The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Extraordinary Stability of Enzymes Dried in Trehalose: Simplified Molecular Biology
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Citations
Cites
Stabilization of dry phospholipid bilayers and proteins by sugars
Crowe, J. H., Crowe, L. M., Carpenter, J. F., & Aurell Wistrom, C. (1987) · Biochemical Journal · doi:10.1042/bj2420001 · Cited by 924
Protein Hydration in Aqueous Solution
Otting, G., Liepinsh, E., & Wüthrich, K. (1991) · Science · doi:10.1126/science.1948083 · Cited by 787
Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly
Green, J. L., & Angell, C. A. (1989) · The Journal of Physical Chemistry · doi:10.1021/j100345a006 · Cited by 609
Regulation of trehalose mobilization in fungi
Thevelein, J. M. (1984) · Microbiological Reviews · doi:10.1128/mmbr.48.1.42-59.1984 · Cited by 565
The mechanism of cryoprotection of proteins by solutes
Carpenter, J. F., & Crowe, J. H. (1988) · Cryobiology · doi:10.1016/0011-2240(88)90032-6 · Cited by 560
The Leeuwenhoek Lecture - The problem of anabiosis or latent life: history and current concept
Keilin, D. (1959) · Proceedings of the Royal Society of London. Series B - Biological Sciences · doi:10.1098/rspb.1959.0013 · Cited by 541
The Metabolism of α,α-Trehalose
Elbein, A. D. (1974) · Advances in Carbohydrate Chemistry and Biochemistry · doi:10.1016/s0065-2318(08)60266-8 · Cited by 526
Crowe, J. H., Carpenter, J. F., Crowe, L. M., & Anchordoguy, T. J. (1990) · Cryobiology · doi:10.1016/0011-2240(90)90023-w · Cited by 467
A restriction map of the bacteriophage T4 genome
O’Farrell, P. H., Kutter, E. M., & Nakanishi, M. (1980) · Molecular and General Genetics MGG · doi:10.1007/bf00425473 · Cited by 306
STRUCTURE AND DYNAMICS OF WATER SURROUNDING BIOMOLECULES
Saenger, W. (1987) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.16.060187.000521 · Cited by 301
Cited by
Richards, A. B., Krakowka, S., Dexter, L. B., Schmid, H., Wolterbeek, A. P. M., Waalkens-Berendsen, D. H., Shigoyuki, A., & Kurimoto, M. (2002) · Food and Chemical Toxicology · doi:10.1016/s0278-6915(02)00011-x · Cited by 593
Trehalose: Current Use and Future Applications
Ohtake, S., & Wang, Y. J. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22458 · Cited by 487
Navati, M. S., & Friedman, J. M. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp909425z · Cited by 12
Metadata
- Authors
- Colaço, C., Sen, S., Thangavelu, M., Pinder, S., & Roser, B.
- Venue
- Nature Biotechnology
- Published
- 1992-09
- Volume
- 10
- Issue
- 9
- Pages
- 1007-1011
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W1985706410
- Cited by
- 277
- References
- 17
- FWCI
- 3.94
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Extraordinary Stability of Enzymes Dried in Trehalose: Simplified Molecular Biology. https://app.cochat.ai/papers/10.1038/nbt0992-1007
- The paper
- Colaço, C., Sen, S., Thangavelu, M., Pinder, S., & Roser, B. (1992). Extraordinary Stability of Enzymes Dried in Trehalose: Simplified Molecular Biology. Nature Biotechnology. https://doi.org/10.1038/nbt0992-1007
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.
