The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Enzyme Kinetics Determined Using Calorimetry: A General Assay for Enzyme Activity?
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Citations
Cites
Rapid measurement of binding constants and heats of binding using a new titration calorimeter
Wiseman, T., Williston, S., Brandts, J. F., & Lin, L.-N. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90213-3 · Cited by 2,675
Microbial ureases: significance, regulation, and molecular characterization.
Mobley, H. L., & Hausinger, R. P. (1989) · Microbiological Reviews · doi:10.1128/mmbr.53.1.85-108.1989 · Cited by 1,507
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., & Sigler, P. B. (1994) · Nature · doi:10.1038/371578a0 · Cited by 1,321
STRUCTURE-BASED INHIBITORS OF HIV-1 PROTEASE
Wlodawer, A., & Erickson, J. W. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.002551 · Cited by 833
Isothermal titration calorimetry
Freire, E., Mayorga, O. L., & Straume, M. (1990) · Analytical Chemistry · doi:10.1021/ac00217a002 · Cited by 602
Novel Fluorogenic Substrates for Assaying Retroviral Proteases by Resonance Energy Transfer
Matayoshi, E. D., Wang, G. T., Krafft, G. A., & Erickson, J. (1990) · Science · doi:10.1126/science.2106161 · Cited by 592
Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding
Todd, M. J., Viitanen, P. V., & Lorimer, G. H. (1994) · Science · doi:10.1126/science.7913555 · Cited by 457
Self-citationViitanen, P. V., Lubben, T. H., Reed, J., Goloubinoff, P., O'Keefe, D. P., & Lorimer, G. H. (1990) · Biochemistry · doi:10.1021/bi00476a003 · Cited by 380
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
Weissman, J. S., Kashi, Y., Fenton, W. A., & Horwich, A. L. (1994) · Cell · doi:10.1016/0092-8674(94)90533-9 · Cited by 358
Debouck, C., Gorniak, J. G., Strickler, J. E., Meek, T. D., Metcalf, B. W., & Rosenberg, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.8903 · Cited by 278
Cited by
Freyer, M. W., & Lewis, E. A. (2008) · Methods in Cell Biology · doi:10.1016/s0091-679x(07)84004-0 · Cited by 512
Enzyme technology: an overview
Beilen, J. B. V., & Li, Z. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00334-8 · Cited by 320
Mapping the reaction coordinates of enzymatic defluorination
Chan, P. W. Y., Yakunin, A. F., Edwards, E. A., & Pai, E. F. (2011) · Journal of the American Chemical Society · doi:10.1021/ja200277d · Cited by 107
Sequence‐ and activity‐based screening of microbial genomes for novel dehalogenases
Chan, W. Y., Wong, M., Guthrie, J., Savchenko, A. V., Yakunin, A. F., Pai, E. F., & Edwards, E. A. (2010) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2009.00155.x · Cited by 77
Vincents, B., Guentsch, A., Kostolowska, D., von Pawel‐Rammingen, U., Eick, S., Potempa, J., & Abrahamson, M. (2011) · The FASEB Journal · doi:10.1096/fj.11-187799 · Cited by 64
Metadata
- Authors
- Todd, M. J., & Gomez, J.
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 2001-09
- Volume
- 296
- Issue
- 2
- Pages
- 179-187
- ISSN
- 0003-2697 (ISSN-L)
- OpenAlex
- W2118527243
- Cited by
- 351
- References
- 25
- FWCI
- 4.32
- Type
- journal article
- Language
- en
- Open access
- closed
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- Todd, M. J., & Gomez, J. (2001). Enzyme Kinetics Determined Using Calorimetry: A General Assay for Enzyme Activity? Analytical Biochemistry. https://doi.org/10.1006/abio.2001.5218
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.
