ID helix-loop-helix proteins in cell growth, differentiation and tumorigenesis

CDK inhibitors: positive and negative regulators of G1-phase progression

Sherr, C. J., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.12.1501 · Cited by 6,115 · see citing works

Notch Signaling: Cell Fate Control and Signal Integration in Development

Artavanis-Tsakonas, S., Rand, M. D., & Lake, R. J. (1999) · Science · doi:10.1126/science.284.5415.770 · Cited by 5,909 · see citing works

The protein Id: A negative regulator of helix-loop-helix DNA binding proteins

Benezra, R., Davis, R. L., Lockshon, D., Turner, D. L., & Weintraub, H. M. (1990) · Cell · doi:10.1016/0092-8674(90)90214-y · Cited by 2,202 · see citing works

Helix-Loop-Helix Proteins: Regulators of Transcription in Eucaryotic Organisms

Massari, M. E., & Murre, C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.2.429-440.2000 · Cited by 1,800 · see citing works

Id1 and Id3 are required for neurogenesis, angiogenesis and vascularization of tumour xenografts

Lyden, D. C., Young, A. Z., Zagzag, D., Yan, W. X., Gerald, W. L., O'Reilly, R., Bader, B., Hynes, R. O., Zhuang, Y., Manova, K., et al. (1999) · Nature · doi:10.1038/44334 · Cited by 912 · see citing works

Development of peripheral lymphoid organs and natural killer cells depends on the helix–loop–helix inhibitor Id2

Yokota, Y., Mansouri, A., Mori, S., Sugawara, S., Adachi, S., Nishikawa, S., & Gruß, P. (1999) · Nature · doi:10.1038/17812 · Cited by 851 · see citing works

Cold Spring Harbor Symposia on Quantitative Biology

(1934) · Science · doi:10.1126/science.79.2061.584 · Cited by 605 · see citing works

Id Proteins Id1 and Id2 Selectively Inhibit DNA Binding by One Class of Helix-Loop-Helix Proteins

Sun, X., Copeland, N. G., Jenkins, N. A., & Baltimore, D. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.11.5603 · Cited by 605 · see citing works

Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins

Jen, Y., Weintraub, H., & Benezra, R. (1992) · Genes & Development · doi:10.1101/gad.6.8.1466 · Cited by 471 · see citing works

HLH proteins, fly neurogenesis, and vertebrate myogenesis

Jan, Y. N., & Jan, L. Y. (1993) · Cell · doi:10.1016/0092-8674(93)90525-u · Cited by 419 · see citing works

Id helix—loop—helix proteins in cell growth and differentiation

Norton, J. D., Deed, R. W., Craggs, G., & Sablitzky, F. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)80013-5 · Cited by 410 · see citing works

extramacrochaetae, a negative regulator of sensory organ development in Drosophila, defines a new class of helix-loop-helix proteins

Ellis, H. M., Spann, D. R., & Posakony, J. W. (1990) · Cell · doi:10.1016/0092-8674(90)90212-w · Cited by 404 · see citing works

The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein.Preprint

Iavarone, A., Garg, P. P., Lasorella, A., Hsu, J. C., & Israel, M. A. (1994) · Genes & Development · doi:10.1101/gad.8.11.1270 · Cited by 365 · see citing works

The Drosophila extramacrochaetae locus, an antagonist of proneural genes that, like these genes, encodes a helix-loop-helix protein

Garrell, J., & Modolell, J. (1990) · Cell · doi:10.1016/0092-8674(90)90213-x · Cited by 363 · see citing works

An Id-related helix-loop-helix protein encoded by a growth factor-inducible gene.

Christy, B. A., Sanders, L. K., Lau, L. F., Copeland, N. G., Jenkins, N. A., & Nathans, D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1815 · Cited by 334 · see citing works

Regulation of the Expression of Cyclin-Dependent Kinase Inhibitor p21 by E2A and Id Proteins

Prabhu, S., Ignatova, A., Park, S. T., et al. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.10.5888 · Cited by 326 · see citing works

Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts.

