I. Ota

发表

A protein interaction network of the malaria parasite Plasmodium falciparum

M. Vignali, S. Fields, R. Chettier, 2005, Nature.

A Proteolytic Pathway That Recognizes Ubiquitin as a Degradation Signal (*)

I. Ota, Erica S. Johnson, P. Ma, 1995, The Journal of Biological Chemistry.

A gene encoding a putative tyrosine phosphatase suppresses lethality of an N-end rule-dependent mutant.

I. Ota, A. Varshavsky, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Binding linkage in a telomere DNA-protein complex at the ends of Oxytricha nova chromosomes.

I. Ota, Mili Shum, M. Horvath, 2005, Journal of molecular biology.

A yeast protein similar to bacterial two-component regulators.

I. Ota, A. Varshavsky, I M Ota, 1993, Science.

Calcium affects the spontaneous degradation of aspartyl/asparaginyl residues in calmodulin.

I. Ota, S. Clarke, 1989, Biochemistry.

Enzymatic methylation of L-isoaspartyl residues derived from aspartyl residues in affinity-purified calmodulin. The role of conformational flexibility in spontaneous isoaspartyl formation.

I. Ota, S. Clarke, 1989, The Journal of biological chemistry.

Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes.

I. Ota, S. Clarke, J. M. Gilbert, 1988, Biochemical and biophysical research communications.

Multiple sites of methyl esterification of calmodulin in intact human erythrocytes.

I. Ota, S. Clarke, 1990, Archives of biochemistry and biophysics.

Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase.

I. Ota, S. Clarke, L. Ding, 1987, The Journal of biological chemistry.

The membrane binding domain of rod cGMP phosphodiesterase is posttranslationally modified by methyl esterification at a C-terminal cysteine.

I. Ota, S. Clarke, B. K. Fung, 1989, Proceedings of the National Academy of Sciences of the United States of America.

The γ subunit of brain G‐proteins is methyl esterified at a C‐terminal cysteine

I. Ota, S. Clarke, H. Yamane, 1990 .

Differential Regulation of the Cell Wall Integrity Mitogen-Activated Protein Kinase Pathway in Budding Yeast by the Protein Tyrosine Phosphatases Ptp2 and Ptp3

I. Ota, C. P. Mattison, S. Spencer, 1999, Molecular and Cellular Biology.

Two Protein-tyrosine Phosphatases Inactivate the Osmotic Stress Response Pathway in Yeast by Targeting the Mitogen-activated Protein Kinase, Hog1*

I. Ota, A. Seto, T Jacoby, 1997, The Journal of Biological Chemistry.

Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast.

I. Ota, C P Mattison, I M Ota, 2000, Genes & development.

Nbp2 targets the Ptc1‐type 2C Ser/Thr phosphatase to the HOG MAPK pathway

I. Ota, James H. Mapes, 2004, The EMBO journal.

Role of Ptc2 Type 2C Ser/Thr Phosphatase in Yeast High-Osmolarity Glycerol Pathway Inactivation

Irene Ota, I. Ota, S. Al-Zarban, 2002, Eukaryotic Cell.

Heat Stress Activates the Yeast High-Osmolarity Glycerol Mitogen-Activated Protein Kinase Pathway, and Protein Tyrosine Phosphatases Are Essential under Heat Stress

I. Ota, A. Burkholder, Christopher Arkind, 2002, Eukaryotic Cell.

Duration of Nuclear NF-kB Action Regulated by Reversible Acetylation

M. Tyers, I. Ota, A. Varshavsky, 2001 .

Initial large-scale exploration of protein-protein interactions in human brain

Jake Yue Chen, Sudhir Sahasrabudhe, Andrey Y. Sivachenko, 2003, Computational Systems Bioinformatics. CSB2003. Proceedings of the 2003 IEEE Bioinformatics Conference. CSB2003.

Ptc1, a Type 2C Ser/Thr Phosphatase, Inactivates the HOG Pathway by Dephosphorylating the Mitogen-Activated Protein Kinase Hog1

Irene Ota, I. Ota, Jennifer Hanneman, 2001, Molecular and Cellular Biology.

Targeting of PP2C in budding yeast.

I. Ota, James H. Mapes, 2007, Methods in molecular biology.

Cleavage initiating activities of sperm fractions injected into the egg of the medaka, Oryzias latipes.

I. Ota, T. Iwamatsu, 1974, The Journal of experimental zoology.