X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA
Open accessAbstract
X-ray structures of the basic/helix-loop-helix/leucine zipper (bHLHZ) domains of Myc-Max and Mad-Max heterodimers bound to their common DNA target (Enhancer or E box hexanucleotide, 5'-CACGTG-3') have been determined at 1.9 A and 2.0 A resolution, respectively. E box recognition by these two structurally similar transcription factor pairs determines whether a cell will divide and proliferate (Myc-Max) or differentiate and become quiescent (Mad-Max). Deregulation of Myc has been implicated in the development of many human cancers, including Burkitt's lymphoma, neuroblastomas, and small cell lung cancers. Both quasisymmetric heterodimers resemble the symmetric Max homodimer, albeit with marked structural differences in the coiled-coil leucine zipper regions that explain preferential homo- and heteromeric dimerization of these three evolutionarily related DNA-binding proteins. The Myc-Max heterodimer, but not its Mad-Max counterpart, dimerizes to form a bivalent heterotetramer, which explains how Myc can upregulate expression of genes with promoters bearing widely separated E boxes.
Integrity signals
Registry
Cites
Statistics
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?
The Myc/Max family DNA-binding site (E-box, 5'-CACGTG-3') encompasses the core sequence 5'-CGTG-3', which is also present in the HIF-1 consensus sequence and is part of the sequence specificity of NSC-13502.
“One example is the Myc/ Max family of transcription factors, whose DNA-binding site (E-box, 5V-CACGTG-3V; ref. 46) encompasses the core sequence 5V-CGTG-3V, which is also present in the HIF-1 consensus sequence and is part of the sequence specificity of NSC-13502.”
From Echinomycin, a small-molecule inhibitor of hypoxia-inducible factor-1 DNA-binding activity. (2005) · cites this paper as [46]
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · see citing works
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,253 · see citing works
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941 · see citing works
X-PLOR Version 3.1: A System for X-ray Crystallography and NMR
Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424 · see citing works
Raster3D Version 2.0. A program for photorealistic molecular graphics
Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,531 · see citing works
Dalla‐Favera, R., Bregni, M., Erikson, J., Patterson, D., Gallo, R. C., & Croce, C. M. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.24.7824 · Cited by 1,764 · see citing works
Max: A Helix-Loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-Binding Complex with Myc
Blackwood, E. M., & Eisenman, R. N. (1991) · Science · doi:10.1126/science.2006410 · Cited by 1,681 · see citing works
X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil
O’Shea, E. K., Klemm, J. D., Kim, P. S., & Alber, T. (1991) · Science · doi:10.1126/science.1948029 · Cited by 1,442 · see citing works
Taub, R. A., Kirsch, I. R., Morton, C. C., Lenoir, G., Swan, D., Tronick, S. R., Aaronson, S. A., & Leder, P. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.24.7837 · Cited by 1,421 · see citing works
Structural basis of water-specific transport through the AQP1 water channel
Sui, H., Han, B.-G., Lee, J. K., Walian, P., & Jap, B. K. (2001) · Nature · doi:10.1038/414872a · Cited by 1,166 · see citing works
MYC oncogenes and human neoplastic disease
Nesbit, C. E., Tersak, J. M., & Prochownik, E. V. (1999) · Oncogene · doi:10.1038/sj.onc.1202746 · Cited by 1,163 · see citing works
c-Myc transactivation of <i>LDH-A</i> : Implications for tumor metabolism and growth
Shim, H., Dolde, C., Lewis, B. C., Wu, C.-S., Dang, G., Jungmann, R. A., Dalla-Favera, R., & Dang, C. V. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6658 · Cited by 1,092 · see citing works
Ellenberger, T. E., Brandl, C. J., Struhl, K., & Harrison, S. C. (1992) · Cell · doi:10.1016/s0092-8674(05)80070-4 · Cited by 972 · see citing works
Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression
Laherty, C. D., Yang, W., Sun, J.-M., Davie, J., Seto, E., & Eisenman, R. N. (1997) · Cell · doi:10.1016/s0092-8674(00)80215-9 · Cited by 933 · see citing works
Coller, H. A., Grandori, C., Tamayo, P., Colbert, T., Lander, E. S., Eisenman, R. N., & Golub, T. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3260 · Cited by 823 · see citing works
Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
Zervos, A. S., Gyuris, J., & Brent, R. (1993) · Cell · doi:10.1016/0092-8674(93)90662-a · Cited by 769 · see citing works
Histone Deacetylase Activity Is Required for Full Transcriptional Repression by mSin3A
Hassig, C. A., Fleischer, T. C., Billin, A. N., Schreiber, S. L., & Ayer, D. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80214-7 · Cited by 740 · see citing works
Transposition and amplification of oncogene-related sequences in human neuroblastomas
Kohl, N. E., Kanda, N., Schreck, R. R., Bruns, G. A. P., Latt, S. A., Gilbert, F., & Alt, F. W. (1983) · Cell · doi:10.1016/0092-8674(83)90169-1 · Cited by 729 · see citing works
Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
Ferré-D’Amaré, A. R., Prendergast, G. C., Ziff, E. B., & Burley, S. K. (1993) · Nature · doi:10.1038/363038a0 · Cited by 719 · see citing works
Self-citationMad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
Ayer, D. E., Kretzner, L., & Eisenman, R. N. (1993) · Cell · doi:10.1016/0092-8674(93)90661-9 · Cited by 697 · see citing works
L-myc, a new myc-related gene amplified and expressed in human small cell lung cancer
Nau, M. M., Brooks, B. J., Battey, J. F., Sausville, E. A., Gazdar, A. F., Kirsch, I. R., McBride, O. W., Bertness, V. L., Hollis, G. F., & Minna, J. D. (1985) · Nature · doi:10.1038/318069a0 · Cited by 649 · see citing works
Ayer, D. E., Lawrence, Q., & Eisenman, R. N. (1995) · Cell · doi:10.1016/0092-8674(95)90355-0 · Cited by 587 · see citing works
The MYC protein activates transcription of the alpha‐prothymosin gene.
Eilers, M., Schirm, S., & Bishop, J. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07929.x · Cited by 571 · see citing works
Prendergast, G. C., Lawe, D., & Ziff, E. B. (1991) · Cell · doi:10.1016/0092-8674(91)90457-a · Cited by 558 · see citing works
The enhanceosome and transcriptional synergy.
Carey, M. (1998) · Cell · doi:10.1016/s0092-8674(00)80893-4 · Cited by 553 · see citing works
The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc
McMahon, S. B., Wood, M. A., & Cole, M. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.2.556-562.2000 · Cited by 494 · see citing works
Function of the c-Myc Oncogenic Transcription Factor
Dang, C. V., Resar, L. M. S., Emison, E. S., Kim, S., Li, Q., Prescott, J. E., Wonsey, D. R., & Zeller, K. I. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4686 · Cited by 377 · see citing works
Schreiber‐Agus, N., Chin, L., Chen, K., Torres, R., Rao, G., Guida, P. M., Skoultchi, A. I., & DePinho, R. A. (1995) · Cell · doi:10.1016/0092-8674(95)90356-9 · Cited by 361 · see citing works
An alternative pathway for gene regulation by Myc
Peukert, K., Staller, P., Schneider, A., Carmichael, G., Hänel, F., & Eilers, M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5672 · Cited by 359 · see citing works
Merika, M., & Thanos, D. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00180-5 · Cited by 353 · see citing works
Liao, D. J., & Dickson, R. B. (2000) · Endocrine Related Cancer · doi:10.1677/erc.0.0070143 · Cited by 345 · see citing works
Somers, W., Stahl, M., & Seehra, J. (1997) · EMBO Journal · doi:10.1093/emboj/16.5.989 · Cited by 320 · see citing works
The Myc oncoprotein: a critical evaluation of transactivation and target gene regulation
Cole, M. D., & McMahon, S. B. (1999) · Oncogene · doi:10.1038/sj.onc.1202748 · Cited by 314 · see citing works
Chromosome localization in normal human cells and neuroblastomas of a gene related to c-myc
Schwab, M., VARMUS, H. E., Bishop, J. M., Grzeschik, K., Naylor, S. L., Sakaguchi, A. Y., Brodeur, G. M., & Trent, J. M. (1984) · Nature · doi:10.1038/308288a0 · Cited by 313 · see citing works
Nucleotide sequence of cloned cDNA of human c-myc oncogene
Watt, R. A., Stanton, L. W., Marcu, K. B., et al. (1983) · Nature · doi:10.1038/303725a0 · Cited by 307 · see citing works
Grandori, C. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01025-6 · Cited by 285 · see citing works
BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells
Wang, Q., Zhang, H., Kajino, K., & Greene, M. I. (1998) · Oncogene · doi:10.1038/sj.onc.1202403 · Cited by 243 · see citing works
The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors.