Hara, E., Yamaguchi, T., Nojima, H., Ide, T., Campisi, J., Okayama, H., & Oda, K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42146-6 · Cited by 311 · see citing works

Inhibition of T Cell and Promotion of Natural Killer Cell Development by the Dominant Negative Helix Loop Helix Factor Id3

Heemskerk, M. H. M., Blom, B., Nolan, G. P., Stegmann, A. P. A., Bakker, A. Q., Weijer, K. C., Res, P. C. M., & Spits, H. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.9.1597 · Cited by 273 · see citing works

The expression pattern ofId4, a novel dominant negative helix-loop-helix protein, is distinct fromId1,1d2andId3

Riechmann, V., van Crüchten, I., & Sablitzky, F. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.5.749 · Cited by 272 · see citing works

Constitutive expression of the Id1 gene impairs mouse B cell development

Sun, X.-H. (1994) · Cell · doi:10.1016/0092-8674(94)90078-7 · Cited by 263 · see citing works

Id2 Specifically Alters Regulation of the Cell Cycle by Tumor Suppressor Proteins

Lasorella, A., Iavarone, A., & Israel, M. A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.6.2570 · Cited by 241 · see citing works

A role for Id-1 in the aggressive phenotype and steroid hormone response of human breast cancer cells.

Lin, C. Q., Singh, J., Murata, K., et al. (2000) · PubMed · Cited by 235 · see citing works

High Incidence of T-Cell Tumors in E2A-Null Mice and E2A/Id1 Double-Knockout Mice

Yan, W. X., Young, A. Z., Soares, V., Kelley, R., Benezra, R., & Zhuang, Y. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.7317 · Cited by 230 · see citing works

Differential Interactions of Id Proteins with Basic-Helix-Loop-Helix Transcription Factors

Langlands, K., Yin, X., Anand, G., & Prochownik, E. V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.19785 · Cited by 226 · see citing works

Id proteins control growth induction in mammalian cells.

Barone, M. V., Pepperkok, R., Peverali, F. A., & Philipson, L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4985 · Cited by 225 · see citing works

Thymocyte Selection Is Regulated by the Helix-Loop-Helix Inhibitor Protein, Id3

Rivera, R. R., Johns, C., Quan, J., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)80155-7 · Cited by 221 · see citing works

The Id4 HLH protein and the timing of oligodendrocyte differentiation

Kondo, T., & Raff, M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.9.1998 · Cited by 203 · see citing works

Regulation of G1 progression by E2A and Id helix‐loop‐helix proteins.

Peverali, F. A., Ramqvist, T., Saffrich, R., Pepperkok, R., Barone, M. V., & Philipson, L. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06749.x · Cited by 197 · see citing works

Coupling of Cell Growth Control and Apoptosis Functions of Id Proteins

Norton, J. D., & Atherton, G. T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.4.2371 · Cited by 187 · see citing works

Suppression of Mammary Epithelial Cell Differentiation by the Helix-Loop-Helix Protein Id-1

Desprez, P., Hara, E., Bissell, M. J., & Campisi, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3398 · Cited by 183 · see citing works

Id Proteins Id1 and Id2 Selectively Inhibit DNA Binding by One Class of Helix-Loop-Helix Proteins

Sun, X., Copeland, N. G., Jenkins, N. A., et al. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.11.5603-5611.1991 · Cited by 173 · see citing works

Impaired Immune Responses and B-Cell Proliferation in Mice Lacking the Id3 Gene

Pan, L., Sato, S., Frederick, J. P., et al. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.9.5969 · Cited by 169 · see citing works

Id-1 and Id-2 Are Overexpressed in Pancreatic Cancer and in Dysplastic Lesions in Chronic Pancreatitis

Maruyama, H., Kleeff, J. H., Wildi, S., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65180-2 · Cited by 153 · see citing works

Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors

Yates, P. R., Atherton, G. T., Deed, R. W., Norton, J. D., & Sharrocks, A. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.968 · Cited by 152 · see citing works

Transcription factors 2: helix-loop-helix.

Littlewood, T. D., & Evan, G. I. (1994) · PubMed · Cited by 149 · see citing works

A Novel Pathway for Mammary Epithelial Cell Invasion Induced by the Helix-Loop-Helix Protein Id-1

Desprez, P., Lin, C. Q., Thomasset, N., Sympson, C. J., Bissell, M. J., & Campisi, J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4577 · Cited by 148 · see citing works

Neural Crest Specification Regulated by the Helix-Loop-Helix Repressor Id2

Martinsen, B. J., & Bronner-Fraser, M. E. (1998) · Science · doi:10.1126/science.281.5379.988 · Cited by 145 · see citing works

Overexpression of the Helix–Loop–Helix protein Id2 blocks T cell development at multiple stages

Morrow, M. A., Mayer, E. W., Perez, C. A., et al. (1999) · Molecular Immunology · doi:10.1016/s0161-5890(99)00071-1 · Cited by 139 · see citing works

Immortalization of primary human keratinocytes by the helix–loop–helix protein, Id-1

Alani, R. M., Hasskarl, J., Grace, M. R., Hernandez, M.-C., Israel, M. A., & Münger, K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9637 · Cited by 137 · see citing works

E2A activity is induced during B‐cell activation to promote immunoglobulin class switch recombination

Quong, M. W., Harris, D. P., Swain, S. L., & Murre, C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6307 · Cited by 136 · see citing works

A human Id-like helix-loop-helix protein expressed during early development.

