The DOI matches its Crossref record; 58 of the 59 references it cites were found in a registry or an index.
Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions
Open accessAbstract
The nuclear factor CREB activates transcription of target genes in part through direct interactions with the KIX domain of the coactivator CBP in a phosphorylation-dependent manner. The solution structure of the complex formed by the phosphorylated kinase-inducible domain (pKID) of CREB with KIX reveals that pKID undergoes a coil-->helix folding transition upon binding to KIX, forming two alpha helices. The amphipathic helix alphaB of pKID interacts with a hydrophobic groove defined by helices alpha1 and alpha3 of KIX. The other pKID helix, alphaA, contacts a different face of the alpha3 helix. The phosphate group of the critical phosphoserine residue of pKID forms a hydrogen bond to the side chain of Tyr-658 of KIX. The structure provides a model for interactions between other transactivation domains and their targets.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“a single hydrogen bond between this phosphoserine and a tyrosine residue within CBP is critical for complexation”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Radhakrishnan et al., 1997
Citations
Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952
Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
Gonzalez, G. A., & Montminy, M. (1989) · Cell · doi:10.1016/0092-8674(89)90013-5 · Cited by 2,464
Self-citationStructure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S.-C., Heyman, R. A., Rose, D. W., Glass, C. K., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81118-6 · Cited by 2,150
Phosphorylated CREB binds specifically to the nuclear protein CBP
Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052
Self-citationThe CBP co-activator is a histone acetyltransferase
Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,828
Knighton, D. R., Zheng, J., Eyck, L. F. T., Ashford, V. A., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,764
Research works printed but not linked: 1
- Bannister, 1995, Stimulation of c-Jun activity by CBP, Oncogene, 11, 2509
Cited by
Sorted by citations
Items 401–500 of 729
Flipping a genetic switch by subunit exchange
Lambert, L. J., Schirf, V., Demeler, B., Cadène, M., & Werner, M. H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.7149 · Cited by 31
Jing, Y.-P., Wang, D., Han, X.-L., Dong, D.-J., Wang, J.-X., & Zhao, X.-F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.706028 · Cited by 30
Capturing a Dynamic Chaperone–Substrate Interaction Using NMR-Informed Molecular Modeling
Salmon, L., Ahlstrom, L. S., Horowitz, S. A., Dickson, A., Brooks, C. L., & Bardwell, J. C. A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b02382 · Cited by 31
Peng, H., Gibson, L. C., Capili, A. D., Borden, K. L. B., Osborne, M. J., Harper, S. L., Speicher, D. W., Zhao, K., Marmorstein, R., Rock, T. A., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.047 · Cited by 30
Molecular Characterization of HTLV-1 Tax Interaction with the KIX Domain of CBP/p300
Ramírez, J. A., & Nyborg, J. K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.06.062 · Cited by 30
Cowley, S. M., Kang, R. S.-O., Frangioni, J. V., Yada, J. J., DeGrand, A. M., Radhakrishnan, I., & Eisenman, R. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2698-2709.2004 · Cited by 30
Self-citationDisordered TPPP/p25 binds GTP and displays Mg2+ -dependent GTPase activity
Zotter, Á., Bodor, A., Oláh, J., Hlavanda, E., Orosz, F., Perczel, A., & Ovádi, J. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.02.006 · Cited by 29
Lee, K. H., & Chen, J. (2017) · Journal of Computational Chemistry · doi:10.1002/jcc.24734 · Cited by 29
Burkart, A. D., Mukherjee, A., & Mayo, K. E. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0204 · Cited by 29
PreSMo Target-Binding Signatures in Intrinsically Disordered Proteins.