Hill, C. P., Osslund, T. D., & Eisenberg, D. S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5167 · Cited by 224 · see citing works
Grandori, C., Mac, J., Siebelt, F., Ayer, D. E., & Eisenman, R. N. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00808.x · Cited by 208 · see citing works
Specific versus non-specific contacts in protein crystals
Janin, J. (1997) · Nature Structural Biology · doi:10.1038/nsb1297-973 · Cited by 206 · see citing works
Transcriptional activation by Myc is under negative control by the transcription factor AP‐2.
Gaubatz, S., Imhof, A., Dosch, R., Werner, O., Mitchell, P. J., Buettner, R., & Eilers, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07137.x · Cited by 197 · see citing works
Dang, C. V., McGuire, M., Buckmire, M., & Lee, W. M. F. (1989) · Nature · doi:10.1038/337664a0 · Cited by 193 · see citing works
New Myc-interacting proteins: a second Myc network emerges
Sakamuro, D., & Prendergast, G. C. (1999) · Oncogene · doi:10.1038/sj.onc.1202725 · Cited by 178 · see citing works
Brownlie, P. D., Ceska, T. A., Lamers, M. H., Romier, C., Stier, G., Teo, H., & Suck, D. (1997) · Structure · doi:10.1016/s0969-2126(97)00207-4 · Cited by 169 · see citing works
Dang, C. V., Dolde, C. E., Gillison, M. L., & Kato, G. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.2.599 · Cited by 159 · see citing works
Mechanism of c-Myb–C/EBPβ Cooperation from Separated Sites on a Promoter
Tahirov, T. H., Sato, K., Ichikawa-Iwata, E., Sasaki, M., Inoue-Bungo, T., Shiina, M., Kimura, K., Takata, S., Fujikawa, A., Morii, H., et al. (2002) · Cell · doi:10.1016/s0092-8674(01)00636-5 · Cited by 158 · see citing works
Larsson, L., Pettersson, M., Oberg, F. G., Nilsson, K., & Lüscher, B. (1994) · PubMed · Cited by 158 · see citing works
Sheiness, D. K., Fanshier, L., & Bishop, J. M. (1978) · Journal of Virology · doi:10.1128/jvi.28.2.600-610.1978 · Cited by 155 · see citing works
Gene-target recognition among members of the Myc superfamily and implications for oncogenesis
O’Hagan, R. C., Schreiber‐Agus, N., Chen, K., et al. (2000) · Nature Genetics · doi:10.1038/72761 · Cited by 137 · see citing works
Tra1p Is a Component of the Yeast Ada·Spt Transcriptional Regulatory Complexes
Saleh, A., Schieltz, D. M., Ting, N. S. Y., McMahon, S. B., Litchfield, D. W., Yates, J. R., Lees‐Miller, S. P., Cole, M. D., & Brandl, C. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26559 · Cited by 133 · see citing works
Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 å resolution
PÁRRAGA, A., Bellsolell, L., Ferré-D’Amaré, A. R., & Burley, S. K. (1998) · Structure · doi:10.1016/s0969-2126(98)00067-7 · Cited by 126 · see citing works
Self-citationWatson, D., Psallidopoulos, M. C., Samuel, K. P., Dalla‐Favera, R., & Papas, T. S. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.12.3642 · Cited by 123 · see citing works
Nekludova, L., & Pabo, C. O. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.6948 · Cited by 103 · see citing works
Isolation and characterization of Nmi, a novel partner of Myc proteins.