Biggs, J. R., Murphy, E. V., & Israel, M. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.4.1512 · Cited by 136 · see citing works

Massive Apoptosis of Thymocytes in T-Cell-Deficient Id1 Transgenic Mice

Kim, D.-S., Peng, X.-C., & Sun, X.-H. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8240 · Cited by 133 · see citing works

Cdk2‐dependent phosphorylation of Id2 modulates activity of E2A‐related transcription factors

Hara, E., Hall, M., & Peters, G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.332 · Cited by 128 · see citing works

Degradation of Id proteins by the ubiquitin‐proteasome pathway

Bounpheng, M. A., Dimas, J., Dodds, S. G., & Christy, B. A. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.15.2257 · Cited by 127 · see citing works

Thymocyte Maturation Is Regulated by the Activity of the Helix-Loop-Helix Protein, E47

Bain, G., Quong, M. W., Soloff, R. S., et al. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.11.1605 · Cited by 126 · see citing works

Id2 Promotes Apoptosis by a Novel Mechanism Independent of Dimerization to Basic Helix-Loop-Helix Factors

Florio, M., Hernandez, M.-C., Yang, H.-T., Shu, H.-K. G., Cleveland, J., & Israel, M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5435 · Cited by 119 · see citing works

Transcription of the Dominant-Negative Helix-Loop-Helix Protein Id1 Is Regulated by a Protein Complex Containing the Immediate-Early Response Gene Egr -1†

Tournay, O., & Benezra, R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.5.2418 · Cited by 118 · see citing works

Ectopic expression of E47 or E12 promotes the death of E2A-deficient lymphomas

Engel, I., & Murre, C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.996 · Cited by 105 · see citing works

Regulation of Id3 Cell Cycle Function by Cdk-2-Dependent Phosphorylation

Deed, R. W., Hara, E., Atherton, G. T., et al. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6815 · Cited by 104 · see citing works

An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types.

Deed, R. W., Bianchi, S. M., Atherton, G. T., et al. (1993) · PubMed · Cited by 96 · see citing works

Disruption of αβ but not of γδ T cell development by overexpression of the helix–loop–helix protein Id3 in committed T cell progenitors

Blom, B., Heemskerk, M. H. M., Verschuren, M. C. M., van Dongen, J. J. M., Stegmann, A. P. A., Bakker, A. Q., Couwenberg, F., Res, P. C. M., & Spits, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.10.2793 · Cited by 93 · see citing works

MIDA1, a Protein Associated with Id, Regulates Cell Growth

Shoji, W., Inoue, T., Yamamoto, T., & Obinata, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.42.24818 · Cited by 91 · see citing works

The helix-loop-helix protein Id2 is overexpressed in human pancreatic cancer.

Kleeff, J. H., Ishiwata, T., Frieß, H., et al. (1998) · PubMed · Cited by 91 · see citing works

Nuclear Localization and Regulation of Id Protein through an E Protein-mediated Chaperone Mechanism

Deed, R. W., Armitage, S., & Norton, J. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.39.23603 · Cited by 87 · see citing works

Forced Expression of Id-1 in the Adult Mouse Small Intestinal Epithelium Is Associated with Development of Adenomas

Wice, B. M., & Gordon, J. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25310 · Cited by 82 · see citing works

Stage- and subcellular-specific expression of Id proteins in male germ and Sertoli cells implicates distinctive regulatory roles for Id proteins during meiosis, spermatogenesis, and Sertoli cell function.

Sablitzky, F., Moore, A., Bromley, M., et al. (1998) · PubMed · Cited by 80 · see citing works

Id2 expression increases with differentiation of human myeloid cells

Ishiguro, A., Ks, S., Shiohara, M., et al. (1996) · Blood · doi:10.1182/blood.v87.12.5225.bloodjournal87125225 · Cited by 79 · see citing works

Genetic Modification of Human B-Cell Development: B-Cell Development Is Inhibited by the Dominant Negative Helix Loop Helix Factor Id3

Jaleco, A. C., Stegmann, A. P. A., Heemskerk, M. H. M., et al. (1999) · Blood · doi:10.1182/blood.v94.8.2637.420k22_2637_2646 · Cited by 77 · see citing works

Growth Inhibition and Apoptosis Due to Restoration of E2A Activity in T Cell Acute Lymphoblastic Leukemia Cells

Park, S. T., Nolan, G. P., & Sun, X.-H. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.3.501 · Cited by 72 · see citing works

