The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
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Citations
Cites
Sikorski, R. S., & Hieter, P. (1989) · Genetics · doi:10.1093/genetics/122.1.19 · Cited by 8,664
Gething, M.-J., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,123
Quality control in the secretory pathway
Hammond, C., & Helenius, A. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80009-3 · Cited by 673
A comparison of strategies to stabilize immunoglobulin Fv-fragments
Glockshuber, R., Malia, M., Pfitzinger, I., & Plueckthun, A. (1990) · Biochemistry · doi:10.1021/bi00458a002 · Cited by 473
Dorner, A. J., Wasley, L. C., & Kaufman, R. J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05201.x · Cited by 342
Protein Disulfide Isomerase and Assisted Protein Folding
Gilbert, H. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29399 · Cited by 281
Nieba, L., Honegger, A., Krebber, C., & Pluckthun, A. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.4.435 · Cited by 248
Engineered turns of a recombinant antibody improve its in vivo folding
Knappik, A., & Plückthun, A. (1995) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/8.1.81 · Cited by 239
Self-citationThe Essential Function of Protein-disulfide Isomerase Is to Unscramble Non-native Disulfide Bonds
Laboissière, M. C. A., Sturley, S. L., & Raines, R. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.28006 · Cited by 210
Self-citationRobinson, A. S., Hines, V., & Wittrup, K. D. (1994) · Bio/Technology · doi:10.1038/nbt0494-381 · Cited by 205
Self-citation
Cited by
Madzak, C., Gaillardin, C., & Beckerich, J.-M. (2004) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2003.10.027 · Cited by 386
Expression of Recombinant Antibodies
Frenzel, A., Hust, M., & Schirrmann, T. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00217 · Cited by 353
[25] Yeast surface display for directed evolution of protein expression, affinity, and stability
Boder, E. T., & Wittrup, K. D. (2000) · Methods in Enzymology · doi:10.1016/s0076-6879(00)28410-3 · Cited by 324
Self-citationHohenblum, H., Gasser, B., Maurer, M., Borth, N., & Mattanovich, D. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.10904 · Cited by 276
Applications of yeast in biotechnology: protein production and genetic analysis
Cereghino, G. P. L., & Cregg, J. M. (1999) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(99)00004-x · Cited by 176
Metadata
- Authors
- Shusta, E. V., Raines, R. T., Plückthun, A., & Wittrup, K. D.
- Venue
- Nature Biotechnology
- Published
- 1998-08
- Volume
- 16
- Issue
- 8
- Pages
- 773-777
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W1971498704
- Cited by
- 276
- References
- 31
- FWCI
- 3.04
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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How to cite
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- This page
- CoChat. (2026). Citation check: Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. https://app.cochat.ai/papers/10.1038/nbt0898-773
- The paper
- Shusta, E. V., Raines, R. T., Plückthun, A., & Wittrup, K. D. (1998). Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nature Biotechnology. https://doi.org/10.1038/nbt0898-773
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.