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Solution structure of the SH3 domain of Src and identification of its ligand-binding site.
- H. Yu, M. Rosen, T. B. Shin, C. Seidel-Dugan, J. Brugge, S. Schreiber
- Biology, ChemistryScience
- 4 December 1992
The solution structure of the SH3 domain of the tyrosine kinase Src was determined by multidimensional nuclear magnetic resonance methods and revealed a hydrophobic binding site on the surface of the protein that is lined with the side chains of conserved aromatic amino acids.
Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains.
A role for the Src SH3 domain is strongly suggested in the recruitment of substrates to this protein tyrosine kinase, either through direct interaction with the SH3domain or indirectly through interactions with proteins that bind to theSH3 domain.
Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells.
Human Semaphorin K1 Is Glycosylphosphatidylinositol-linked and Defines a New Subfamily of Viral-related Semaphorins*
Sema K1 is the first semaphorin known to be associated with cell surfaces via a glycosylphosphatidylinositol linkage and is highly homologous to a viral semaphOrin and can interact with specific immune cells, suggesting that like its viral counterpart, semaK1 could play an important role in regulating immune function.
SCH529074, a Small Molecule Activator of Mutant p53, Which Binds p53 DNA Binding Domain (DBD), Restores Growth-suppressive Function to Mutant p53 and Interrupts HDM2-mediated Ubiquitination of Wild…
- M. Demma, E. Maxwell, B. Dasmahapatra
- Biology, ChemistryThe Journal of Biological Chemistry
- 2 February 2010
This small molecule reactivates mutant p53 by acting as a chaperone, in a manner similar to that previously reported for the peptide CDB3, and restores wild type function to many oncogenic mutant forms of p53.
Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src.
- C. Seidel-Dugan, B. Meyer, S. M. Thomas, J. Brugge
- BiologyMolecular and cellular biology
- 1 April 1992
It is indicated that deletion of the A, B, or C homology box causes an activation of the catalytic and transforming potential of c-Src and that while these mutations caused subtle differences in substrate phosphorylation, the homology boxes are not required for many of the phenotypic changes associated with transformation by Src.
C3b receptor activity on transfected cells expressing glycoprotein C of herpes simplex virus types 1 and 2
The results suggest that other proteins expressed during HSV-2 infection prevent receptor activity, and three in-frame deletion mutants of gC-2 are constructed to identify domains on the protein important for C3b receptor activity.
Herpes simplex virus glycoprotein C is a receptor for complement component iC3b.
Using linker insertion mutants, three domains on gC2 that are important for binding iC3b were mapped; these regions were similar to previously defined regions involved in binding C3b, suggesting that some of the functions served by gC may be similar to those of CR3, the mammalian receptor for iC2.
Evaluating TBK1 as a Therapeutic Target in Cancers with Activated IRF3
regulation of pathways important for cell proliferation in some NSCLC, pancreatic, and colorectal cell lines is not solely dependent on TBK1 activity, and phosphorylation of its downstream target IRF3 is a biomarker of TBK 1 activity.
Identification of C3b-binding regions on herpes simplex virus type 2 glycoprotein C
- C. Seidel-Dugan, M. Ponce de Leon, H. Friedman, R. Eisenberg, G. Cohen
- BiologyJournal of virology
- 1 May 1990
In-frame linker-insertion mutagenesis of the cloned gene for gC-2 was used to identify regions of the protein involved in C3b binding, which suggested that each of the mutant proteins was folded into a native structure and that a loss of C3B binding by any of the mutants could be attributed to the disruption of a specific functional domain.