S. I. Yang

Publication List Details

Period

2000 - 2000

Number

8

Co-Authors

AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation.

Datta, K, Franke, T F, Chan, T O, Makris, A, Yang, S I, Kaplan, D R, ...

The cytoplasmic serine-threonine protein kinase coded for by the c-akt proto-oncogene features a protein kinase C-like catalytic domain and a unique NH2-terminal domain (AH domain). The AH domain is...

Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase.

Green, D D, Yang, S I, Mumby, M C

We have isolated a cDNA clone corresponding to the Mr 38,000 catalytic subunit of bovine type 2A protein phosphatase. The cDNA was isolated from a bovine adrenal gland cDNA library through the use of...

Control of protein phosphatase 2A by simian virus 40 small-t antigen.

Yang, S I, Lickteig, R L, Estes, R, Rundell, K, Walter, G, Mumby, M C

Soluble, monomeric simian virus 40 (SV40) small-t antigen (small-t) was purified from bacteria and assayed for its ability to form complexes with protein phosphatase 2A (PP2A) and to modify its...

AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation.

Datta, K, Franke, T F, Chan, T O, Makris, A, Yang, S I, Kaplan, D R, ...

The cytoplasmic serine-threonine protein kinase coded for by the c-akt proto-oncogene features a protein kinase C-like catalytic domain and a unique NH2-terminal domain (AH domain). The AH domain is...

Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase.

Green, D D, Yang, S I, Mumby, M C

We have isolated a cDNA clone corresponding to the Mr 38,000 catalytic subunit of bovine type 2A protein phosphatase. The cDNA was isolated from a bovine adrenal gland cDNA library through the use of...

Control of protein phosphatase 2A by simian virus 40 small-t antigen.

Yang, S I, Lickteig, R L, Estes, R, Rundell, K, Walter, G, Mumby, M C

Soluble, monomeric simian virus 40 (SV40) small-t antigen (small-t) was purified from bacteria and assayed for its ability to form complexes with protein phosphatase 2A (PP2A) and to modify its...