Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions

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

Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

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

Structure 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

A CBP Integrator Complex Mediates Transcriptional Activation and AP-1 Inhibition by Nuclear Receptors

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

The CBP co-activator is a histone acetyltransferase

Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,828

Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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

The Folding Pathway of the KIX Domain

Troilo, F., Bonetti, D., Toto, A., Visconti, L., Brunori, M., Longhi, S., & Gianni, S. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00289 · Cited by 6

Design and Biochemical Characterization of Peptidic Inhibitors of the Myb/p300 Interaction

Jones, M. D., Grosche, P., Floersheimer, A., André, J., Gattlen, R., Oser, D., Tinchant, J., Wille, R., Chie-Leon, B., Gerspacher, M., et al. (2023) · Biochemistry · doi:10.1021/acs.biochem.2c00690 · Cited by 6

Interplay Between Protein Order, Disorder and Oligomericity in Receptor Signaling

Sigalov, A. B. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0659-4_4 · Cited by 6

Structural biology of e1F4F: mRNA recognition and preparation in eukaryotic translation initiation

Marcotrigiano, J., & Burley, S. K. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)61007-1 · Cited by 6

Adenovirus DNA binding protein inhibits SrCap-activated CBP and CREB-mediated transcription

Xu, X., Tarakanova, V. L., Chrivia, J. C., & Yaciuk, P. (2003) · Virology · doi:10.1016/s0042-6822(03)00386-6 · Cited by 6

CREB-binding protein transcription activation domain for enhanced transgene expression by a positive feedback system

Kanda, G. N., Ochiai, H., Harashima, H., & Kamiya, H. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.09.016 · Cited by 6

KIXBASE: A comprehensive web resource for identification and exploration of KIX domains

Yadav, A., Thakur, J. K., & Yadav, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-14617-0 · Cited by 6

Order-disorder transition of intrinsically disordered kinase inducible transactivation domain of CREB

Liu, H., Guo, X. J., Han, J., Luo, R., & Chen, H. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5027869 · Cited by 6

A Cell‐Permeable Synthetic Transcription Factor Mimic

Xiao, X., Yu, P., Lim, H., Sikder, D. S., & Kodadek, T. J. (2007) · Angewandte Chemie · doi:10.1002/ange.200604485 · Cited by 6

Molecular Mechanisms of Transcription Factors with Dual Activator and Repressor Functions

Dong, J., & Guertin, M. J. (2026) · Molecular and Cellular Biology · doi:10.1080/10985549.2026.2619741 · Cited by 5

Revisiting allostery in CREB-binding protein (CBP) using residue-based interaction energy

Yazar, M., & Özbek, P. (2020) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-020-00316-y · Cited by 5

Genome-wide analysis of KIX gene family for organ size regulation in soybean (Glycine max L.)

Park, G. T., Moon, J., Park, S., Park, S.-K., Baek, J., & Seo, M. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1252016 · Cited by 5

Preparation of Phosphorylated Proteins for NMR Spectroscopy

Kumar, G. S., Page, R., & Peti, W. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.07.004 · Cited by 5

Landscape of intrinsically disordered proteins in mental disorder diseases

Zhang, X., Song, X., Hu, G., Yang, Y., Liu, R., Zhou, N., Basu, S., Qiao, D., & Hou, Q. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.10.043 · Cited by 4

Garcinolic Acid Distinguishes Between GACKIX Domains and Modulates Interaction Networks

Breen, M. E., Joy, S. T., Baruti, O. J., Beyersdorf, M. S., Henley, M. J., Salle, S. N. D., Ycas, P. D., Croskey, A., Cierpicki, T., Pomerantz, W. C. K., et al. (2023) · ChemBioChem · doi:10.1002/cbic.202300439 · Cited by 5

Molecular Simulations of Intrinsically Disordered Proteins and Their Binding Mechanisms

Chu, X., Nagpal, S., & Muñoz, V. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1716-8_19 · Cited by 4

Functional Analyses of Rare Germline Missense BRCA1 Variants Located within and outside Protein Domains with Known Functions

Hovland, H. N., Mchaina, E. K., Høberg‐Vetti, H., Ariansen, S. L., Sjursen, W., Ghelue, M. V., Haukanes, B. I., Knappskog, P. M., Aukrust, I., & Ognedal, E. (2023) · Genes · doi:10.3390/genes14020262 · Cited by 4

Characterizing the molecular architectures of chromatin-modifying complexes

Setiaputra, D., & Yip, C. K. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.06.018 · Cited by 4

