The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Hop: more than an Hsp70/Hsp90 adaptor protein
Abstract
Molecular chaperones facilitate the correct folding of other proteins under physiological and stress conditions. Recently it has become evident that various co‐chaperone proteins regulate the cellular functions of these chaperones, particularly Hsp70 and Hsp90. Hop is one of the most extensively studied co‐chaperones that is able to directly associate with both Hsp70 and Hsp90. The current dogma proposes that Hop functions primarily as an adaptor that directs Hsp90 to Hsp70‐client protein complexes in the cytoplasm. However, recent evidence suggests that Hop can also modulate the chaperone activities of these Hsps, and that it is not dedicated to Hsp70 and Hsp90. While the co‐chaperone function of Hop within the cytoplasm has been extensively studied, its association with nuclear complexes and prion proteins remains to be elucidated. This article will review the structural features of Hop, and the evidence that its biological function is considerably broader than previously envisaged. BioEssays 26:1058–1068, 2004. © 2004 Wiley Periodicals, Inc.
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Citations
Cites
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370
Structure of the TPR Domain of p67phox in Complex with Rac·GTP
Lapouge, K., Smith, S. J. M., Walker, P. A., Gamblin, S. J., Smerdon, S. J., & Rittinger, K. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00091-2 · Cited by 311
Under cover: causes, effects and implications of Hsp90‐mediated genetic capacitance
Sangster, T. A., Lindquist, S., & Queitsch, C. (2004) · BioEssays · doi:10.1002/bies.20020 · Cited by 251
Silverstein, A. M., Galigniana, M. D., Kanelakis, K. C., Radanyi, C., Renoir, J.-M., & Pratt, W. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.36980 · Cited by 186
20S cyclosome complex formation and proteolytic activity inhibited by the cAMP/PKA pathway
Yamashita, Y. M., Nakaseko, Y., Samejima, I., Kumada, K., Yamada, H., Michaelson, D., & Yanagida, M. (1996) · Nature · doi:10.1038/384276a0 · Cited by 163
Cheung-Flynn, J., Roberts, P. J., Riggs, D. L., & Smith, D. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300955200 · Cited by 96
Cited by
Physiology of the prion protein
Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617
The glucocorticoid responses are shaped by molecular chaperones
Grad, I., & Picard, D. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.018 · Cited by 423
Jackson, S. E. (2012) · Topics in Current Chemistry · doi:10.1007/128_2012_356 · Cited by 338
Effects of Sleep and Wake on Oligodendrocytes and Their Precursors
Bellesi, M., Pfister-Genskow, M., Maret, S., Keles, S., Tononi, G., & Cirelli, C. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.5102-12.2013 · Cited by 261
The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop
Schmid, A. B., Lagleder, S., Gräwert, M. A., Röhl, A., Hagn, F., Wandinger, S. K., Cox, M. B., Demmer, O., Richter, K., Groll, M., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2011.472 · Cited by 229
The proteome of central and peripheral retina with progression of age-related macular degeneration
Ethen, C. M., Reilly, C., Feng, X., Olsen, T. W., & Ferrington, D. A. (2006) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.05-1395 · Cited by 99
Metadata
- Authors
- Odunuga, O. O., Longshaw, V. M., & Blatch, G. L.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 2004-09-20
- Volume
- 26
- Issue
- 10
- Pages
- 1058-1068
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W1991101492
- Cited by
- 229
- References
- 8
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- closed
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