The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
FoldIndex(C): a simple tool to predict whether a given protein sequence is intrinsically unfolded
Open accessAbstract
Summary: An easy-to-use, versatile and freely available graphic web server, FoldIndex© is described: it predicts if a given protein sequence is intrinsically unfolded implementing the algorithm of Uversky and co-workers, which is based on the average residue hydrophobicity and net charge of the sequence. FoldIndex© has an error rate comparable to that of more sophisticated fold prediction methods. Sliding windows permit identification of large regions within a protein that possess folding propensities different from those of the whole protein. Availability: FoldIndex© can be accessed at http://bioportal.weizmann.ac.il/fldbin/findex Contact: [email protected] Supplementary information: http://www.weizmann.ac.il/sb/faculty_pages/Sussman/papers/suppl/Prilusky_2005
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Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,843
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins: Structure, Function, and Genetics · doi:10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7 · Cited by 2,078
Intrinsic Disorder and Protein Function
Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731 · cited 1×
“They include: PONDR (Romero et al., 1997; Dunker et al., 2002, http://www.disprot. org), NORSP (Liu and Rost, 2003, http://cubic.bioc.columbia.edu/ services/NORSp), DisEMBL™(Linding et al., 2003a, http://dis.”
Linding, R., Jensen, L. J., Diella, F., Bork, P., Gibson, T. J., & Russell, R. B. (2003) · Structure · doi:10.1016/j.str.2003.10.002 · Cited by 1,212
GlobPlot: exploring protein sequences for globularity and disorder
Linding, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg519 · Cited by 998
The DISOPRED server for the prediction of protein disorder
Ward, J. J., McGuffin, L. J., Bryson, K., Buxton, B. F., & Jones, D. T. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth195 · Cited by 688
Intrinsic protein disorder in complete genomes.
Dunker, A. K., Zoran Obradovic, A., Romero, P. R., Garner, E. C., & Brown, C. J. (2000) · PubMed · Cited by 661
Schweers, O., Schönbrunn-Hanebeck, E., Marx, A., & Mandelkow, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51080-8 · Cited by 567
Removing near-neighbour redundancy from large protein sequence collections.
Holm, L., & Sander, C. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.5.423 · Cited by 294
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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057
The MAP1 family of microtubule-associated proteins.
Dehmelt (2004) · Genome biology · doi:10.1186/gb-2004-6-1-204 · Cited by 972
Function and structure of inherently disordered proteins
Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.002 · Cited by 963
Self-citationStress granules and neurodegeneration
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Metadata
- Authors
- Prilusky, J., Felder, C. E., Zeev-Ben-Mordehai, T., Rydberg, E. H., Man, O., Beckmann, J. S., Silman, I., & Sussman, J. L.
- Venue
- Bioinformatics
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-06-14
- Volume
- 21
- Issue
- 16
- Pages
- 3435-3438
- ISSN
- 0266-7061 (ISSN-L)
- 1367-4803
- 1460-2059
- OpenAlex
- W2131965976
- Cited by
- 916
- References
- 20
- FWCI
- 14.40
- Type
- journal article
- Language
- en
- Open access
- bronze
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