Bringing the Signal into the Nucleus

Kramer, I. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394803-8.00007-3 · Cited by 4

De novo design of phosphorylation-induced protein switches for synthetic signaling in cellsPreprint

Buckley, S., Miao, Y., Idris, M., Lee, P., Scheller, L., Riek, R., Maerkl, S. J., Abriata, L. A., & Correia, B. E. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.10.675034 · Cited by 9

Recognition of two hydrophobic pockets in the KIX domain of CBP by FOXO4 transactivation domain

Heo, J., Ryu, K., & Park, C. (2025) · Communications Biology · doi:10.1038/s42003-025-09146-w · Cited by 3

6-Paradol mitigates rotenone-induced Parkinson’s disease via shutting TNFR-1/RIPK1/RIPK3/MLKL cascade and enhancement of PPARγ/PGC-1α/TFAM axis

Sirwi, A., Rabie, M. A., Koshak, A. E., Albadawi, D. A. I., Halawany, A. M. E., Ibrahim, S. R. M., Mohamed, G. A., Abdallah, H. M., & Sayed, N. S. E. (2025) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-025-00831-5 · Cited by 3

Breaking the CREB–CBP alliance: Progress, challenges, and therapeutic promise of small-molecule and peptide disruptors of the pKID–KIX interaction

Rudayni, H. A. (2025) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2025.110734 · Cited by 3

Generating intrinsically disordered protein conformational ensembles from a Markov chain

Cukier, R. I. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5010428 · Cited by 3

The interaction strength of an intrinsically disordered protein domain with its binding partner is little affected by very different cosolutes

Schnatwinkel, J., & Herrmann, C. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/d0cp03040f · Cited by 3

Metadynamics Simulations to Study the Structural Ensembles and Binding Processes of Intrinsically Disordered Proteins

Zhou, R., & Duan, M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1855-4_9 · Cited by 3

Cooperative folding as a molecular switch in an evolved antibody binder

Jönsson, M., Mushtaq, A. U., Nagy, T. M., von Witting, E., Löfblom, J., Nam, K., Wolf‐Watz, M., & Hober, S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107795 · Cited by 3

Bromodomains as Anticancer Targets

Filippakopoulos, P., & Knapp, S. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802208-5.00010-2 · Cited by 3

Structural Studies with Coactivators for the Estrogen Receptor

Yi, P., Wang, Z., & O’Malley, B. W. (2018) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-99350-8_4 · Cited by 3

ACTIVATION OF GENE EXPRESSION BY TRANSCRIPTION FACTORS

Latchman, D. S. (2008) · Elsevier eBooks · doi:10.1016/b978-012373983-4.50013-4 · Cited by 3

Binding Induced Intrinsically Disordered Protein Folding with Molecular Dynamics Simulation

Chen, H. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-94-017-9245-5_9 · Cited by 3

MORPHOGENESIS OF PROTEINS: CLASSIC VIEWS AND CHALLENGES AHEAD

Giri, R., Travaglini‐Allocatelli, C., Gianni, S., Giardina, G., & Brunori, M. (2013) · Journal of Proteins and Proteomics · Cited by 3

Multivalent and Bidirectional Binding of Transcriptional Transactivation Domains to the MED25 Coactivator

Jeffery, H. M., & Weinzierl, R. O. J. (2020) · Biomolecules · doi:10.3390/biom10091205 · Cited by 3

Computational Analysis of Modular Protein Architectures

Linding, R., Letunić, I., Gibson, T. J., & Peer Bork, B. (2008) · Protein Science Encyclopedia · doi:10.1002/9783527610754.sa11 · Cited by 3

Application of Reduced Models to Protein Structure Prediction

Skolnick, J., Koliński, A., & Ortíz, Á. R. (1999) · Theoretical and computational chemistry · doi:10.1016/s1380-7323(99)80086-7 · Cited by 3

The IFN I response in tumor cells is shaped by PARP7–p300/CBP interactions through distinct loss- and gain-of-function mechanismsPreprint

Siordia, I. R., Rieth, S., Morgan, R. K., Jeltema, D., Tullis, J., Orth, J., Yan, N., Marx, A., & Cohen, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.30.662483 · Cited by 4

Discovery of peptidomimetic inhibitors of CREB/CBP by targeting hydrophobic grooves on the surface of the CBP KIX domain