Functional antagonism between inhibitor of DNA binding (Id) and adipocyte determination and differentiation factor 1/sterol regulatory element-binding protein-1c (ADD1/SREBP-1c) trans-factors for the regulation of fatty acid synthase promoter in adipocytes

Moldes, M., Boizard, M., Lièpvre, X. L., Fève, B., Dugail, I., & Pairault, J. (1999) · Biochemical Journal · doi:10.1042/bj3440873 · Cited by 71 · see citing works

Expression of Id1 Results in Apoptosis of Cardiac Myocytes through a Redox-dependent Mechanism

Tanaka, K., Pracyk, J. B., Takeda, K., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25922 · Cited by 62 · see citing works

Role of EP2 receptors and cAMP in prostaglandin E2 regulated expression of type I collagen α1, lysyl oxidase, and cyclooxygenase-1 genes in human embryo lung fibroblasts

Choung, J., Taylor, L., Thomas, K. M., Zhou, X. C., Kagan, H. M., Yang, X., & POLGAR, P. R. (1998) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19981101)71:2 · Cited by 58 · see citing works

Regulation of cell differentiation in C2C12 myoblasts by the Id3 helix-loop-helix protein.

Atherton, G. T., Travers, H., Deed, R. W., & Norton, J. D. (1996) · PubMed · Cited by 58 · see citing works

Regulation of the Proneural Gene achaete by Helix-Loop-Helix Proteins

Martı́nez, C., Modolell, J., & Garrell, J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3514 · Cited by 55 · see citing works

Id4 Expression Induces Apoptosis in Astrocytic Cultures and Is Down-regulated by Activation of the cAMP-Dependent Signal Transduction Pathway

Andrés-Barquin, P. J., Hernandez, M., & Israel, M. A. (1999) · Experimental Cell Research · doi:10.1006/excr.1998.4360 · Cited by 53 · see citing works

Id genes in nervous system development.

Andrés-Barquin, P. J., Hernández, M., & Israel, M. A. (2000) · PubMed · doi:10.14670/hh-15.603 · Cited by 53 · see citing works

Differential Biological Activities of Mammalian Id Proteins in Muscle Cells

Melnikova, I. N., Bounpheng, M. A., Schatteman, G. C., Gilliam, D., & Christy, B. A. (1999) · Experimental Cell Research · doi:10.1006/excr.1998.4330 · Cited by 49 · see citing works

Structural organisation and chromosomal mapping of the human Id-3 gene

Deed, R. W., Hirose, T., Mitchell, E. L. D., et al. (1994) · Gene · doi:10.1016/0378-1119(94)90676-9 · Cited by 49 · see citing works

Lymphoid-specific Expression of the Id3 Gene in Hematopoietic Cells

Deed, R. W., Jasiok, M., & Norton, J. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.14.8278 · Cited by 40 · see citing works

Id genes encoding inhibitors of transcription are expressed during in vitro astrocyte differentiation and in cell lines derived from astrocytic tumors.

Andrés-Barquin, P. J., Hernandez, M., Hayes, T. E., et al. (1997) · PubMed · Cited by 40 · see citing works

MIDA1, an Id-Associating Protein, Has Two Distinct DNA Binding Activities That Are Converted by the Association with Id1: A Novel Function of Id Protein

Inoue, T., Shoji, W., & Obinata, M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1779 · Cited by 38 · see citing works

Relationships between extramacrochaetae and Notch signalling in Drosophila wing development

Baonza, A., de Celis, J. F., & Garcı́a-Bellido, A. (2000) · Development · doi:10.1242/dev.127.11.2383 · Cited by 37 · see citing works

Identification of Id2 as a Globin Regulatory Protein by Representational Difference Analysis of K562 Cells Induced To Express γ-Globin with a Fungal Compound

Holmes, M. L., Haley, J. D., Cerruti, L., Zhou, W., Zogos, H., Smith, D. E., Cunningham, J. M., & Jane, S. M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4182 · Cited by 26 · see citing works

Suppression of adenovirus E1A-induced apoptosis by mutated p53 is overcome by coexpression with Id proteins

Nakajima, T., Sakurai‐Yageta, M., Shiotsu, K., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10590 · Cited by 25 · see citing works

MIDA1 is a sequence specific DNA binding protein with novel DNA binding properties

Inoue, T., Shoji, W., & Obinata, M. (2000) · Genes to Cells · doi:10.1046/j.1365-2443.2000.00362.x · Cited by 22 · see citing works

Dual role of extramacrochaetae in cell proliferation and cell differentiation during wing morphogenesis in Drosophila

