The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Converging concepts of protein folding in vitro and in vivo
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Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
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
Self-citationSittler, A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.12.1307 · Cited by 442 · cited 1×
“It also suggests that searching for ways to re-establish protein homeostasis, for example by upregulating the expression of chaperones, may offer promising venues for therapeutic interventio”
BackgroundPolypeptide Flux through Bacterial Hsp70
Teter, S. A., Houry, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., & Hartl, F. U. (1999) · Cell · doi:10.1016/s0092-8674(00)80787-4 · Cited by 424
Self-citationThe native 3D organization of bacterial polysomes
Brandt, F., Etchells, S. A., Ortiz, J. O., Elcock, A. H., Hartl, F. U., & Baumeister, W. (2009) · Cell · doi:10.1016/j.cell.2008.11.016 · Cited by 258
The interaction network of the chaperonin CCT
Dekker, C., Stirling, P. C., McCormack, E. A., Filmore, H., Paul, A., Brost, R. L., Costanzo, M., Boone, C., Leroux, M. R., & Willison, K. R. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.108 · Cited by 220
Cited by
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
Self-citationHSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Clearance systems in the brain—implications for Alzheimer disease
Tarasoff-Conway, J. M., Carare, R. O., Osorio, R. S., Glodzik, L., Butler, T., Fieremans, E., Axel, L., Rusinek, H., Nicholson, C., Zlokovic, B. V., et al. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.119 · Cited by 1,678
The endoplasmic reticulum: structure, function and response to cellular signaling
Schwarz, D. S., & Blower, M. D. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2052-6 · Cited by 1,613
Protein misfolding in neurodegenerative diseases: Implications and strategies
Sweeney, P., Park, H., Baumann, M., Dunlop, J., Frydman, J., Kopito, R., McCampbell, A., Leblanc, G., Venkateswaran, A., Nurmi, A., et al. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0077-5 · Cited by 675
Metadata
- Authors
- Hartl, F. U., & Hayer-Hartl, M.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-06
- Volume
- 16
- Issue
- 6
- Pages
- 574-581
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2078010704
- Cited by
- 1,185
- References
- 9
- FWCI
- 40.93
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hartl, F. U., & Hayer-Hartl, M. (2009). Converging concepts of protein folding in vitro and in vivo. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1591
Data sources
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.