Huang, B., Gregory‐Lott, E., Li, B. X., Tran, T. H., Li, S., Xue, M., Wang, S., Asokan, A., Shen, N., Sun, X., et al. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.08.023 · Cited by 2

Exploring Helical Fraying Linked to Dynamics and Catalysis in Adenylate Kinase

Mattsson, J., Phoeurk, C., Schierholz, L., Mushtaq, A. U., Buitrago, J. A. R., Rogne, P., Sauer-Eriksson, A. E., & Wolf‐Watz, M. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00306 · Cited by 2

Biological Significance of Intrinsically Disordered Protein Structure

Sato, M. (2022) · Chem-Bio Informatics Journal · doi:10.1273/cbij.22.26 · Cited by 2

From Immunogenic Peptides to Intrinsically Disordered Proteins

Dyson, H. J., & Wright, P. E. (2023) · Israel Journal of Chemistry · doi:10.1002/ijch.202300051 · Cited by 2

Reassessing the folding of the KIX domain: Evidence for a two‐state mechanism

Morrone, A., Giri, R., Brunori, M., & Gianni, S. (2012) · Protein Science · doi:10.1002/pro.2159 · Cited by 2

Analysis of Phosphorylation-Dependent Protein-Protein Interactions Using a Bacterial Two-Hybrid System

Shaywitz, A. J., Dove, S. L., Greenberg, M. E., & Hochschild, A. (2002) · Science Signaling · doi:10.1126/scisignal.1422002pl11 · Cited by 2

Mapping Protein Folding Landscapes by NMR Relaxation

Wright, P. E., Felitsky, D. J., Sugase, K., & Dyson, H. J. (2009) · Biological and medical physics series · doi:10.1007/978-3-540-88787-4_1 · Cited by 2

[10] The yeast split-hybrid system

DeMaggio, A. J., Goodman, P., Shih, H.-M., Goodman, R. H., & Hoekstra, M. F. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)28395-x · Cited by 2

Mechanisms of Transcriptional Activation in Eukaryotes

Herrera, F. J., Shooltz, D. D., & Triezenberg, S. J. (2004) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-18932-6_1 · Cited by 2

Tandem association of CLOCK:BMAL1 complexes on DNA enables recruitment of CBP/p300 through multivalent interactionsPreprint

Sharma, D., Stoos, L., Torgrimson, M. R., Crosby, P., Franks, K. M., Parsley, N. C., Membreño, M. W., Kempf, G., Kater, L., Gustafson, C. L., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.04.674342 · Cited by 3

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

Usher, E. T., & Pelham, J. F. (2025) · FEBS Letters · doi:10.1002/1873-3468.70238 · Cited by 2

OX-LDL causes vascular endothelial injury by interfering with the CREB1-MDH1B-malate axis

Pu, C., Yang, H., Wang, G., Wang, X., Wan, X., Liu, Q., & Zhao, Y. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.12.051 · Cited by 1

Dormancy exit correlates with CREB1 reactivation that is a potential target to overcome endocrine therapy resistance in ER+ breast cancer cells

Duan, L., O'Hara, K. M., & Maki, C. G. (2026) · iScience · doi:10.1016/j.isci.2026.115610 · Cited by 1

Assessment of machine‐learning predictions for the Mediator complex subunit MED25 ACID domain interactions with transactivation domains

(2024) · doi:10.1002/1873-3468.14837 · Cited by 1

Functional protein oligomers

Sahoo, S., Balireddygari, L. R., Padhy, A. A., Kumari, S., Hegde, P., & Mishra, P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21809-5.00003-x · Cited by 1

Efficacy of independence sampling in replica exchange simulations of ordered and disordered proteins

Lee, K. H., & Chen, J. (2017) · Journal of Computational Chemistry · doi:10.1002/jcc.24923 · Cited by 1

A suite of bioassays to evaluate CREB inhibitors

Li, B. X., & Xiao, X. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.11.002 · Cited by 1

The LEF-1 high-mobility group box adopts residual structure in its DNA-free form

Alderson, T. R., Habacher, H., Bourgeois, B. M. R., & Madl, T. (2022) · Journal of Magnetic Resonance Open · doi:10.1016/j.jmro.2022.100074 · Cited by 1

Exploring the mechanisms of protein foldingPreprint

Xu, J., Han, M., Ren, Y., & Li, J. (2013) · arXiv (Cornell University) · doi:10.48550/arxiv.1307.4147 · Cited by 1