Baonza, A., & Garcı́a-Bellido, A. (1999) · Mechanisms of Development · doi:10.1016/s0925-4773(98)00198-1 · Cited by 21 · see citing works

Identification of a novel transcriptional activity of mammalian Id proteins

Bounpheng, M. A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.7.1740 · Cited by 18 · see citing works

Helix-Loop-Helix-Proteins

Schwab, M. (2011) · Springer eBooks · doi:10.1007/978-3-642-16483-5_6349 · Cited by 2 · see citing works

Direct Binding of Smad1 and Smad4 to Two Distinct Motifs Mediates Bone Morphogenetic Protein-specific Transcriptional Activation ofId1 Gene

López-Rovira, T., Chalaux, E., Massagué, J., Rosa, J. L., & Ventura, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106826200 · Cited by 285 · see citing works

The c‐myc Promoter: Still MysterY and Challenge

(2008) · Advances in Cancer Research · doi:10.1016/s0065-230x(07)99004-1 · Cited by 211 · see citing works

Denervation stimulates apoptosis but not Id2 expression in hindlimb muscles of aged rats

Alway, S. E., Degens, H., Krishnamurthy, G., & Chaudhrai, A. (2003) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/58.8.b687 · Cited by 96 · see citing works

Multiple roles of Id4 in developmental myelination: predicted outcomes and unexpected findings

Marin‐Husstege, M., He, Y., Li, J., Kondo, T., Sablitzky, F., & Casaccia‐Bonnefil, P. (2006) · Glia · doi:10.1002/glia.20385 · Cited by 91 · see citing works

Evolutionary aspects of developmentally regulated helix-loop-helix transcription factors in striated muscle of jellyfish

Müller, P., Seipel, K., Yanze, N., Reber-Müller, S., Streitwolf-Engel, R., Stierwald, M., Spring, J. Ü., & Schmid, V. (2003) · Developmental Biology · doi:10.1016/s0012-1606(02)00091-x · Cited by 69 · see citing works

Riding the crest of the wave: parallels between the neural crest and cancer in epithelial-to-mesenchymal transition and migration

Powell, D. R., Blasky, A. J., Britt, S. G., & Artinger, K. B. (2013) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1224 · Cited by 62 · see citing works

A role for Id2 in regulating photic entrainment of the mammalian circadian system

Duffield, G. E., Watson, N. P., Mantani, A., Peirson, S. N., Robles-Murguia, M., Loros, J. J., Israel, M. A., & Dunlap, J. C. (2009) · Current Biology · doi:10.1016/j.cub.2008.12.052 · Cited by 59 · see citing works

Ablation of the ID2 gene results in altered circadian feeding behavior, and sex-specific enhancement of insulin sensitivity and elevated glucose uptake in skeletal muscle and brown adipose tissue

Mathew, D., Zhou, P., Pywell, C. M., van der Veen, D. R., Shao, J., Xi, Y., Bonar, N. A., Hummel, A. D., Chapman, S., Leevy, W. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073064 · Cited by 30 · see citing works

Regulation of TCF ETS-domain transcription factors by helix-loop-helix motifs

Stinson, J. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg689 · Cited by 27 · see citing works

Regulatory interdependence of myeloid transcription factors revealed by Matrix RNAi analysis

Tomaru, Y., Simon, C., Forrest, A. R., Miura, H., Kubosaki, A., Hayashizaki, Y., & Suzuki, M. (2009) · Genome biology · doi:10.1186/gb-2009-10-11-r121 · Cited by 21 · see citing works

Cross-talk between redox regulation and the ubiquitin–proteasome system in mammalian cell differentiation

Demasi, M., Simões, V., & Bonatto, D. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.10.031 · Cited by 18 · see citing works

Basic helix-loop-helix transcription factors and epidermal cell fate determination in Arabidopsis

Zhao, H., Li, X., & Ma, L. (2012) · Plant Signaling & Behavior · doi:10.4161/psb.22404 · Cited by 38 · see citing works

Regulation of retinal cell fate specification by multiple transcription factors

Ohsawa, R., & Kageyama, R. (2007) · Brain Research · doi:10.1016/j.brainres.2007.04.014 · Cited by 190 · see citing works

The Role of Cellular Differentiation and Cell Fate in Malignant Melanoma

Kuzel, P., & Andy, J. C. (2011) · InTech eBooks · doi:10.5772/20002

A Generalized Gene-Regulatory Network Model of Stem Cell Differentiation for Predicting Lineage Specifiers

Okawa, S., Nicklas, S., Zickenrott, S., Schwamborn, J. C., & del Sol, A. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.07.014 · Cited by 50 · see citing works