbc.270.48.28897  0.303
1994 Zhang F, Strand A, Robbins D, Cobb MH, Goldsmith EJ. Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature. 367: 704-11. PMID 8107865 DOI: 10.1038/367704A0  0.301
1993 Robbins DJ, Zhen E, Owaki H, Vanderbilt CA, Ebert D, Geppert TD, Cobb MH. Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro. The Journal of Biological Chemistry. 268: 5097-106. PMID 8444886  0.322
1993 Cheng JT, Cobb MH, Baer R. Phosphorylation of the TAL1 Oncoprotein by the Extracellular-Signal-Regulated Protein Kinase ERK1 Molecular and Cellular Biology. 13: 801-808. PMID 8423803 DOI: 10.1128/mcb.13.2.801-808.1993  0.326
1993 Sontag E, Fedorov S, Kamibayashi C, Robbins D, Cobb M, Mumby M. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation. Cell. 75: 887-97. PMID 8252625 DOI: 10.1016/0092-8674(93)90533-V  0.377
1993 Cheng JT, Cobb MH, Baer R. Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1. Molecular and Cellular Biology. 13: 801-808. DOI: 10.1128/MCB.13.2.801  0.326
1992 Funasaka Y, Boulton T, Cobb M, Yarden Y, Fan B, Lyman SD, Williams DE, Anderson DM, Zakut R, Mishima Y. c-Kit-kinase induces a cascade of protein tyrosine phosphorylation in normal human melanocytes in response to mast cell growth factor and stimulates mitogen-activated protein kinase but is down-regulated in melanomas. Molecular Biology of the Cell. 3: 197-209. PMID 1372524 DOI: 10.1091/Mbc.3.2.197  0.408
1992 Haycock JW, Ahn NG, Cobb MH, Krebs EG. ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. Proceedings of the National Academy of Sciences of the United States of America. 89: 2365-9. PMID 1347949 DOI: 10.1073/Pnas.89.6.2365  0.307
1992 Shibuya EK, Boulton TG, Cobb MH, Ruderman JV. Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest. The Embo Journal. 11: 3963-75. PMID 1327752 DOI: 10.1002/J.1460-2075.1992.Tb05490.X  0.301
1992 Ahn NG, Robbins DJ, Haycock JW, Seger R, Cobb MH, Krebs EG. Identification of an activator of the microtubule-associated protein 2 kinases ERK1 and ERK2 in PC12 cells stimulated with nerve growth factor or bradykinin. Journal of Neurochemistry. 59: 147-56. PMID 1319464 DOI: 10.1111/J.1471-4159.1992.Tb08885.X  0.322
1991 Boulton TG, Nye SH, Robbins DJ, Ip NY, Radziejewska E, Morgenbesser SD, DePinho RA, Panayotatos N, Cobb MH, Yancopoulos GD. ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. Cell. 65: 663-75. PMID 2032290 DOI: 10.1016/0092-8674(91)90098-J  0.318
1991 Seger R, Ahn NG, Boulton TG, Yancopoulos GD, Panayotatos N, Radziejewska E, Ericsson L, Bratlien RL, Cobb MH, Krebs EG. Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation. Proceedings of the National Academy of Sciences of the United States of America. 88: 6142-6. PMID 1712480 DOI: 10.1073/Pnas.88.14.6142  0.318
1991 Cobb MH, Robbins DJ, Boulton TG. ERKs, extracellular signal-regulated MAP-2 kinases. Current Opinion in Cell Biology. 3: 1025-32. PMID 1667578 DOI: 10.1016/0955-0674(91)90124-H  0.316
1991 Boulton TG, Cobb MH. Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies Cell Regulation. 2: 357-371. PMID 1654126 DOI: 10.1091/MBC.2.5.357  0.32
1990 Boulton TG, Yancopoulos GD, Gregory JS, Slaughter C, Moomaw C, Hsu J, Cobb MH. An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control Science. 249: 64-67. PMID 2164259 DOI: 10.1126/SCIENCE.2164259  0.33
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