Matthew C. Good, Ph.D. - Publications

Affiliations: 
2010 Biochemistry and Molecular Biology University of California, San Francisco, San Francisco, CA 
Area:
Cellular Signaling Systems

14 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
2015 Good MC. Turn Up the Volume: Uncovering Nucleus Size Control Mechanisms. Developmental Cell. 33: 496-7. PMID 26058052 DOI: 10.1016/j.devcel.2015.05.015  0.68
2015 Crowder ME, Strzelecka M, Wilbur JD, Good MC, von Dassow G, Heald R. A Comparative Analysis of Spindle Morphometrics across Metazoans. Current Biology : Cb. 25: 1542-50. PMID 26004761 DOI: 10.1016/j.cub.2015.04.036  0.68
2013 Good MC, Vahey MD, Skandarajah A, Fletcher DA, Heald R. Cytoplasmic volume modulates spindle size during embryogenesis. Science (New York, N.Y.). 342: 856-60. PMID 24233724 DOI: 10.1126/science.1243147  0.68
2011 Good MC, Zalatan JG, Lim WA. Scaffold proteins: hubs for controlling the flow of cellular information. Science (New York, N.Y.). 332: 680-6. PMID 21551057 DOI: 10.1126/science.1198701  0.68
2010 Lombana TN, Echols N, Good MC, Thomsen ND, Ng HL, Greenstein AE, Falick AM, King DS, Alber T. Allosteric activation mechanism of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknB. Structure (London, England : 1993). 18: 1667-77. PMID 21134645 DOI: 10.1016/j.str.2010.09.019  0.68
2010 Mok J, Kim PM, Lam HY, Piccirillo S, Zhou X, Jeschke GR, Sheridan DL, Parker SA, Desai V, Jwa M, Cameroni E, Niu H, Good M, Remenyi A, Ma JL, et al. Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs. Science Signaling. 3: ra12. PMID 20159853 DOI: 10.1126/scisignal.2000482  0.68
2009 Good M, Tang G, Singleton J, Reményi A, Lim WA. The Ste5 scaffold directs mating signaling by catalytically unlocking the Fus3 MAP kinase for activation. Cell. 136: 1085-97. PMID 19303851 DOI: 10.1016/j.cell.2009.01.049  0.68
2008 King N, Westbrook MJ, Young SL, Kuo A, Abedin M, Chapman J, Fairclough S, Hellsten U, Isogai Y, Letunic I, Marr M, Pincus D, Putnam N, Rokas A, Wright KJ, ... ... Good M, et al. The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans. Nature. 451: 783-8. PMID 18273011 DOI: 10.1038/nature06617  0.68
2006 Reményi A, Good MC, Lim WA. Docking interactions in protein kinase and phosphatase networks. Current Opinion in Structural Biology. 16: 676-85. PMID 17079133 DOI: 10.1016/j.sbi.2006.10.008  0.68
2006 Bhattacharyya RP, Reményi A, Good MC, Bashor CJ, Falick AM, Lim WA. The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway. Science (New York, N.Y.). 311: 822-6. PMID 16424299 DOI: 10.1126/science.1120941  0.68
2005 Reményi A, Good MC, Bhattacharyya RP, Lim WA. The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network. Molecular Cell. 20: 951-62. PMID 16364919 DOI: 10.1016/j.molcel.2005.10.030  0.68
2004 Pullen KE, Ng HL, Sung PY, Good MC, Smith SM, Alber T. An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase. Structure (London, England : 1993). 12: 1947-54. PMID 15530359 DOI: 10.1016/j.str.2004.09.008  0.68
2004 Good MC, Greenstein AE, Young TA, Ng HL, Alber T. Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller. Journal of Molecular Biology. 339: 459-69. PMID 15136047 DOI: 10.1016/j.jmb.2004.03.063  0.68
2002 Asano K, Bohlmeyer TJ, Westcott JY, Zisman L, Kinugawa K, Good M, Minobe WA, Roden R, Wolfel EE, Lindenfeld J, David Port J, Perryman MB, Clevel J, Lowes BD, Bristow MR. Altered expression of endothelin receptors in failing human left ventricles Journal of Molecular and Cellular Cardiology. 34: 833-846. PMID 12099722 DOI: 10.1006/jmcc.2002.2022  0.68
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