Bao, J., & As, Z. (1996) · PubMed · Cited by 99 · see citing works
Baca, M., Muir, T. W., Schnoelzer, M., et al. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00112a003 · Cited by 96 · see citing works
Myc/Max and other helix-loop-helix/leucine zipper proteins bend DNA toward the minor groove.
Fisher, D. E., Parent, L. A., & Sharp, P. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11779 · Cited by 77 · see citing works
Jp, M., Dc, H., Littlewood, T. D., & Evan, G. I. (1987) · PubMed · Cited by 76 · see citing works
Control of Cell Proliferation by Myc Family Genes
Eilers, M. (1999) · Molecules and Cells · doi:10.1016/s1016-8478(23)13499-6 · Cited by 60 · see citing works
The Mad Protein Family Links Transcriptional Repression to Cell DifferentiationPreprint
McArthur, G. A., Laherty, C. D., Quéva, C., Hurlin, P. J., Loo, L. W. M., JAMES, L., Grandori, C., Gallant, P., Shiio, Y., Hokanson, W., et al. (1998) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1998.63.423 · Cited by 58 · see citing works
Hurlin, P. J., Ayer, D. E., Grandori, C., & Eisenman, R. N. (1994) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1994.059.01.014 · Cited by 56 · see citing works
Brain tumours and lymphomas in transgenic mice that carry HTLV-I LTR/c-myc and Ig/tax genes.
Benvenisty, N., Ornitz, D. M., Bennett, G. L., Sahagan, B. G., Kuo, A. C., Cardiff, R. D., & Leder, P. (1992) · PubMed · Cited by 53 · see citing works
Determination of Copy Number of c-Myc Protein per Cell by Quantitative Western Blotting
Rudolph, C., Adam, G., & Simm, A. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.3095 · Cited by 53 · see citing works
Larsson, L.-G., Bahram, F., Burkhardt, H., et al. (1997) · Oncogene · doi:10.1038/sj.onc.1201390 · Cited by 43 · see citing works
Transcriptional Activities of the Myc and Max Proteins in Mammalian Cells
Kretzner, L., Blackwood, E. M., & Eisenman, R. N. (1992) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-77633-5_55 · Cited by 42 · see citing works
Rapid identification of key amino-acid–DNA contacts through combinatorial peptide synthesis
Winston, R. L., & Gottesfeld, J. M. (2000) · Chemistry & Biology · doi:10.1016/s1074-5521(00)00099-5 · Cited by 35 · see citing works
Robinson, R., Grey, L., Staunton, D., Vankelecom, H., Vernallis, A., Moreau, J., Stuart, D., Heath, J. K., & Jones, E. (1994) · Cell · doi:10.1016/0092-8674(94)90449-9
Flagged first, then by citations
Cited by
Sorted by citations
Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390 · see citing works
Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · see citing works
Pioneer Transcription Factors Target Partial DNA Motifs on Nucleosomes to Initiate Reprogramming
Soufi, A., Garcia, M. F., Jaroszewicz, A., Osman, N., Pellegrini, M., & Zaret, K. S. (2015) · Cell · doi:10.1016/j.cell.2015.03.017 · Cited by 780 · see citing works
MYC: Connecting selective transcriptional control to global RNA production
Kress, T. R., Sabò, A., & Amati, B. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3984 · Cited by 521 · see citing works
Echinomycin, a small-molecule inhibitor of hypoxia-inducible factor-1 DNA-binding activity.
