Year |
Citation |
Score |
2001 |
Tam A, Schmidt WK, Michaelis S. The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor. The Journal of Biological Chemistry. 276: 46798-806. PMID 11581258 DOI: 10.1074/Jbc.M106150200 |
0.719 |
|
2001 |
Leung GK, Schmidt WK, Bergo MO, Gavino B, Wong DH, Tam A, Ashby MN, Michaelis S, Young SG. Biochemical studies of Zmpste24-deficient mice. The Journal of Biological Chemistry. 276: 29051-8. PMID 11399759 DOI: 10.1074/Jbc.M102908200 |
0.677 |
|
2000 |
Schmidt WK, Tam A, Michaelis S. Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis. The Journal of Biological Chemistry. 275: 6227-33. PMID 10692417 DOI: 10.1074/Jbc.275.9.6227 |
0.696 |
|
1998 |
Loayza D, Tam A, Schmidt WK, Michaelis S. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Molecular Biology of the Cell. 9: 2767-84. PMID 9763443 DOI: 10.1091/Mbc.9.10.2767 |
0.665 |
|
1998 |
Schmidt WK, Tam A, Fujimura-Kamada K, Michaelis S. Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proceedings of the National Academy of Sciences of the United States of America. 95: 11175-80. PMID 9736709 DOI: 10.1073/Pnas.95.19.11175 |
0.715 |
|
1998 |
Tam A, Nouvet FJ, Fujimura-Kamada K, Slunt H, Sisodia SS, Michaelis S. Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing. The Journal of Cell Biology. 142: 635-49. PMID 9700155 DOI: 10.1083/Jcb.142.3.635 |
0.683 |
|
1996 |
Geller D, Taglicht D, Edgar R, Tam A, Pines O, Michaelis S, Bibi E. Comparative topology studies in Saccharomyces cerevisiae and in Escherichia coli. The N-terminal half of the yeast ABC protein Ste6. The Journal of Biological Chemistry. 271: 13746-53. PMID 8662764 DOI: 10.1074/Jbc.271.23.13746 |
0.639 |
|
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