The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation
Abstract
A 60 amino acid domain of the myogenic determination gene MyoD is necessary and sufficient for sequence-specific DNA binding in vitro and myogenic conversion of transfected C3H10T1/2 cells. We show that a highly basic region, immediately upstream of the helix-loop-helix (HLH) oligomerization motif, is required for MyoD DNA binding in vitro. Replacing helix1, helix2, or the loop of MyoD with the analogous sequence of the Drosophila T4 achaete-scute protein (required for peripheral neurogenesis) has no substantial effect on DNA binding in vitro or muscle-specific gene activation in transfected C3H10T1/2 cells. However, replacing the basic region of MyoD with the analogous sequence of other HLH proteins (the immunoglobulin enhancer binding E12 protein or T4 achaete scute protein) allows DNA binding in vitro, yet abolishes muscle-specific gene activation. These findings suggest that a recognition code that determines muscle-specific gene activation lies within the MyoD basic region and that the capacity for specific DNA binding is insufficient to activate the muscle program.
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In the citing paper
“Mutation analysis has shown that the amino acids A114, T115, and K124 of mouse MyoD1 are crucial for myogenic activity.”
From Evolutionary aspects of developmentally regulated helix-loop-helix transcription factors in striated muscle of jellyfish (2003) · cites this paper as Davis et al., 1990
In the citing paper
“Remarkably, placing the corresponding amino acid residues from MyoD1 into its dimerization partner E-12 produces a protein that functions as myogenic activator”
From Evolutionary aspects of developmentally regulated helix-loop-helix transcription factors in striated muscle of jellyfish (2003) · cites this paper as Davis et al., 1990
In the citing paper
“JellyD1 contains two of the crucial amino acids needed for myogenic activity”
From Evolutionary aspects of developmentally regulated helix-loop-helix transcription factors in striated muscle of jellyfish (2003) · cites this paper as Davis et al., 1990
Citations
Cites
Recombinant Genomes Which Express Chloramphenicol Acetyltransferase in Mammalian Cells
Gorman, C., Moffat, L. F., & Howard, B. H. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.9.1044 · Cited by 7,674
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Expression of a single transfected cDNA converts fibroblasts to myoblasts
Davis, R. L., Weintraub, H. M., & Lassar, A. B. (1987) · Cell · doi:10.1016/0092-8674(87)90585-x · Cited by 3,388
Self-citationPrediction of protein conformation
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a002 · Cited by 3,309
Murre, C., Page-McCaw, P., & Baltimore, D. (1989) · Cell · doi:10.1016/0092-8674(89)90682-x · Cited by 2,713
Chamberlain, J. P. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90716-4 · Cited by 1,970
How eukaryotic transcriptional activators work
Ptashne, M. (1988) · Nature · doi:10.1038/335683a0 · Cited by 1,828
Murre, C., Page-McCaw, P., Vaessin, H., Caudy, M. A., Jan, L. Y., Jan, Y. N., Cabrera, C. V., Buskin, J. N., Hauschka, S. D., Lassar, A. B., et al. (1989) · Cell · doi:10.1016/0092-8674(89)90434-0 · Cited by 1,815
Self-citationAmino Acid Preferences for Specific Locations at the Ends of α Helices
Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364
DNA-mediated transfer of the adenine phosphoribosyltransferase locus into mammalian cells.
Wigler, M. H., Pellicer, À., Silverstein, S. J., Axel, R., Urlaub, G., & Chasin, L. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.3.1373 · Cited by 1,278
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Hoshijima, K., Kohyama‐Koganeya, A., Watakabe, I., Inoue, K., Sakamoto, H., & Shimura, Y. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.17.3441 · Cited by 27
Shirakata, M., & Paterson, B. M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07165.x · Cited by 27
Heme oxygenase—regulation of and physiological implication in heme catabolism
Shibahara, S. (1994) · Stem Cells · doi:10.1002/stem.5530120713 · Cited by 27
Kinney, W. R., McNamara, R. K., Valcourt, E. G., & Routtenberg, A. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(95)00287-3 · Cited by 27
Qasba, P., Lin, E. H., Zhou, M., Kumar, A., & Siddiqui, M. A. Q. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.1107 · Cited by 27
Alternative multimeric structures affect myogenin DNA binding activity.
