The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Kinetics of Molecular Chaperone Action
Abstract
Molecular chaperones of the Hsp70 type transiently sequester unfolded segments of proteins and promote their correct folding. Target peptides were labeled with an environmentally sensitive fluorophore so that their binding to the molecular chaperone DnaK of Escherichia coli could be followed in real time. The two-step process was characterized by relaxation times of 27 seconds and 200 seconds with 2 μM DnaK and 0.1 μM ligand at 25°C. In the presence of adenosine triphosphate, the formation of the complex was greatly accelerated and appeared to be a single-exponential process with a relaxation time of 0.4 second. The binding-release cycle of DnaK thus occurs in the time range of polypeptide chain elongation and folding and is too fast to be stoichiometrically coupled to the adenosine triphosphatase activity of the chaperone (turnover number, 0.13 per minute at 30°C).
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Speculations on the functions of the major heat shock and glucose-regulated proteins
Pelham, H. R. B. (1986) · Cell · doi:10.1016/0092-8674(86)90693-8 · Cited by 1,546
Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
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Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
Rothman, J. E. (1989) · Cell · doi:10.1016/0092-8674(89)90005-6 · Cited by 879
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., & Zylicz, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.7.2874 · Cited by 845
Peptide-binding specificity of the molecular chaperone BiP
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Cited by
Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., & Hendrickson, W. A. (1996) · Science · doi:10.1126/science.272.5268.1606 · Cited by 1,258
Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones
Mayer, M. P., & Gierasch, L. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002810 · Cited by 295
HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum
Wang, J., Lee, J., Liem, D., & Ping, P. (2017) · Gene · doi:10.1016/j.gene.2017.03.005 · Cited by 308
NEMO Trimerizes through Its Coiled-coil C-terminal Domain
Agou, F., Ye, F., Goffinont, S., Courtois, G., Yamaoka, S., Israël, A., & Véron, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201964200 · Cited by 79
Eftekharzadeh, B., Banduseela, V. C., Chiesa, G., Martínez-Cristóbal, P., Rauch, J. N., Nath, S. R., Schwarz, D. M. C., Shao, H., Marin-Argany, M., Di Sanza, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11594-y · Cited by 76
Metadata
- Authors
- Schmid, D., Baici, A., Gehring, H., & Christen, P.
- Venue
- Science
- Published
- 1994-02-18
- Volume
- 263
- Issue
- 5149
- Pages
- 971-973
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2089457735
- Cited by
- 438
- References
- 12
- FWCI
- 8.33
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