Kong, D., Park, E. J., Stephen, A. G., Calvani, M., Cardellina, J. H., Monks, A., Fisher, R. J., Shoemaker, R. H., & Melillo, G. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1235 · Cited by 508 · see citing works
An Overview of MYC and Its Interactome
Conacci-Sorrell, M., McFerrin, L., & Eisenman, R. N. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014357 · Cited by 408 · see citing works
Target gene-independent functions of MYC oncoproteins
Baluapuri, A., Wolf, E., & Eilers, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0215-2 · Cited by 310 · see citing works
The MYC transcription factor network: balancing metabolism, proliferation and oncogenesis
Carroll, P. A., Freie, B. W., Mathsyaraja, H., & Eisenman, R. N. (2018) · Frontiers of Medicine · doi:10.1007/s11684-018-0650-z · Cited by 289 · see citing works
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288 · see citing works
Carabet, L. A., Rennie, P. S., & Cherkasov, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010120 · Cited by 172 · see citing works
“Ten years later, the X-ray structures of Myc-Max (PDB ID: 1NKP) and Mad-Max heterodimers (PDB ID: 1NLW) were resolved, re-enforcing the secondary structure composition of the Max homodimer [75].”
BackgroundMethodInfluentialStabilization of the Max Homodimer with a Small Molecule Attenuates Myc-Driven Transcription
Struntz, N. B., Chen, A., Deutzmann, A., Wilson, R. M., Stefan, E., Evans, H. L., Ramirez, M. A., Liang, T., Caballero, F., Wildschut, M. H. E., et al. (2019) · Cell Chemical Biology · doi:10.1016/j.chembiol.2019.02.009 · Cited by 130 · see citing works
Jung, L. A., Gebhardt, A., Koelmel, W., Ade, C. P., Walz, S., Kuper, J., von Eyss, B., Letschert, S., Redel, C., d'Artista, L., et al. (2017) · Oncogene · doi:10.1038/onc.2016.354 · Cited by 101 · see citing works
Stabilizers of the Max Homodimer Identified in Virtual Ligand Screening Inhibit Myc Function
Jiang, H., Bower, K. E., Beuscher, A. E., Zhou, B., Bobkov, A. A., Olson, A. J., & Vogt, P. K. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.054858 · Cited by 62 · see citing works
Small-molecule perturbation of competing interactions between c-Myc and Max
Follis, A. V., Hammoudeh, D. I., Daab, A. T., & Metallo, S. J. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.12.025 · Cited by 60 · see citing works
Direct inhibition of c-Myc-Max heterodimers by celastrol and celastrol-inspired triterpenoids
Wang, H., Teriete, P., Hu, A., Raveendra-Panickar, D., Pendelton, K., Lazo, J. S., Eiseman, J., Holien, T., Misund, K., Oliynyk, G., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6116 · Cited by 53 · see citing works
Formation of a structurally-stable conformation by the intrinsically disordered MYC:TRRAP complex
Feris, E. J., Hinds, J. W., & Cole, M. D. (2019) · PLOS ONE · doi:10.1371/journal.pone.0225784 · Cited by 29 · see citing works
Yao, R., Zhang, M., Zhou, J., Liu, L., Zhang, Y., Gao, J., & Xu, K. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00868-6 · Cited by 32 · see citing works
Gao, J., Wang, Y., Li, K., Zhang, J., & Geng, X. (2022) · Journal of Molecular Modeling · doi:10.1007/s00894-022-05082-2 · Cited by 6 · see citing works
- Authors
- Nair, S. K., & Burley, S. K.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Burley, Stephen K.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-01
- Volume
- 112
- Issue
- 2
- Pages
- 193-205
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2104538433
- Cited by
- 551
- References
- 70
- Citations by year
- 2026: 21 · 2025: 34 · 2024: 37 · 2023: 38 · 2022: 28 · 2021: 31 · 2020: 22 · 2019: 33 · 2018: 24 · 2017: 27 · 2016: 13 · 2015: 25 · 2014: 33 · 2013: 20 · 2012: 25
- FWCI
- 7.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3850 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- Myc-Max heterodimer, bHLH-Zip transcription factors, Burkitt lymphoma, neuroblastoma, small cell lung cancer
- MeSH terms
- Amino Acid Sequence, Base Sequence, Crystallization, DNA, DNA-Binding Proteins, Gene Expression Regulation, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Repressor Proteins, Structure-Activity Relationship, Transcription Factors, Proto-Oncogene Proteins c-myc, Leucine Zippers, Crystallography, X-Ray, Dimerization, Protein Structure, Quaternary, E-Box Elements, Basic-Leucine Zipper Transcription Factors, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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