Farmer, K., Catala, F., & Wright, W. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42812-8 · Cited by 27
Diagnostic utility of oncogenes and their products in human cancer
McKenzie, S. J. (1991) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(91)90014-c · Cited by 27
Reprogramming to a muscle fate by fusion recapitulates differentiation
Pomerantz, J. H., Mukherjee, S., Palermo, A. T., & Blau, H. M. (2009) · Journal of Cell Science · doi:10.1242/jcs.041376 · Cited by 26
The Id proteins: targets for inhibiting tumor cells and their blood supply
Benezra, R. (2001) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(01)00028-2 · Cited by 26
Physical and Functional Interactions between the Transcriptional Inhibitors Id3 and ITF-2b
Chen, B., & Lim, R. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2459 · Cited by 26
Klamut, H. J., Bosnoyan-Collins, L., Worton, R. G., & Ray, P. N. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.8.1618 · Cited by 26
Zhou, Y., Liu, Y., Jiang, X., Du, H., Li, X., & Zhu, Q. C. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9838-2 · Cited by 25
Dehydrocorydaline promotes myogenic differentiation via p38 MAPK activation
Yoo, M., Lee, S., Kim, Y. K., Seo, D. W., Baek, N., Ryu, J., Kang, J., & Bae, G. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5653 · Cited by 25
Louis, M., Holm, L., Sánchez, L., & Kaufman, M. (2003) · Genetics · doi:10.1093/genetics/165.3.1355 · Cited by 25
Dowell, S. J., Tsang, J. S. H., & Mellor, J. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.16.4229 · Cited by 25
Peleg, Y., & Metzenberg, R. L. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.7816 · Cited by 24
Yamane, A., Mayo, M. L., Bringas, P., Chen, L., Huynh, M., Thai, K., Shum, L., & Slavkin, H. C. (1997) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199708)209:4 · Cited by 24
Determinants of Helix-Loop-Helix Dimerization Affinity
Goldfarb, A. N., Lewandowska, K., & Shoham, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2683 · Cited by 24
Foreman, P. K., & Davis, R. W. (1993) · Genetics · doi:10.1093/genetics/135.2.287 · Cited by 24
Self-citationShimizu‐Nishikawa, K., Tazawa, I., Uchiyama, K., & Yoshizato, K. (1999) · Development Growth & Differentiation · doi:10.1046/j.1440-169x.1999.00477.x · Cited by 24
Expression of Id2 and Id3 mRNA in human lymphocytes
Ishiguro, A., Spirin, K. S., Shiohara, M., Tobler, A., Norton, J. D., Rigolet, M., Shimbo, T., & Koeffler, H. P. (1995) · Leukemia Research · doi:10.1016/0145-2126(95)00084-4 · Cited by 24
Robinson, G. L., Cordle, S. R., Henderson, E., Weil, P. A., Teitelman, G., & Stein, R. W. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6704 · Cited by 24
Wong, M. V., Jiang, S., Palasingam, P., & Kolatkar, P. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048591 · Cited by 23
Lin, H., & Konieczny, S. F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42899-2 · Cited by 23
8 Developmental Regulation of Sarcomeric Gene Expression
Ordahl, C. P. (1992) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)60444-5 · Cited by 23
Multiple positive and negative elements regulate human brain creatine kinase gene expression
Ritchie, M. E., Trask, R. V., Fontanet, H. L., & Billadello, J. J. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.22.6231 · Cited by 23
Wang, C., Wang, M., Arrington, J. V., Shan, T., Yue, F., Nie, Y., Tao, W. A., & Kuang, S. (2016) · Development · doi:10.1242/dev.138099 · Cited by 22
Gyoja, F. (2017) · genesis · doi:10.1002/dvg.23051 · Cited by 22
Ouyang, Q., Ruiz-Noriega, M., & Henry, S. A. (1999) · Genetics · doi:10.1093/genetics/152.1.89 · Cited by 22
Regulation of mammalian gene expression
Beyersmann, D. (2000) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-0348-8393-1_2 · Cited by 22
Annweiler, A., Müller, U., & Wirth, T. C. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.7.1503 · Cited by 22
Javaux, F., Donda, A., Vassart, G., & Christophe, D. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.5.1121 · Cited by 22
B-Cell Factor 1 Is Required for Optimal Expression of the DRA Promoter in B Cells
Voliva, C. F., Aronheim, A., WALKER, M. D., & Peterlin, B. M. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2383 · Cited by 22
Jacobs, Y., Xin, X., Dorshkind, K. A., & Nelson, C. G. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.4087 · Cited by 22
Liu, L. N., Dias, P., & Houghton, P. J. (1998) · PubMed · Cited by 21
HMG box proteins in early T-cell differentiation.
