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For: Kurotani A, Sakurai T. In Silico Analysis of Correlations between Protein Disorder and Post-Translational Modifications in Algae. Int J Mol Sci 2015;16:19812-35. [PMID: 26307970 DOI: 10.3390/ijms160819812] [Cited by in Crossref: 13] [Cited by in F6Publishing: 15] [Article Influence: 1.9] [Reference Citation Analysis]
Number Citing Articles
1 Launay H, Receveur-Bréchot V, Carrière F, Gontero B. Orchestration of algal metabolism by protein disorder. Arch Biochem Biophys 2019;672:108070. [PMID: 31408624 DOI: 10.1016/j.abb.2019.108070] [Cited by in Crossref: 7] [Cited by in F6Publishing: 6] [Article Influence: 2.3] [Reference Citation Analysis]
2 Wang Z, Yang J, Li G, Sun N, Sun W, Peng Q, Liu N. Chemical Modifications of Peptides and Proteins with Low Concentration Formaldehyde Studied by Mass Spectrometry. Chinese Journal of Analytical Chemistry 2016;44:1193-9. [DOI: 10.1016/s1872-2040(16)60949-0] [Cited by in Crossref: 10] [Article Influence: 1.7] [Reference Citation Analysis]
3 Jain G, Pendola M, Rao A, Cölfen H, Evans JS. A Model Sea Urchin Spicule Matrix Protein Self-Associates To Form Mineral-Modifying Protein Hydrogels. Biochemistry 2016;55:4410-21. [PMID: 27426695 DOI: 10.1021/acs.biochem.6b00619] [Cited by in Crossref: 19] [Cited by in F6Publishing: 18] [Article Influence: 3.2] [Reference Citation Analysis]
4 Johnson KL, Cassin AM, Lonsdale A, Wong GK, Soltis DE, Miles NW, Melkonian M, Melkonian B, Deyholos MK, Leebens-Mack J, Rothfels CJ, Stevenson DW, Graham SW, Wang X, Wu S, Pires JC, Edger PP, Carpenter EJ, Bacic A, Doblin MS, Schultz CJ. Insights into the Evolution of Hydroxyproline-Rich Glycoproteins from 1000 Plant Transcriptomes. Plant Physiol 2017;174:904-21. [PMID: 28446636 DOI: 10.1104/pp.17.00295] [Cited by in Crossref: 30] [Cited by in F6Publishing: 28] [Article Influence: 6.0] [Reference Citation Analysis]
5 Salazar-Retana AL, Maruri-López I, Hernández-Sánchez IE, Becerra-Flora A, Guerrero-González ML, Jiménez-Bremont JF. PEST sequences from a cactus dehydrin regulate its proteolytic degradation. PeerJ 2019;7:e6810. [PMID: 31143531 DOI: 10.7717/peerj.6810] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.7] [Reference Citation Analysis]
6 Appadurai R, Uversky VN, Srivastava A. The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins. J Membrane Biol 2019;252:273-92. [DOI: 10.1007/s00232-019-00069-2] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 2.0] [Reference Citation Analysis]
7 Zambelli B, Uversky VN, Ciurli S. Nickel impact on human health: An intrinsic disorder perspective. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2016;1864:1714-31. [DOI: 10.1016/j.bbapap.2016.09.008] [Cited by in Crossref: 82] [Cited by in F6Publishing: 55] [Article Influence: 13.7] [Reference Citation Analysis]
8 Johnson KL, Cassin AM, Lonsdale A, Bacic A, Doblin MS, Schultz CJ. Pipeline to Identify Hydroxyproline-Rich Glycoproteins. Plant Physiol 2017;174:886-903. [PMID: 28446635 DOI: 10.1104/pp.17.00294] [Cited by in Crossref: 33] [Cited by in F6Publishing: 33] [Article Influence: 6.6] [Reference Citation Analysis]
9 Chang EP, Perovic I, Rao A, Cölfen H, Evans JS. Insect Cell Glycosylation and Its Impact on the Functionality of a Recombinant Intracrystalline Nacre Protein, AP24. Biochemistry 2016;55:1024-35. [PMID: 26784838 DOI: 10.1021/acs.biochem.5b01186] [Cited by in Crossref: 18] [Cited by in F6Publishing: 15] [Article Influence: 3.0] [Reference Citation Analysis]
10 Alves CML, Noyszewski AK, Smith AG. Structure and function of class III pistil-specific extensin-like protein in interspecific reproductive barriers. BMC Plant Biol 2019;19:118. [PMID: 30922239 DOI: 10.1186/s12870-019-1728-8] [Cited by in Crossref: 5] [Cited by in F6Publishing: 4] [Article Influence: 1.7] [Reference Citation Analysis]
11 Landau KS, Na I, Schenck RO, Uversky VN. Unfoldomics of prostate cancer: on the abundance and roles of intrinsically disordered proteins in prostate cancer. Asian J Androl 2016;18:662-72. [PMID: 27453073 DOI: 10.4103/1008-682X.184999] [Cited by in Crossref: 6] [Cited by in F6Publishing: 1] [Article Influence: 1.2] [Reference Citation Analysis]
12 Noyszewski AK, Liu YC, Tamura K, Smith AG. Polymorphism and structure of style-specific arabinogalactan proteins as determinants of pollen tube growth in Nicotiana. BMC Evol Biol 2017;17:186. [PMID: 28797243 DOI: 10.1186/s12862-017-1011-2] [Cited by in Crossref: 9] [Cited by in F6Publishing: 7] [Article Influence: 1.8] [Reference Citation Analysis]
13 Darling AL, Uversky VN. Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter. Front Genet 2018;9:158. [PMID: 29780404 DOI: 10.3389/fgene.2018.00158] [Cited by in Crossref: 95] [Cited by in F6Publishing: 90] [Article Influence: 23.8] [Reference Citation Analysis]
14 Carmicheal J, Atri P, Sharma S, Kumar S, Chirravuri Venkata R, Kulkarni P, Salgia R, Ghersi D, Kaur S, Batra SK. Presence and structure-activity relationship of intrinsically disordered regions across mucins. FASEB J 2020;34:1939-57. [PMID: 31908009 DOI: 10.1096/fj.201901898RR] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 1.5] [Reference Citation Analysis]
15 Zhang Y, Launay H, Schramm A, Lebrun R, Gontero B. Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii. Sci Rep 2018;8:6805. [PMID: 29717210 DOI: 10.1038/s41598-018-24772-7] [Cited by in Crossref: 14] [Cited by in F6Publishing: 16] [Article Influence: 3.5] [Reference Citation Analysis]
16 Banerjee S, Feyertag F, Alvarez-Ponce D. Intrinsic protein disorder reduces small-scale gene duplicability. DNA Res 2017;24:435-44. [PMID: 28430886 DOI: 10.1093/dnares/dsx015] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.6] [Reference Citation Analysis]