Kim, D.-H., & Han, K. (2018) · Europe PMC (PubMed Central) · doi:10.14348/molcells.2018.0192 · Cited by 28
Hosoya, Y., & Ohkanda, J. (2021) · Molecules · doi:10.3390/molecules26082118 · Cited by 30
Combinatorial regulation of a signal-dependent activator by phosphorylation and acetylation
Paz, J. C., Park, S., Phillips, N., Matsumura, S., Tsai, W., Kasper, L. H., Brindle, P. K., Zhang, G., Zhou, M., Wright, P. E., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420389111 · Cited by 28
Self-citationA Tale of Chromatin and Transcription in 100 Structures
Cramer, P. (2014) · Cell · doi:10.1016/j.cell.2014.10.047 · Cited by 28
Uncoupled binding and folding of immune signaling-related intrinsically disordered proteins
Sigalov, A. B. (2011) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2011.08.005 · Cited by 28
Denis, C. M., Langelaan, D. N., Kirlin, A. C., Chitayat, S., Munro, K., Spencer, H. L., LeBrun, D. P., & Smith, S. P. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku206 · Cited by 27
Immobilized Peptides as High-Affinity Capture Agents for Self-Associating Proteins
Naffin-Olivos, J. L., Han, Y., Olivos, H. J., Reddy, M. M., Sun, T., & Kodadek, T. J. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00049-8 · Cited by 28
Li, P., Gao, X.-G., Arellano, R. O., & Renugopalakrishnan, V. (2001) · Protein Expression and Purification · doi:10.1006/prep.2001.1431 · Cited by 28
Shi, X.-Z. P., Choudhury, B. K., Pasricha, P. J., & Sarna, S. K. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.02.016 · Cited by 28
Insight Into the Tumor Suppressor Function of CBP Through the Viral Oncoprotein Tax
Orden, K. V., & Nyborg, J. K. (2001) · Gene Expression · doi:10.3727/000000001783992678 · Cited by 28
Intrinsic disorder accelerates dissociation rather than association
Umezawa, K., Ohnuki, J., Higo, J., & Takano, M. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25057 · Cited by 27
Differential Regulation of the BDNF Gene in Cortical and Hippocampal Neurons
Esvald, E., Tuvikene, J., Moistus, A., Rannaste, K., Kõomägi, S., & Timmusk, T. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.2535-21.2022 · Cited by 29
Specialized rules of gene transcription in male germ cells: the CREM paradigm*
Monaco, L., Kotaja, N., Fienga, G., Hogeveen, K. N., Kolthur‐Seetharam, U., Kimmins, S., Brancorsini, S., Macho, B., & Sassone‐Corsi, P. (2004) · International Journal of Andrology · doi:10.1111/j.1365-2605.2004.00494.x · Cited by 27
Zhong, Z., Chang, S. A., Kalinowski, A., Wilson, K. L., & Dahl, K. N. (2010) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-010-0121-3 · Cited by 27
Kumar, V., Waseem, M., Dwivedi, N., Maji, S., Kumar, A., & Thakur, J. K. (2018) · Plant Signaling & Behavior · doi:10.1080/15592324.2018.1428514 · Cited by 28
Extreme Fuzziness: Direct Interactions between Two IDPs
Wang, W., & Wang, D. (2019) · Biomolecules · doi:10.3390/biom9030081 · Cited by 27
Intrinsic disorder and coiled‐coil formation in prostate apoptosis response factor 4
Libich, D. S., Schwalbe, M., Kate, S., Venugopal, H., Claridge, J. K., Edwards, P. J. B., Dutta, K., & Pascal, S. M. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07087.x · Cited by 27
The Multifunctional Role of E1A in the Transcriptional Regulation of CREB/CBP-Dependent Target Genes
Brockmann, D., & Esche, H. (2003) · Current topics in microbiology and immunology · doi:10.1007/978-3-662-05597-7_4 · Cited by 27
TOLNAY, M., JUANG, Y.-T., & TSOKOS, G. C. (2002) · Biochemical Journal · doi:10.1042/bj3630127 · Cited by 27
Involvement of cAMP Response Element-Binding Protein Activation in Salivary Secretion
Yamada, K., Inoue, H., Kida, S., Masushige, S., Nishiyama, T., Mishima, K., & Saito, I. (2006) · Pathobiology · doi:10.1159/000093086 · Cited by 26
Lee, J., Tong, T., Takemori, H., & Jefcoate, C. R. E. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.01.022 · Cited by 26
Szénási, T., Oláh, J., Szabó, A., Szunyogh, S., Láng, A., Perczel, A., Lehotzky, A., Uversky, V. N., & Ovádi, J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.09.017 · Cited by 26
Steven, A., Heiduk, M., Recktenwald, C. V., Hiebl, B., Wickenhauser, C., Massa, C., & Seliger, B. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0590 · Cited by 26
A specific programme of gene transcription in male germ cells
Kimmins, S., Kotaja, N., Fienga, G., Kolthur‐Seetharam, U., Brancorsini, S., Hogeveen, K. N., Monaco, L., & Sassone‐Corsi, P. (2004) · Reproductive BioMedicine Online · doi:10.1016/s1472-6483(10)61094-2 · Cited by 26
Chong, P. A., Ozdamar, B., Wrana, J. L., & Forman-Kay, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404375200 · Cited by 26
Wagner, B. L., Bauer, A., Schütz, G., & Montminy, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8263 · Cited by 26
Self-citationCan You Hear Me Now? Regulating Transcriptional Activators by Phosphorylation
Gardner, K. H., & Montminy, M. (2005) · Science's STKE · doi:10.1126/stke.3012005pe44 · Cited by 25
Self-citationCoiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
Mueller, C., & Grossmann, T. N. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201811515 · Cited by 25
Takayama, Y., Nakasako, M., Okajima, K., Iwata, A., Kashojiya, S., Matsui, Y., & Tokutomi, S. (2011) · Biochemistry · doi:10.1021/bi101689b · Cited by 26
Phosphorylation of the IDP KID Modulates Affinity for KIX by Increasing the Lifetime of the Complex
Dahal, L., Shammas, S. L., & Clarke, J. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.10.015 · Cited by 25
Visible-light-driven photocontrol of the Trp-cage protein fold by a diazocine cross-linker.
