Geraldine Mbamalu

Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands (1996)

Holland, Sacha J., Gale, Nicholas W., Mbamalu, Geraldine, Yancopoulos, George D., Henkemeyer, Mark, Pawson, Tony

Receptor tyrosine kinases of the EPH class have been implicated in the control of axon guidance and fasciculation [1-7], in regulating cell migration [8], and in defining compartments in the...

Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands (1996)

Holland, Sacha J., Gale, Nicholas W., Mbamalu, Geraldine, Yancopoulos, George D., Henkemeyer, Mark, Pawson, Tony

Receptor tyrosine kinases of the EPH class have been implicated in the control of axon guidance and fasciculation [1-7], in regulating cell migration [8], and in defining compartments in the...

A Drosophila SH2-SH3 Adaptor Protein Implicated in Coupling the Sevenless Tyrosine Kinase to an Activator of Ras Guanine Nucleotide Exchange, Sos (1993)

Olivier, Jean Paul, Raabe, Thomas, Henkerneyer, Mark, Dickson, Barry, Mbamalu, Geraldine, Margolis, Ben, ...

A Drosophila gene (drk) encodes a widely expressed protein with a single SH2 domain and two flanking SH3 domains, which is homologous to the Sem-5 protein of C. elegans and mammalian GRB2. Genetic...

A Drosophila SH2-SH3 Adaptor Protein Implicated in Coupling the Sevenless Tyrosine Kinase to an Activator of Ras Guanine Nucleotide Exchange, Sos (1993)

Olivier, Jean Paul, Raabe, Thomas, Henkerneyer, Mark, Dickson, Barry, Mbamalu, Geraldine, Margolis, Ben, ...

A Drosophila gene (drk) encodes a widely expressed protein with a single SH2 domain and two flanking SH3 domains, which is homologous to the Sem-5 protein of C. elegans and mammalian GRB2. Genetic...

WW Domains Provide a Platform for the Assembly of Multiprotein Networks†

Ingham, Robert J., Colwill, Karen, Howard, Caley, Dettwiler, Sabine, Lim, Caesar S. H., Yu, Joanna, ...

WW domains are protein modules that mediate protein-protein interactions through recognition of proline-rich peptide motifs and phosphorylated serine/threonine-proline sites. To pursue the functional...

WW Domains Provide a Platform for the Assembly of Multiprotein Networks†

Ingham, Robert J., Colwill, Karen, Howard, Caley, Dettwiler, Sabine, Lim, Caesar S. H., Yu, Joanna, ...

WW domains are protein modules that mediate protein-protein interactions through recognition of proline-rich peptide motifs and phosphorylated serine/threonine-proline sites. To pursue the functional...