TY  - GEN
AU  - Zarich-Dimitrievich, Natasha
AU  - Oliva-Martinez, Jose Luis
AU  - Jorge, Rocío
AU  - Santos, E
AU  - Rojas-Cabañeros, Jose Maria
PY  - 2000
DO  - 10.1038/sj.onc.1203955
SN  - 0950-9232
UR  - https://hdl.handle.net/20.500.12105/26110
AB  - hSos1 isoform II, defined by the presence of a 15 amino acid stretch in its carboxy-terminal region, exhibits higher Grb2 affinity than hSos1 isoform I. In this study, we investigated the cause for this difference and observed that, in addition to the...
LA  - eng
PB  - Nature Publishing Group
KW  - hSos1
KW  - Isoforms
KW  - Grb2
KW  - SH3 domains
KW  - 3T3 Cells
KW  - Adaptor Proteins, Signal Transducing
KW  - Amino Acid Sequence
KW  - Animals
KW  - Binding Sites
KW  - COS Cells
KW  - Chlorocebus aethiops
KW  - GRB2 Adaptor Protein
KW  - Glutathione Transferase
KW  - Humans
KW  - Mice
KW  - Molecular Sequence Data
KW  - Mutagenesis, Site-Directed
KW  - Peptide Fragments
KW  - Polymerase Chain Reaction
KW  - Protein Isoforms
KW  - Protein Structure, Tertiary
KW  - Proteins
KW  - Recombinant Fusion Proteins
KW  - SOS1 Protein
KW  - Saccharomyces cerevisiae
KW  - Substrate Specificity
KW  - src Homology Domains
TI  - The isoform-specific stretch of hSos1 defines a new Grb2-binding domain.
TY  - research article
ER  -