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NTIS 바로가기Biochemical and biophysical research communications, v.494 no.3/4, 2017년, pp.602 - 607
Ota, Haruki (Corresponding author.) , Fukuchi, Satoshi
Abstract Intrinsically disordered proteins are proteins with intrinsically disordered regions (IDRs) that do not adopt a globular structure in their free state. IDRs have unique regions having protein-binding segments of which play pivotal roles in many biological processes. The binding sites in ID...
Biochemistry Dunker 41 6573 2002 10.1021/bi012159+ Intrinsic disorder and protein function
Nat. Rev. Mol. Cell Biol. Dyson 6 197 2005 10.1038/nrm1589 Intrinsically unstructured proteins and their functions
FEBS Lett. Tompa 579 3346 2005 10.1016/j.febslet.2005.03.072 The interplay between structure and function in intrinsically unstructured proteins
Biochim. Biophys. Acta Uversky 1804 1231 2010 10.1016/j.bbapap.2010.01.017 Understanding protein non-folding
BMC Struct. Biol. Fukuchi 11 29 2011 10.1186/1472-6807-11-29 Binary classification of protein molecules into intrinsically disordered and ordered segments
J. Mol. Biol. Minezaki 359 1137 2006 10.1016/j.jmb.2006.04.016 Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation
J. Mol. Biol. Ward 337 635 2004 10.1016/j.jmb.2004.02.002 Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
J. Mol. Biol. Iakoucheva 323 573 2002 10.1016/S0022-2836(02)00969-5 Intrinsic disorder in cell-signaling and cancer-associated proteins
Nucleic Acids Res. Fukuchi 42 D320 2014 10.1093/nar/gkt1010 IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners
Nucleic Acids Res. Fukuchi 40 D507 2012 10.1093/nar/gkr884 IDEAL: intrinsically disordered proteins with extensive annotations and literature
Nucleic Acids Res. Dinkel 44 D294 2016 10.1093/nar/gkv1291 ELM 2016-data update and new functionality of the eukaryotic linear motif resource
Mol. Biosyst. Moesa 8 3262 2012 10.1039/c2mb25202c Chemical composition is maintained in poorly conserved intrinsically disordered regions and suggests a means for their classification
Sci. Signal Nguyen Ba 5 rs1 2012 10.1126/scisignal.2002515 Proteome-wide discovery of evolutionary conserved sequences in disordered regions
Curr. Opin. Struct. Biol. Schlessinger 21 412 2011 10.1016/j.sbi.2011.03.014 Protein disorder-a breakthrough invention of evolution?
Mol. Biol. Evol. Brown 27 609 2010 10.1093/molbev/msp277 Comparing models of evolution for ordered and disordered proteins
PLoS Comput. Biol. Xia 5 e1000413 2009 10.1371/journal.pcbi.1000413 Integrated assessment of genomic correlates of protein evolutionary rate
Mol. Biosyst. Nido 8 353 2012 10.1039/C1MB05199G Protein disorder in the centrosome correlates with complexity in cell types number
Nucleic Acids Res. The UniProt 45 D158 2017 10.1093/nar/gkw1099 UniProt: the universal protein knowledgebase
Bioinformatics Larkin 23 2947 2007 10.1093/bioinformatics/btm404 Clustal W and clustal X version 2.0
Bioinformatics Pei 17 700 2001 10.1093/bioinformatics/17.8.700 AL2CO: calculation of positional conservation in a protein sequence alignment
Proteins Valdar 42 108 2001 10.1002/1097-0134(20010101)42:1<108::AID-PROT110>3.0.CO;2-O Protein-protein interfaces: analysis of amino acid conservation in homodimers
EMBO J. Eklof Spink 20 6203 2001 10.1093/emboj/20.22.6203 Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex
EMBO J. Dajani 22 494 2003 10.1093/emboj/cdg068 Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex
J. Med. Chem. Fugel 56 264 2013 10.1021/jm301575n 3,6-Diamino-4-(2-halophenyl)-2-benzoylthieno[2,3-b]pyridine-5-carbonitriles are selective inhibitors of Plasmodium falciparum glycogen synthase kinase-3
Elife Stamos 3 e01998 2014 10.7554/eLife.01998 Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6
J. Med. Chem. Tahtouh 55 9312 2012 10.1021/jm301034u Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B
J. Mol. Biol. Takeda 412 226 2011 10.1016/j.jmb.2011.07.038 Structural basis of importin-alpha-mediated nuclear transport for Ku70 and Ku80
Nature Walker 412 607 2001 10.1038/35088000 Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair
Mol. Biosyst. Davey 8 268 2012 10.1039/C1MB05231D Attributes of short linear motifs
Science Holt 325 1682 2009 10.1126/science.1172867 Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution
PLoS Genet. Kim 8 e1002510 2012 10.1371/journal.pgen.1002510 Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution
Elife Hultqvist 6 2017 10.7554/eLife.16059 Emergence and evolution of an interaction between intrinsically disordered proteins
Genet. Mol. Biol. Viscardi 40 181 2017 10.1590/1678-4685-gmb-2016-0115 FOXP in Tetrapoda: intrinsically disordered regions, short linear motifs and their evolutionary significance
Biochemistry Subekti 56 4134 2017 10.1021/acs.biochem.7b00292 The disordered linker in p53 participates in nonspecific binding to and one-dimensional sliding along DNA revealed by single-molecule fluorescence measurements
Mol. Cell Tompa 55 161 2014 10.1016/j.molcel.2014.05.032 A million peptide motifs for the molecular biologist
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