The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTReconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregationGerd Zettlmeissl, Rainer Rudolph, and Rainer JaenickeCite this: Biochemistry 1979, 18, 25, 5567–5571Publication Date (Print):December 11, 1979Publication History Published online1 May 2002Published inissue 11 December 1979https://pubs.acs.org/doi/10.1021/bi00592a007https://doi.org/10.1021/bi00592a007research-articleACS PublicationsRequest reuse permissionsArticle Views418Altmetric-Citations221LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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Citations
Cites
Experimental and Theoretical Aspects of Protein Folding
Anfinsen, C. B., & Scheraga, H. A. (1975) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60413-1 · Cited by 969
The flattering of the absorption spectrum of suspensions, as compared to that of solutions
Duyens, L. N. M. (1956) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(56)90380-8 · Cited by 718
Intermediates in Protein Folding Reactions and the Mechanism of Protein Folding
Baldwin, R. L. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.002321 · Cited by 256
Protein conformation in biomembranes: Optical rotation and absorption of membrane suspensions
Urry, D. W. (1972) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(72)90021-4 · Cited by 203
The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation.
Orsini, G., & Goldberg, M. E. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34821-4 · Cited by 122
Cited by
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,921
Protein aggregation: folding aggregates, inclusion bodies and amyloid
Fink, A. L. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00002-9 · Cited by 1,157
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
Colon, W., & Kelly, J. W. (1992) · Biochemistry · doi:10.1021/bi00151a036 · Cited by 573
GroE facilitates refolding of citrate synthase by suppressing aggregation
Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F. X., & Kiefhaber, T. (1991) · Biochemistry · doi:10.1021/bi00220a020 · Cited by 485
Self-citationKiefhaber, T., Rudolph, R., Kohler, H.-H., & Buchner, J. (1991) · Nature Biotechnology · doi:10.1038/nbt0991-825 · Cited by 441
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Metadata
- Authors
- Zettlmeissl, G., Rudolph, R., & Jaenicke, R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1979-12-11
- Volume
- 18
- Issue
- 25
- Pages
- 5567-5571
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1997088693
- Cited by
- 280
- References
- 5
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- closed
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