Characterization of the Dynamic Interactions of Transcriptional Activators

Wands, A. M. (2010) · Deep Blue (University of Michigan) · Cited by 1

Evolution of Conditional Cooperativity Between HOXA11 and FOXO1 Through Allosteric RegulationPreprint

Nnamani, M. C., Ganguly, S., Lynch, V. J., Mizoue, L. S., Tong, Y., Darling, H. L., Fuxreiter, M., Meiler, J., & Wagner, G. P. (2015) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/014381 · Cited by 1

The Split-Hybrid System: Uncoding Multiprotein Networks and Defining Mutations That Affect Protein Interactions

Goldman, P. S., DeMaggio, A. J., Goodman, R. H., & Hoekstra, M. F. (2003) · Humana Press eBooks · doi:10.1385/1-59259-210-4:261 · Cited by 1

Histone acetyltransferase activity of CREB-binding protein is essential for synaptic plasticity in LymnaeaPreprint

Hatakeyama, D., Sunada, H., Totani, Y., Watanabe, T., Felletár, I., Fitchett, A., Eravci, M., Anagnostopoulou, A., Miki, R., Kuzuhara, T., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.26.445902 · Cited by 1

Examining the effect of CBP on the E2A-PBX1 and HOXB4 interaction

Menezes, S. C. (2008)

Transcriptional Regulation via the cAMP Responsive Activator CREB

Montminy, M., & Du, K. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50649-5

Investigação molecular por sequenciamento do gene CBP em portadores da síndrome de Rubinstein-Taybi

Suzuki, K. T. (2012) · doi:10.11606/d.5.2012.tde-24052012-154642

Análisis genético de la percepción del ácido salicílico en Arabidopsis thaliana. Caracterización de NRB4

Canet, J. V. (2012) · doi:10.4995/thesis/10251/16962

NMR solution structure of the Set2 SRI domain and preparation of RNA polymerase II complexes with the elongation factor Spt4-Spt5

Vojnic, E. (2006) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.6976

Molecular Dynamic Studies of Nuclear Receptors Ligand Binding Domain

Burendahl, S. (2009) · Figshare

Structural and functional characterization of villin domain 6 and supervillin N-terminal fragments

Fedetchkine, S. (2020) · Western CEDAR (Western Washington University) · doi:10.25710/50xt-z035

El papel de las células dendríticas en la respuesta a patrones moleculares de la pared de hongos y a la sobrecarga de células apoptóticas

Gil, E. B. H. (2013) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/3011

Modulating Transcription with Artificial Regulators

Mapp, A. K., Ansari, A. Z., Wu, Z., & Lü, Z. (2004) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-18932-6_18

Role of basic region leucine zipper transcription factors in controlling gene transcription in mammalian cells

Alsarraj, J. (2006) · Publications of the UdS (Saarland University) · doi:10.22028/d291-20748

Profile of Marc R. Montminy

Zeliadt, N. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205291109

Structure Analysis of Biological Macromolecule in Solution by Neutron Scattering

Mamoru, S. A. T. O. (2010) · RADIOISOTOPES · doi:10.3769/radioisotopes.59.405

A REVIEW OF NUCLEAR RECEPTOR GENE ACTIVATION THROUGH COFACTOR PROTEIN INTERACTIONS

Baker, R. L. (2008) · KU ScholarWorks (The University of Kansas)

Construction of a Database of Secondary Structure Segments and Short Regions of Disorder and Analysis of Their Properties

Zhang, Y. (2004)

Visualizing CREB family transcription factor activation in living cells

Friedrich, M. (2007) · doi:10.5282/edoc.7069

Structural and functional studies on the pituitary-specific transcription factor Pit-1

Augustijn, K. D. (2002) · Utrecht University Repository (Utrecht University)

Using Small Molecules to Inhibit an E2APBX1:CBP In teraction Involved in Acute Lymphoblastic Leukemia

Purvis, A. D. (2009)

Evaluation of the Mechanisms of Gene Regulation on the Chromatin Level at the Example of Human Hyaluronan Synthase 2 and Cyclin C Genes

Saavalainen, K. (2007)

Understanding the functional significance of intrinsically disordered regions in proteins using computational methods

Singh, G. P. (2009) · INFLIBNET

Molecular Recognition of Intrinsically Disordered Proteins Studied by All-Atom Molecular Simulation

Higo, J., & Umezawa, K. (2014) · Seibutsu Butsuri · doi:10.2142/biophys.54.096

Activity-dependent gene regulation in neurons: energy coupling and a novel biosensor

