Prolyl Isomerases and Nuclear Function

A human peptidyl–prolyl isomerase essential for regulation of mitosis

Lu, K. P., Hanes, S. D., & Hunter, T. (1996) · Nature · doi:10.1038/380544a0 · Cited by 908

Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism

Yaffe, M. B., Schutkowski, M., Shen, M., Zhou, X. Z., Stukenberg, P. T., Rahfeld, J., Xu, J., Kuang, J., Kirschner, M. W., Fischer, G. S., et al. (1997) · Science · doi:10.1126/science.278.5345.1957 · Cited by 770

Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid

Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706 · cited 1×

Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent

Ranganathan, R., Lu, K. P., Hunter, T. R., & Noel, J. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80273-1 · Cited by 703

Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices

Ogata, K., Morikawa, S., Nakamura, H., Sekikawa, A., Inoue, T., Kanai, H., Sarai, A., Ishii, S., & Nishimura, Y. (1994) · Cell · doi:10.1016/0092-8674(94)90549-5 · Cited by 489

All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae

Dolinski, K. J., Muir, S., Cardenas, M. E., & Heitman, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13093 · Cited by 282

Confirmation of the existence of a third family among peptidyl‐prolyl cis/trans isomerases Amino acid sequence and recombinant production of parvulin

Rahfeld, J., Rücknagel, K. P., Alvarez, B. H., et al. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00932-5 · Cited by 198

The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb.Preprint

Dash, A. B., Orrico, F. C., & Ness, S. A. (1996) · Genes & Development · doi:10.1101/gad.10.15.1858 · Cited by 168

Point Mutations in v-Myb Disrupt a Cyclophilin-Catalyzed Negative Regulatory Mechanism

Leverson, J. D., & Ness, S. A. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80021-0 · Cited by 144

The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin.

Jin, Y. J., & Burakoff, S. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7769 · Cited by 122

The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae.

Maleszka, R., Hanes, S. D., Hackett, R. L., de Couet, H. G., & Miklos, G. L. G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.447 · Cited by 107

Cyclophilin A and FKBP12 Interact with YY1 and Alter Its Transcriptional Activity

Yang, W., Inouye, C. J., & Seto, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.15187 · Cited by 100

Protein folding: Prolyl isomerases join the fold

Schmid, F. X. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00197-7 · Cited by 99

The Homeobox Gene GBX2, a Target of the myb Oncogene, Mediates Autocrine Growth and Monocyte Differentiation

Kowenz‐Leutz, E., Herr, P., Niß, K., & Leutz, A. (1997) · Cell · doi:10.1016/s0092-8674(00)80401-8 · Cited by 96

Differential Regulation of c-Myb-induced Transcription Activation by a Phosphorylation Site in the Negative Regulatory Domain

Miglarese, M. R., Richardson, A. F., Aziz, N. A., & Bender, T. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22697 · Cited by 57

Catalysis of protein folding by parvulin 1 1Edited by P. E. Wright

Scholz, C., Rahfeld, J., Fischer, G. S., & Schmid, F. X. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1301 · Cited by 56

Functions of FKBP12 and Mitochondrial Cyclophilin Active Site Residues In Vitro and In Vivo inSaccharomyces cerevisiae

Dolinski, K. J., Scholz, C., Muir, R. S., Rospert, S., Schmid, F. X., Cardenas, M. E., & Heitman, J. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.11.2267 · Cited by 35

Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate

Scholz, C., Schindler, T. H., Dolinski, K. J., Heitman, J., & Schmid, F. X. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00979-4 · Cited by 32

Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation

Musich, P. R., Li, Z., & Zou, Y. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-56017-5_4 · Cited by 23

Prolyl Isomerases

Schmid, F. X. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)59008-7 · Cited by 76

The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer

Stifani, S. (2018) · Biomolecules · doi:10.3390/biom8040112 · Cited by 12

Small Molecule Inhibitors of Peptidylprolyl cis/trans Isomerase

Mori, T., & Uchida, T. (2010) · Current Enzyme Inhibition · doi:10.2174/157340810790712005 · Cited by 6

Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis.

Rippmann, J. F., Hobbie, S., Daiber, C., Guilliard, B., Bauer, M., Birk, J., Nar, H., Garin‐Chesa, P., Rettig, W. J., & Schnapp, A. (2000) · PubMed · Cited by 126

Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism

Yaffe, M. B., Schutkowski, M., Shen, M., Zhou, X. Z., Stukenberg, P. T., Rahfeld, J., Xu, J., Kuang, J., Kirschner, M. W., Fischer, G. S., et al. (1997) · Science · doi:10.1126/science.278.5345.1957 · Cited by 770