Oosterwegel, M. A., van de Wetering, M., & Clevers, H. C. (1993) · PubMed · Cited by 21
Identification of a highly conserved region at the 5′ flank of the phospholamban gene
Johns, D. C., & Feldman, A. M. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91144-f · Cited by 21
Understanding the molecular mechanisms of reprogramming
Krause, M. N., Sancho-Martinez, I., & Belmonte, J. C. I. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.11.120 · Cited by 21
Making muscle: Morphogenetic movements and molecular mechanisms of myogenesis in Xenopus laevis
Sabillo, A., Ramirez, J. C., & Domingo, C. R. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.02.006 · Cited by 21
Nuclear transcription factors in the hippocampus
Hinoi, E., Balcar, V. J., Kuramoto, N., Nakamichi, N., & Yoneda, Y. (2002) · Progress in Neurobiology · doi:10.1016/s0301-0082(02)00078-3 · Cited by 20
Functional conservation of nematode and vertebrate myogenic regulatory factors
Krause, M., Fire, A. Z., Harrison, S. M. W., Weintraub, H. M., & Tapscott, S. J. (1992) · Journal of Cell Science · doi:10.1242/jcs.1992.supplement_16.13 · Cited by 20
Self-citationMohun, T. J. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90119-w · Cited by 20
Cell plasticity in Caenorhabditis elegans: From induced to natural cell reprogramming
Hajdůšková, M., Ahier, A., Daniele, T., & Jarriault, S. (2011) · genesis · doi:10.1002/dvg.20806 · Cited by 20
Topno, N. S., Muthu, K., & Krishna, R. (2015) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2015.12.002 · Cited by 19
CCAAT/Enhancer Binding Protein β inhibits myogenic differentiation via ID3
AlSudais, H., Lala-Tabbert, N., & Wiper‐Bergeron, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-34871-0 · Cited by 19
HES6-1 and HES6-2 Function through Different Mechanisms during Neuronal Differentiation
Vilas‐Boas, F., & Henrique, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015459 · Cited by 19
Transcriptional analysis of the titin cap gene
Zhang, S., Londhe, P., Zhang, M., & Davie, J. K. (2011) · Molecular Genetics and Genomics · doi:10.1007/s00438-011-0603-6 · Cited by 19
Momoi, T., Miyagawa‐Tomita, S., Nakamura, S., Kimura, I., & Momoi, M. Y. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81484-6 · Cited by 19
Sandmöller, A., Meents, H., & Arnold, H.-H. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5846 · Cited by 19
Structure and myofiber-specific expression of the rat muscle regulatory gene MRF4
Hinterberger, T. J., Mays, J. L., & Konieczny, S. F. (1992) · Gene · doi:10.1016/0378-1119(92)90730-d · Cited by 19
Maged1, a new regulator of skeletal myogenic differentiation and muscle regeneration
Nguyen, T. H., Bertrand, M. J. M., Sterpin, C., Achouri, Y., & Backer, O. D. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-57 · Cited by 18
Expression Analysis of a Tyrosinase Promoter Sequence in Zebrafish
Camp, E., Badhwar, P., Mann, G. J., & Lardelli, M. T. (2003) · Pigment Cell Research · doi:10.1034/j.1600-0749.2003.00002.x · Cited by 18
van de Klundert, F. A. J. M., Jansen, H. J., & BLOEMENDAL, H. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42337-4 · Cited by 18
Sparn, H. G., Lieder-Ochs, B. A., & Franke, W. W. (1994) · Differentiation · doi:10.1046/j.1432-0436.1994.5630191.x · Cited by 18
MyoD: A Regulatory Gene of Skeletal Myogenesis
Tapscott, S. J., Davis, R. L., Lassar, A. B., & Weintraub, H. M. (1990) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-5865-7_1 · Cited by 18
Self-citationLi, F.-Q., Coonrod, A., & Horwitz, M. S. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.4.1043 · Cited by 18
The role of cellular oncogenes in myogenesis and muscle cell hypertrophy
Hesketh, J. E., & Whitelaw, P. F. (1992) · International Journal of Biochemistry · doi:10.1016/0020-711x(92)90247-x · Cited by 18
