This collection showcases the journal articles and other publications authored by researchers in the Roger Davis Lab in the Program in Molecular Medicine at the University of Massachusetts Medical School. The cJun NH2-terminal kinase (JNK) signal transduction pathway is implicated in several stress-related disease processes including cancer, diabetes, inflammation, and stroke. Our hope is that drugs targeting the JNK pathway may be useful for the treatment of these diseases. The goal of this laboratory is to understand the molecular processes that are engaged by JNK in both health and disease.
Publications from 1992
Increased oncogenic potential of ErbB is associated with the loss of a COOH-terminal domain serine phosphorylation site, Steven J. Theroux, Cherie A. Taglienti, Nandini Nair, Janice L. Countaway, Harriet L. Robinson, and Roger J. Davis
Publications from 1991
Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase, Elvira Alvarez, Ingrid C. Northwood, Fernando A. Gonzalez, Debra A. Latour, Alpna Seth, Cory Abate, Tom Curran, and Roger J. Davis
Constitutive phosphorylation of the epidermal growth factor receptor blocks mitogenic signal transduction, Sharon Bowen, Krista Stanley, Erica Marie Selva, and Roger J. Davis
Mutational analysis of the cytoplasmic tail of the human transferrin receptor. Identification of a sub-domain that is required for rapid endocytosis, Nuria Girones, Elvira Alvarez, Alpna Seth, I-Mei Lin, Debra A. Latour, and Roger J. Davis
Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases, Fernando A. Gonzalez, David L. Raden, and Roger J. Davis
Publications from 1990
A point mutation in the cytoplasmic domain of the transferrin receptor inhibits endocytosis, Elvira Alvarez, Nuria Girones, and Roger J. Davis
Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid, Elvira Alvarez, Nuria Girones, and Roger J. Davis
Signal transduction by the epidermal growth factor receptor after functional desensitization of the receptor tyrosine protein kinase activity, Ingrid C. Northwood and Roger J. Davis
Publications from 1989
Reconstitution of epidermal growth factor receptor transmodulation by platelet-derived growth factor in Chinese hamster ovary cells, Janice L. Countaway, Nuria Girones, and Roger J. Davis
Mechanism of phosphorylation of the epidermal growth factor receptor at threonine 669, Janice L. Countaway, Ingrid C. Northwood, and Roger J. Davis
Comparison of the kinetics of cycling of the transferrin receptor in the presence or absence of bound diferric transferrin, Nuria Girones and Roger J. Davis
Protein kinase C inhibition of the epidermal growth factor receptor tyrosine protein kinase activity is independent of the oligomeric state of the receptor, Ingrid C. Northwood and Roger J. Davis
Publications from 1988
Two alternative mechanisms control the interconversion of functional states of the epidermal growth factor receptor, Roger J. Davis, Nuria Girones, and Mark Faucher
Regulation of the epidermal growth factor receptor phosphorylation state by sphingosine in A431 human epidermoid carcinoma cells, Mark Faucher, Nuria Girones, Yusuf A. Hannun, Robert M. Bell, and Roger J. Davis
Publications from 1987
Insulin-like growth factor I and epidermal growth factor regulate the expression of transferrin receptors at the cell surface by distinct mechanisms, Roger J. Davis, Mark Faucher, Lori Kuck Racaniello, Anthony Carruthers, and Michael P. Czech
Regulation of transferrin receptor cycling by protein kinase C is independent of receptor phosphorylation at serine 24 in Swiss 3T3 fibroblasts, Roger J. Davis and Herman Meisner
Publications from 1986
Identification of serine 24 as the unique site on the transferrin receptor phosphorylated by protein kinase C, Roger J. Davis, Gary L. Johnson, Daniel J. Kelleher, Jaquelin K. Anderson, John E. Mole, and Michael P. Czech