Li, Z. (2015) · OpenBU (Boston University) · Cited by 1

How do Proteins Work

Dyson, H. (2007)

CBP/p300 Recruitment Signaling Activates Ets-1 and Ets-2 by Ras/Mitogen-Activated Protein Kinase

Graves, B. J., Foulds, C. E., Nelson, M. L., & Blaszczak, A. G. (2014)

The CREB Coactivator dTORC is Required for Metabolic Stress Resistance and Maintenance of Cardiac Function in Drosophila

Goode, J. (2010) · eScholarship (California Digital Library)

The role of neural cell adhesion molecule in melanoma progression and mesenchymal stromal cells migration

Shi, Y. (2013) · doi:10.32657/10356/53512

Elucidation of the physical and functional interactions between the MEIS1A and the CREB and CRTC transcription factors

Looi, Y. (2012) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/50694

Stress-induced non-coding RNAs allosterically regulate TLS, a HAT-inhibitory RNA binding protein, to mediate transcriptional repression

Wang, X. (2007) · eScholarship (California Digital Library)

Probing the Role of Nascent Helicity in Protein Function: p27kip1 as a Regulator of the Cell Cycle

Otieno, S. B. (2007) · doi:10.21007/etd.cghs.2007.0231

Activation of Gene Expression by Transcription Factors

Latchman, D. S. (2004) · Elsevier eBooks · doi:10.1016/b978-012437178-1/50011-4

Convergent organization of aberrant MYB complex controls oncogenic gene expression in acute myeloid leukemiaPreprint

Takao, S., Forbes, L., Uni, M., Cheng, S., Pineda, J. M. B., Tarumoto, Y., Cifani, P., Minuesa, G., Chen, C., Kharas, M. G., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.05.077156

Investigating phase separation mechanisms for transcriptional control

Boehning, M. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8312

Mapping the Promiscuous Binding Interface of HOX-A11 with KIX by Experimentally Guided in-silico dockingPreprint

Ganguly, S., Wagner, G. P., & Meiler, J. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.11.426190

Direct recruitment of BCOR by AF9 forms a fuzzy complex required for MLL-AF9 leukemogenesis

Schmidt, C. (2017) · doi:10.18130/v3p55dg3t

CREB Binding Protein—Coactivator Complexes

Kurokawa, R., & Glass, C. K. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-032-2_23

Faculty Opinions recommendation of Metformin and insulin suppress hepatic gluconeogenesis through phosphorylation of CREB binding protein.

Rosenzweig, S. A. (2009) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1159871.621299

References

(2009) · Chapman & Hall/CRC eBooks · doi:10.1201/9781420078930.bmatt

References

(2012) · Wiley eBooks · doi:10.1002/9783527644506.refs

Structural insights into Arginine-Serine rich proteins and N-H spin-spin coupling constants

Xiang, S. (2013) · doi:10.53846/goediss-4157

Faculty Opinions recommendation of Binding-induced folding of a natively unstructured transcription factor.

Fiser, A. (2008) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1108390.565132

Paper Alert

Liddington, R., & Frederick, C. (1998) · Structure · doi:10.1016/s0969-2126(98)00026-4

Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions

Beltrão, P., & Serrano, L. G. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0010026.eor

Transcriptional Activator−Coactivator Recognition: Nascent Folding of a Kinase-Inducible Transactivation Domain Predicts Its Structure on Coactivator Binding

Hua, Q. X., Jia, W.-H., Bullock, B. P., Habener, J. F., & Weiss, M. A. (1998) · Biochemistry · doi:10.1021/bi9800808 · Cited by 92

Roles of Phosphorylation and Helix Propensity in the Binding of the KIX Domain of CREB-binding Protein by Constitutive (c-Myb) and Inducible (CREB) Activators

Zor, T., Mayr, B. M., Dyson, H. J., Montminy, M., & Wright, P. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207361200 · Cited by 169

Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: implications for mapping the boundaries of structural domains

Radhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M., & Wright, P. E. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2658 · Cited by 73

Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of c-Myb

Zor, T., Guzman, R. N. D., Dyson, H. J., & Wright, P. E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.038 · Cited by 209

Magnitude of the CREB-Dependent Transcriptional Response Is Determined by the Strength of the Interaction between the Kinase-Inducible Domain of CREB and the KIX Domain of CREB-Binding Protein

Michael, & Greenberg, E. (2000)