MacQuarrie, K. L., Yao, Z., Fong, A. P., & Tapscott, S. J. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-26 · Cited by 17
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Shibata, H., Oda, H., Mukai, H., Oishi, K., Misaki, K., Ohkubo, H., & Ono, Y. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00273-9 · Cited by 17
Benton, B. K., Reid, M. S., & Okayama, H. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05639.x · Cited by 17
Schaefer, B. M., Koch, J., Wirzbach, A., & Kramer, M. D. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5215 · Cited by 16
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Miyagishi, M., Hatta, M., Ohshima, T., Ishida, J., Fujii, R., Nakajima, T., & Fukamizu, A. (2000) · Molecular and Cellular Biochemistry · doi:10.1023/a:1007057611868 · Cited by 16
Emerging Parallels between Stomatal and Muscle Cell Lineages
Serna, L. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.133090 · Cited by 16
Thelen, H., Simonides, W. S., Muller, A., & van Hardeveld, C. (1998) · Biochemical Journal · doi:10.1042/bj3290131 · Cited by 16
Chakraborty, T., Martin, J. F., & Olson, E. N. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37069-3 · Cited by 16
Myogenin binds to and represses c‐fos promoter
Trouche, D., Masutani, H., Groisman, R., Robin, P., Lenormand, J., & Harel‐Bellan, A. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00140-5 · Cited by 16
Braatz, J., Harloff, H., & Jung, C. (2018) · Euphytica · doi:10.1007/s10681-018-2113-7 · Cited by 15
Jeong, J., Choi, K., Kim, S., Lee, D., Oh, J., Lee, M., Choe, G. C., & Lee, C. (2021) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-021-00583-1 · Cited by 15
Okagami, M., Ueno, M., Makino, K., Shimomura, M., Saito, I., Morii, T., & Sugiura, Y. (1995) · Bioorganic & Medicinal Chemistry · doi:10.1016/0968-0896(95)00047-k · Cited by 15
Daczewska, M. (2001) · Zoomorphology · doi:10.1007/s004350100042 · Cited by 15
MyoD Functions as a Transcriptional Repressor in Proliferating Myoblasts
Chu, C., Cogswell, J. P., & Kohtz, D. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3145 · Cited by 15
Kobiyama, A., Hirayama, M., Muramatsu-Uno, M., & Watabe, S. (2006) · Gene · doi:10.1016/j.gene.2005.12.006 · Cited by 15
Hikosaka, A., Satoh, N., & Makabe, K. W. (1993) · Development Genes and Evolution · doi:10.1007/bf00539896 · Cited by 15
Adenoviral mediated MyoD gene transfer into fibroblasts: Myogenic disease diagnosis
Fujii, I., Matsukura, M., Ikezawa, M., Suzuki, S., Shimada, T., & Miike, T. (2006) · Brain and Development · doi:10.1016/j.braindev.2005.12.007 · Cited by 15
Tsai, C. C., Saffitz, J. E., & Billadello, J. J. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119135 · Cited by 15
Laue, T. M., Starovasnik, M. A., Weintraub, H. M., Sun, X.-H., Snider, L. D., & Klevit, R. E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11824 · Cited by 15
Self-citationTang, F., Yao, X., Zhu, H., Mu, H., Niu, Z., Yu, M., Yang, C., Peng, S., Li, G., & Hua, J. (2013) · Cell Proliferation · doi:10.1111/cpr.12077 · Cited by 14
Caveolin-3 Is a Sensitive and Specific Marker for Rhabdomyosarcoma
Fine, S. W., Lisanti, M. P., Argani, P., & Li, M. (2005) · Applied immunohistochemistry & molecular morphology · doi:10.1097/00129039-200509000-00003 · Cited by 14
Lindh, J. G., Connolly, B., McGhie, D., & Smith, D. F. (1998) · Molecular and Biochemical Parasitology · doi:10.1016/s0166-6851(97)00242-9 · Cited by 14
Molecular cloning of a myoD-like gene from the parasitic nematode, Trichinella spiralis
Connolly, B., Trenholme, K. R., & Smith, D. F. (1996) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(96)02673-4 · Cited by 14
Single chain dimers of MASH-1 bind DNA with enhanced affinity
Sieber, M. A., & Allemann, R. K. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.6.1408 · Cited by 14
Rubio, N., & Torres, C. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00177-1 · Cited by 14
Liu, Z., Kim, S., Kucuktas, H., & Karsi, A. (2001) · Gene · doi:10.1016/s0378-1119(01)00679-5 · Cited by 14
Olson, E. N. (1992) · Trends in Cardiovascular Medicine · doi:10.1016/1050-1738(92)90044-s · Cited by 14
The human M creatine kinase gene enhancer contains multiple functional interacting domains
Trask, R. V., Koster, J. C., Ritchie, M. E., & Billadello, J. J. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.9.2313 · Cited by 14
Anand, G., Shapiro, D. N., Dickman, P. S., & Prochownik, E. V. (1994) · Journal of Clinical Investigation · doi:10.1172/jci116982 · Cited by 13
Muscle-specific RNA processing continues in the absence of myogenin expression.
Saitoh, O., Olson, E. N., & Periasamy, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45379-8 · Cited by 13
The myb and myc nuclear oncogenes as transcriptional activators
Cole, M. D. (1990) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(90)90134-z · Cited by 13
Muthuchamy, M., Pajak, L., & Wieczorek, D. F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37022-x · Cited by 13
Sequence diversity in the 5′ untranslated region of rabbit muscle phosphofructokinase mRNA
Li, J., Chen, Z., Lu, L., Byrnes, M., & Chang, S. H. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)90499-d · Cited by 13
Cloning and analysis of a new developmentally regulated member of the basic helix-loop-helix family
Helms, J. A., Kuratani, S., & Maxwell, G. D. (1994) · Mechanisms of Development · doi:10.1016/0925-4773(94)90019-1 · Cited by 13
MEF2A Gene Polymorphisms are Associated with Growth Traits in Chinese Indigenous Cattle Breeds
Chen, F., Chen, H., Wang, J.-Q., Niu, H., Lan, X., Hua, L., Li, Z., Lei, C., & Fang, X. (2010) · Journal of Animal and Veterinary Advances · doi:10.3923/javaa.2010.814.819 · Cited by 12
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Sarkar, C., & Maitra, A. (2007) · Gene · doi:10.1016/j.gene.2007.10.026 · Cited by 13
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Mak, K.-L., LONGCOR, L. C., Johnson, S., Lemercier, C., To, R. Q., & Konieczny, S. F. (1996) · DNA and Cell Biology · doi:10.1089/dna.1996.15.1 · Cited by 12
Moss, J. B., Olson, E. N., & Schwartz, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31688 · Cited by 12
Thomas‐Tikhonenko, A., Hartman, A., & Linial, M. L. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3623 · Cited by 12
Metadata
- Authors
- Davis, R. L., Cheng, P.-F., Lassar, A. B., & Weintraub, H.
- Affiliations
- University of Washington (US)
- Fred Hutch Cancer Center (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1990-03
- Volume
- 60
- Issue
- 5
- Pages
- 733-746
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2078709292
- Cited by
- 765
- References
- 52
- Citations by year
- 2026: 2 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 3 · 2017: 7 · 2016: 9 · 2015: 5 · 2014: 5 · 2013: 8 · 2012: 12
- FWCI
- 45.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- MyoD, DNA-binding domain, helix-loop-helix proteins, basic region, E12, C3H10T1/2 cells, sequence-specific DNA binding, transcriptional activation
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Differentiation, Cells, Cultured, Chromosome Deletion, DNA, Enhancer Elements, Genetic, Gene Expression Regulation, Genes, Models, Molecular, Molecular Sequence Data, Muscle Proteins, Muscles, Protein Conformation, Transfection, Oligonucleotide Probes, Transcriptional Activation, MyoD Protein, Mice
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 ›
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