Preußke, N., Moormann, W., Bamberg, K., Lipfert, M., Herges, R., & Sönnichsen, F. (2020) · Organic and biomolecular chemistry · doi:10.1039/c9ob02442e · Cited by 6
Yang, C. K., Kim, J. H., & Stallcup, M. R. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0200 · Cited by 25
ZNF384-Related Fusion Genes in Acute Lymphoblastic Leukemia
Zhu, L., Bai, W., Cheng, Q., & Fang, J. (2023) · Cancer Control · doi:10.1177/10732748231182787 · Cited by 24
Functional Characterization and Conformational Analysis of the Herpesvirus saimiri Tip-C484 Protein
Mitchell, J., Trible, R. P., Emert‐Sedlak, L. A., Weis, D. D., Lerner, E. C., Applen, J. J., Sefton, B. M., Smithgall, T. E., & Engen, J. R. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.026 · Cited by 24
Nucleosome distortion as a possible mechanism of transcription activation domain function
Erkina, T. Y., & Erkine, A. M. (2016) · Epigenetics & Chromatin · doi:10.1186/s13072-016-0092-2 · Cited by 23
Matsuno, H., Furusawa, H., & Okahata, Y. (2004) · Chemistry - A European Journal · doi:10.1002/chem.200400030 · Cited by 24
A conserved helix‐unfolding motif in the naturally unfolded proteins
Zetina, C. R. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.1113 · Cited by 24
Butscher, W. G., Haggerty, C. M., Chaudhry, S., & Gardner, K. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009614200 · Cited by 24
Bridges, K. G., Hua, Q., Brigham-Burke, M. R., Martin, J. D., Hensley, P., Dahl, C. E., Digard, P., Weiss, M. A., & Coen, D. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.472 · Cited by 24
Promiscuity, stability and cold adaptation of a newly isolated acylaminoacyl peptidase
Brunialti, E., Gatti‐Lafranconi, P., & Lotti, M. (2011) · Biochimie · doi:10.1016/j.biochi.2011.05.010 · Cited by 23
Sambi, I., Gatti‐Lafranconi, P., Longhi, S., & Lotti, M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07825.x · Cited by 23
Dynamic α‐helices: Conformations that do not conform
Sandhu, K. S., & Dash, D. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21328 · Cited by 23
CBP-HSF2 structural and functional interplay in Rubinstein-Taybi neurodevelopmental disorder
de Thonel, A., Ahlskog, J. K., Daupin, K., Dubreuil, V., Berthelet, J., Chaput, C., Pires, G., Leonetti, C., Abane, R., Cordón-Barris, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34476-2 · Cited by 27
Re-Balancing Replica Exchange with Solute Tempering for Sampling Dynamic Protein Conformations
Zhang, Y., Liu, X., & Chen, J. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c01139 · Cited by 22
Shiina, M., Hamada, K., Inoue-Bungo, T., Shimamura, M., Uchiyama, A., Baba, S., Sato, K., Yamamoto, M., & Ogata, K. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.07.020 · Cited by 22
Jiang, M., Li, B. X., Xie, F., Delaney, F., & Xiao, X. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300043c · Cited by 21
Chu, X., & Wang, J. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp06803h · Cited by 21
Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
Hong, S., Choi, S., Kim, R., & Koh, J. (2020) · Molecules and Cells · doi:10.14348/molcells.2020.0186 · Cited by 23
Malarial EBA-175 Region VI Crystallographic Structure Reveals a KIX-Like Binding Interface
Martinez, C., Haire, L. F., Hackett, F., Walker, P. A., Howell, S. A., Smerdon, S. J., Dodson, G. G., & Blackman, M. J. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.071 · Cited by 23
Prediction of natively unfolded regions in protein chains
Galzitskaya, O. V., Garbuzynskiy, S. O., & Lobanov, M. Y. (2006) · Molecular Biology · doi:10.1134/s0026893306020166 · Cited by 21
Kistanova, E. K., Dell, H., Tsantili, P., Falvey, E., Cladaras, C., & Hadzopoulou‐Cladaras, M. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560635 · Cited by 21
SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA
Dudenhoeffer, B. R., Schneider, H., Schweimer, K., & Knauer, S. H. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz442 · Cited by 20
Peng, J., Miller, M. A., Li, B. X., & Xiao, X. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00499 · Cited by 20
Fast and accurate protein intrinsic disorder prediction by using a pretrained language model
Song, Y., Yuan, Q., Chen, S., Chen, K., Zhou, Y., & Yang, Y. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad173 · Cited by 21
Backbone conformational preferences of an intrinsically disordered protein in solution
Espinoza-Fonseca, M., Ilizaliturri‐Flores, I., & Correa‐Basurto, J. (2012) · Molecular BioSystems · doi:10.1039/c2mb00004k · Cited by 20
Structural investigation on the intrinsically disordered N-terminal region of HPV16 E7 protein
Lee, C., Kim, D., Lee, S., Su, J., & Han, K. (2016) · BMB Reports · doi:10.5483/bmbrep.2016.49.8.021 · Cited by 20
Linking CREB function with altered metabolism in murine fibroblast-based model cell lines
Steven, A., Leisz, S., Wickenhauser, C., Schulz, K., Mougiakakos, D., Kiessling, R. W., Denkert, C., & Seliger, B. (2017) · Oncotarget · doi:10.18632/oncotarget.22135 · Cited by 20
Jiang, M., Yan, Y., Yang, K., Liu, Z., Qi, J., Zhou, H., Qian, N., Zhou, Q., Wang, T., Xu, X. Y., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14024 · Cited by 20
Xie, F., Fan, Q., Li, B. X., & Xiao, X. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01207 · Cited by 21
Ozaki, J., Takemaru, K., Ikegami, T., Mishima, M., Ueda, H., Hirose, S., Kabe, Y., Handa, H., & Shirakawa, M. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00267.x · Cited by 20
Peptides Targeting Estrogen Receptor Alpha-Potential Applications for Breast Cancer Treatment
Leclercq, G., Gallo, D., Cossy, J., Laı̈os, I., Larsimont, D., Laurent, G., & Jacquot, Y. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211797416048 · Cited by 20
Lumb, K. J., & Mestas, S. P. (1999) · Nature Structural Biology · doi:10.1038/10655 · Cited by 20
Kim, J. H., Yang, C. K., & Stallcup, M. R. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl361 · Cited by 20
Cross-Regulation of T Cell Growth Factor Expression by p53 and the Tax Oncogene
Chaudhry, S., Freebern, W. J., Smith, J. L., Butscher, W. G., Haggerty, C. M., & Gardner, K. L. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.12.6767 · Cited by 20
Umezawa, K., Ikebe, J., Takano, M., Nakamura, H., & Higo, J. (2012) · Biomolecules · doi:10.3390/biom2010104 · Cited by 19
Small Molecule Modulation of Intrinsically Disordered Proteins Using Molecular Dynamics Simulations
Herrera-Nieto, P., Pérez, A., & Fabritiis, G. D. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00381 · Cited by 22
Xie, F., Li, B. X., Broussard, C., & Xiao, X. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.07.053 · Cited by 19
Inhibition of Ras-mediated signaling pathways in CML stem cells
Bertacchini, J., Ketabchi, N., Mediani, L., Capitani, S., Marmiroli, S., & Saki, N. (2015) · Cellular Oncology · doi:10.1007/s13402-015-0248-2 · Cited by 19
Clark, M. D., Kumar, G. S., Marcum, R. D., Luo, Q., Zhang, Y., & Radhakrishnan, I. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00332 · Cited by 19
Self-citationThe 9aaTAD Is Exclusive Activation Domain in Gal4
Piskáček, M., Havelka, M., Řezáčová, M., & Knight, A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169261 · Cited by 19
Yang, K., Stanfield, R. L., Martinez‐Yamout, M. A., Dyson, H. J., Wilson, I. A., & Wright, P. E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810397115 · Cited by 19
Self-citationDual Role of Protein Phosphorylation in DNA Activator/Coactivator Binding
Dadarlat, V. M., & Skeel, R. D. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2010.11.053 · Cited by 18
Dyson, H. J., & Wright, P. E. (2006) · IUBMB Life · doi:10.1080/15216540500484376 · Cited by 19
Self-citationCross, E., Duncan‐Flavell, P. J., Howarth, R. J., Hobbs, J. I., Thomas, N. S., & Bunyan, D. J. (2020) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61813 · Cited by 19
Mechanism of Ligand-Induced Folding of a Natively Unfolded Helixless Variant of Rabbit I-BABP
Rea, A. M., Thurston, V., & Searle, M. S. (2009) · Biochemistry · doi:10.1021/bi900805s · Cited by 18
Structural flexibility of intrinsically disordered proteins induces stepwise target recognition
Shirai, N. C., & Kikuchi, M. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4838476 · Cited by 18
Mechanism and rate constants of the Cdc42 GTPase binding with intrinsically disordered effectors
Pang, X., & Zhou, H. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25018 · Cited by 18
Rabuck-Gibbons, J. N., Lodge, J. M., Mapp, A. K., & Ruotolo, B. T. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-2043-6 · Cited by 18
Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy
Kim, D.-H., Lee, J., Mok, K. H., Lee, J., & Han, K. (2020) · Biomolecules · doi:10.3390/biom10030428 · Cited by 18
Shaywitz, A. J., Dove, S. L., Greenberg, M. E., & Hochschild, A. (2002) · Science s STKE · doi:10.1126/stke.2002.142.pl11 · Cited by 18
The evolution of the Amber additive protein force field: History, current status, and future
Wang, X., Xiong, D., Zhang, Y., Zhai, J., Gu, Y., & He, X. D. (2025) · The Journal of Chemical Physics · doi:10.1063/5.0227517 · Cited by 18
SARS‐CoV‐2 infection activates CREB/CBP in cellular cyclic AMP‐dependent pathways
Yang, Q., Tang, J., Cao, J., Liu, F., Fu, M., Xue, B., Zhou, A., Chen, S., Liu, J., Zhou, Y., et al. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28383 · Cited by 17
Martinez‐Yamout, M. A., Nasir, I., Shnitkind, S., Ellis, J. P., Berlow, R. B., Kroon, G. J. A., Deniz, A. A., Dyson, H. J., & Wright, P. E. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313835120 · Cited by 19
Self-citationPrehna, G., Ramirez, B. E., & Lovering, A. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115390 · Cited by 17
Espinoza-Fonseca, M. (2009) · Biochemistry · doi:10.1021/bi901705z · Cited by 17
Transcriptional tools: Small molecules for modulating CBP KIX‐dependent transcriptional activators
Bates, C. A., Pomerantz, W. C. K., & Mapp, A. K. (2010) · Biopolymers · doi:10.1002/bip.21548 · Cited by 17
Kim, D.-H., Lee, S., Nam, K. H., Chi, S., Chang, I.-S., & Han, K. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.7.411 · Cited by 17
Tunable regulation of CREB DNA binding activity couples genotoxic stress response and metabolism
Kim, S. H., Trinh, A. T., Larsen, M. C., Mastrocola, A. S., Jefcoate, C. R. E., Bushel, P. R., & Tibbetts, R. S. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw643 · Cited by 19
Activation and repression in the nervous system
Goodman, R. H., & Mandel, G. (1998) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(98)80069-x · Cited by 17
Dioxin-inducible Transactivation in a Chromosomal Setting
Jones, L. C., & Whitlock, J. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102910200 · Cited by 17
Crystal Structure of the CLOCK Transactivation Domain Exon19 in Complex with a Repressor
Hou, Z., Su, L., Pei, J., Grishin, N. V., & Zhang, H. (2017) · Structure · doi:10.1016/j.str.2017.05.023 · Cited by 16
Metadata
- Authors
- Radhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., & Wright, P. E.
- Affiliations
- Scripps Research Institute (US)
- Joslin Diabetes Center (US)
- Corresponding author
- Wright, Peter E
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-12
- Volume
- 91
- Issue
- 6
- Pages
- 741-752
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1968910000
- Cited by
- 728
- References
- 59
- Citations by year
- 2026: 11 · 2025: 18 · 2024: 10 · 2023: 17 · 2022: 20 · 2021: 14 · 2020: 19 · 2019: 19 · 2018: 25 · 2017: 24 · 2016: 29 · 2015: 23 · 2014: 30 · 2013: 27 · 2012: 32
- FWCI
- 10.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- CREB, CBP, KIX domain, transactivation domain, transcriptional coactivator, protein-protein interaction, amphipathic helix, hydrophobic groove, transcriptional activation, solution structure
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Phosphopeptides, Protein Conformation, Transcription Factors, Trans-Activators, Consensus Sequence, Sequence Alignment, Cyclic AMP Response Element-Binding Protein, Sequence Homology, Amino Acid, Protein Structure, Secondary, Nuclear Magnetic Resonance, Biomolecular, CREB-Binding Protein
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review