Terrence D. Mulhern

The solution structure and intramolecular associations of the Tec kinase SRC homology 3 domain.

1H, 13C and 15N chemical shift assignments of the SH2 domain of the Csk homologous kinase.

A novel non-catalytic mechanism employed by the C-terminal Src-homologous kinase to inhibit Src-family kinase activity.

Tom22', an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes.

A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway.

Endogenous and synthetic inhibitors of the Src-family protein tyrosine kinases.

C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)--endogenous negative regulators of Src-family protein kinases.

Engineering of the Escherichia coli Im7 immunity protein as a loop display scaffold.

The C-terminal TPR domain of Tom70 defines a family of mitochondrial protein import receptors found only in animals and fungi.

C-terminal Src kinase-homologous kinase (CHK), a unique inhibitor inactivating multiple active conformations of Src family tyrosine kinases.

PTEN catalysis of phospholipid dephosphorylation reaction follows a two-step mechanism in which the conserved aspartate-92 does not function as the general acid--mechanistic analysis of a familial Cowden disease-associated PTEN mutation.

Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1).

Structure, topology and function of the translocase of the outer membrane of mitochondria.

Evidence of a reduced and modified mitochondrial protein import apparatus in microsporidian mitosomes.

Domain organization of the monomeric form of the Tom70 mitochondrial import receptor.

Recognition of mitochondrial targeting sequences by the import receptors Tom20 and Tom22.

Bacterial expression and purification of active hematopoietic cell kinase.

Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.

Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity.