Transcription Factor Pip Can Enhance DNA Binding by E47, Leading to Transcriptional Synergy Involving Multiple Protein Domains

Nagulapalli, Sujatha; Atchison, Michael L.

doi:10.1128/mcb.18.8.4639

Cited by 66Genomics and Chromatin DynamicsT-cell and B-cell ImmunologyDevelopmental Biology and Gene Regulation

Transcription Factor Pip Can Enhance DNA Binding by E47, Leading to Transcriptional Synergy Involving Multiple Protein Domains

Open access

Nagulapalli, Sujatha, Atchison, Michael L.·1998·Molecular and Cellular Biology

DOI 10.1128/mcb.18.8.4639PMC PMC109050

Open this paper in CoChat — free account Open PDF

Abstract

The transcription factors E2A (E12/E47) and Pip are both required for normal B-cell development. Each protein binds to regulatory sequences within various immunoglobulin enhancer elements. Activity of E2A proteins can be regulated by interactions with other proteins which influence their DNA binding or activation potential. Similarly, Pip function can be influenced by interaction with the protein PU.1, which can recruit Pip to bind to DNA. We show here that a previously unidentified Pip binding site resides adjacent to the E2A binding site within the immunoglobulin kappa 3' enhancer. Both of these binding sites are crucial for high-level enhancer activity. We found that E47 and Pip can functionally interact to generate a very potent 100-fold transcriptional synergy. Through a series of mutagenesis experiments, we identified the Pip sequences necessary for transcriptional activation and for synergy with E47. Two synergy domains (residues 140 to 207 and 300 to 420) in addition to the Pip DNA binding domain (residues 1 to 134) are required for maximal synergy with E47. We also identified a Pip domain (residues 207 to 300) that appears to mask Pip transactivation potential. Part of the synergy mechanism between E47 and Pip appears to involve the ability of Pip to increase DNA binding by E47, perhaps by inducing a conformational change in the E47 protein. E47 may also induce a conformational change in Pip which unmasks sequences important for transcriptional activity. Based upon our results, we propose a model for E47-Pip transcriptional synergy.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1128/mcb.18.8.4639

Cites

76 of 76 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

ICSBP interacts with E47 on the element composed of an IRS-like sequence and the E2A binding site found in the Igκ 3' enhancer to activate transcription, like IRF-4.
“ICSBP was also shown to interact with E47 (encoded by the E2A gene) on the element composed of IRS-like sequence and the E2A binding site found in the Ig k 3 9 enhancer to activate transcription, again like IRF-4. (5,32)”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [32]
IRF-4 interacts with some partners common to ICSBP, namely PU.1 and E47.
“IRF-4 is similar to ICSBP in structure, interacts with some common partners (PU.1 and E47), and regulates an overlapping set of target promoters. (31,32,63,64)”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [32]
IRF-4 regulates an overlapping set of target promoters with ICSBP.
“IRF-4 is similar to ICSBP in structure, interacts with some common partners (PU.1 and E47), and regulates an overlapping set of target promoters. (31,32,63,64)”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [32]
IRF-4 is similar to ICSBP in structure.
“IRF-4 is similar to ICSBP in structure, interacts with some common partners (PU.1 and E47), and regulates an overlapping set of target promoters. (31,32,63,64)”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [32]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

A new technique for the assay of infectivity of human adenovirus 5 DNA
Graham, F. L., & van der Eb, A. J. (1973) · Virology · doi:10.1016/0042-6822(73)90341-3 · Cited by 9,734 · see citing works
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 7,673 · see citing works
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., & Pease, L. R. (1989) · Gene · doi:10.1016/0378-1119(89)90358-2 · Cited by 7,354 · see citing works
Rapid detection of octamer binding proteins with ‘mini extracts’, prepared from a small number of cells
Schreiber, E. H., Matthias, P., Müller, M. M., & Schaffner, W. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.15.6419 · Cited by 4,179 · see citing works
Recombinant Genomes Which Express Chloramphenicol Acetyltransferase in Mammalian Cells
Gorman, C. M., Moffat, L. F., & Howard, B. H. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.9.1044-1051.1982 · Cited by 3,106 · see citing works
A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins
Murre, C., Page-McCaw, P., & Baltimore, D. (1989) · Cell · doi:10.1016/0092-8674(89)90682-x · Cited by 2,713 · 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
Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence
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 · see citing works
The MyoD family and myogenesis: Redundancy, networks, and thresholds
Weintraub, H. (1993) · Cell · doi:10.1016/0092-8674(93)90610-3 · Cited by 1,057 · see citing works
Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-β gene regulatory elements
Miyamoto, M., Fujita, T., Kimura, Y., Maruyama, M., Harada, H., Sudo, Y., Miyata, T., & Taniguchi, T. (1988) · Cell · doi:10.1016/s0092-8674(88)91307-4 · Cited by 977 · see citing works
Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes
Harada, H., Fujita, T., Miyamoto, M., Kimura, Y., Maruyama, M., Furia, A., Miyata, T., & Taniguchi, T. (1989) · Cell · doi:10.1016/0092-8674(89)90107-4 · Cited by 957 · see citing works
Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo
Lassar, A. B., Davis, R. L., Wright, W. E., Kadesch, T. R., Murre, C., Voronova, A., Baltimore, D., & Weintraub, H. M. (1991) · Cell · doi:10.1016/0092-8674(91)90620-e · Cited by 836 · see citing works
E2A proteins are required for proper B cell development and initiation of immunoglobulin gene rearrangements
Bain, G. (1994) · Cell · doi:10.1016/0092-8674(94)90077-9 · Cited by 779 · see citing works
bHLH factors in muscle development: dead lines and commitments, what to leave in and what to leave out.Preprint
Olson, E. N., & Klein, W. H. (1994) · Genes & Development · doi:10.1101/gad.8.1.1 · Cited by 684 · see citing works
The helix-loop-helix gene E2A is required for B cell formation
Zhuang, Y. (1994) · Cell · doi:10.1016/0092-8674(94)90076-0 · Cited by 675 · see citing works
Protein-Binding Sites in Ig Gene Enhancers Determine Transcriptional Activity and Inducibility
Lenardo, M. J., Pierce, J. W., & Baltimore, D. (1987) · Science · doi:10.1126/science.3109035 · Cited by 616 · 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
Requirement for the Transcription Factor LSIRF/IRF4 for Mature B and T Lymphocyte Function
Mittrücker, H.-W., Matsuyama, T., Grossman, A., Kündig, T. M., Potter, J., Shahinian, A., Wakeham, A., Patterson, B., Ohashi, P. S., & Mak, T. W. (1997) · Science · doi:10.1126/science.275.5299.540 · Cited by 583 · see citing works
Identification of cellular proteins that can interact specifically with the T/ElA-binding region of the retinoblastoma gene product
Kaelin, W. G., Pallas, D. C., DeCaprio, J. A., Kaye, F. J., & Livingston, D. M. (1991) · Cell · doi:10.1016/0092-8674(91)90236-r · Cited by 518 · see citing works
Structure and function of helix-loop-helix proteins
Murre, C., Bain, G., van Dijk, M. A., Engel, I., Furnari, B. A., Massari, M. E., Matthews, J. R., Quong, M. W., Rivera, R. R., & Stuiver, M. H. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90001-9 · Cited by 506 · see citing works
ISGF3, the transcriptional activator induced by interferon alpha, consists of multiple interacting polypeptide chains.
Fu, X.-Y., Kessler, D. S., Veals, S. A., Levy, D. E., & Darnell, J. E., Jr. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8555 · Cited by 490 · see citing works
Two Distinct Transcription Factors that Bind the Immunoglobulin Enhancer μE5/κE2 Motif
Henthorn, P. S., Kiledjian, M., & Kadesch, T. R. (1990) · Science · doi:10.1126/science.2105528 · Cited by 482 · see citing works
Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.
Eisenbeis, C. F., Singh, H., & Storb, U. (1995) · Genes & Development · doi:10.1101/gad.9.11.1377 · Cited by 447 · see citing works
Absence of the type I IFN system in EC cells: Transcriptional activator (IRF-1) and repressor (IRF-2) genes are developmentally regulated
Harada, H., Willison, K. R., Sakakibara, J., Miyamoto, M., Fujita, T., & Taniguchi, T. (1990) · Cell · doi:10.1016/0092-8674(90)90163-9 · Cited by 368 · see citing works
Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation.Preprint
Eckner, R., Yao, T., Oldread, E., & Livingston, D. M. (1996) · Genes & Development · doi:10.1101/gad.10.19.2478 · Cited by 359 · see citing works
Induction of endogenous IFN-α and IFN-β genes by a regulatory transcription factor, IRF-1
Fujita, T., Kimura, Y., Miyamoto, M., Barsoumian, E. L., & Taniguchi, T. (1989) · Nature · doi:10.1038/337270a0 · Cited by 358 · see citing works
PU.1 recruits a second nuclear factor to a site important for immunoglobulin kappa 3' enhancer activity.
Pongubala, J. M., Nagulapalli, S., Klemsz, M. J., McKercher, S. R., Maki, R. A., & Atchison, M. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.1.368 · Cited by 354 · see citing works
Self-citation
B-Lymphocyte Development Is Regulated by the Combined Dosage of Three Basic Helix-Loop-Helix Genes, E2A , E2-2 , and HEB†
Zhuang, Y., Cheng, P.-F., & Weintraub, H. M. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.6.2898 · Cited by 339 · 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
Interferon-alpha regulates nuclear translocation and DNA-binding affinity of ISGF3, a multimeric transcriptional activator.
Kessler, D. S., Veals, S. A., Fu, X. Y., & Levy, D. E. (1990) · Genes & Development · doi:10.1101/gad.4.10.1753 · Cited by 312 · see citing works
Human and Drosophila Homeodomain Proteins That Enhance the DNA-Binding Activity of Serum Response Factor
Grueneberg, D. A., Natesan, S., Alexandre, C., & Gilman, M. Z. (1992) · Science · doi:10.1126/science.257.5073.1089 · Cited by 310 · see citing works
HEB, a Helix-Loop-Helix Protein Related to E2A and ITF2 That Can Modulate the DNA-Binding Ability of Myogenic Regulatory Factors
Hu, J. S., Olson, E. N., & Kingston, R. E. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.1031 · Cited by 310 · see citing works
Effect of PU.1 phosphorylation on interaction with NF-EM5 and transcriptional activation
Pongubala, J., Van Beveren, C., Nagulapalli, S., Klemsz, M., McKercher, Maki, R., & Atchison, M. (1993) · Science · doi:10.1126/science.8456286 · Cited by 282 · cited 1× · see citing works
“1 to stimulate 39 enhancer activity (49).”
Self-citation
IRF-7, a new interferon regulatory factor associated with Epstein-Barr virus latency
Zhang, L.-W., & Pagano, J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.10.5748 · Cited by 277 · 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
Critical role of a common transcription factor, IRF‐1, in the regulation of IFN‐beta and IFN‐inducible genes.
Reis, L. F. L., Harada, H., Wolchok, J. D., Taniguchi, T., & Vilček, J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05041.x · Cited by 243 · see citing works
Pip, a lymphoid-restricted IRF, contains a regulatory domain that is important for autoinhibition and ternary complex formation with the Ets factor PU.1.
Brass, A. L., Kehrli, E., Eisenbeis, C. F., Storb, U., & Singh, H. (1996) · Genes & Development · doi:10.1101/gad.10.18.2335 · Cited by 242 · see citing works
Molecular cloning ofLSIRF, a lymphoid-specific member of the interferon regulatory factor family that binds the interferon-stimulated response element (ISRE)
Matsuyama, T., Grossman, A., Mittrücker, H.-W., Siderovski, D. P., Kiefer, F., Kawakami, T., Richardson, C. D., Taniguchi, T., Yoshinaga, S. K., & Mak, T. W. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.12.2127 · Cited by 232 · see citing works
The role of the κ enhancer and its binding factor NF-κB in the developmental regulation of κ gene transcription
Atchison, M. L., & Perry, R. P. (1987) · Cell · doi:10.1016/0092-8674(87)90362-x · Cited by 232 · see citing works
Self-citation
Regulation of lymphoid-specific immunoglobulin mu heavy chain gene enhancer by ETS-domain proteins
Nelsen, B., Tian, G., Erman, B., Gregoire, J., Maki, R., Graves, B., & Sen, R. (1993) · Science · doi:10.1126/science.8316859 · Cited by 222 · see citing works
EGR3, a novel member of the Egr family of genes encoding immediate-early transcription factors.
Patwardhan, S., Gashler, A., Mg, S., Chang, L. C., Joseph, L. J., Shows, T. B., Beau, M. M. L., & Sukhatme, V. P. (1991) · PubMed · Cited by 220 · see citing works
The immunoglobulin kappa locus contains a second, stronger B‐cell‐specific enhancer which is located downstream of the constant region.
Meyer, K. B., & Neuberger, M. S. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03601.x · Cited by 214 · see citing works
A Novel Interferon Regulatory Factor Family Transcription Factor, ICSAT/Pip/LSIRF, That Negatively Regulates the Activity of Interferon-Regulated Genes
Yamagata, T., Nishida, J., Tanaka, T., Sakai, R., Mitani, K., Yoshida, M., Taniguchi, T., Yazaki, Y., & Hirai, H. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1283 · Cited by 196 · see citing works
Interferon consensus sequence-binding protein, a member of the interferon regulatory factor family, suppresses interferon-induced gene transcription.
Nelson, N., Marks, M. S., Driggers, P. H., & Ozato, K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.588 · Cited by 192 · see citing works
Interferon Consensus sequence-Binding Protein, a Member of the Interferon Regulatory Factor Family, Suppresses Interferon-Induced Gene Transcription
Nelson, N., Marks, M. S., Driggers, P. H., & Ozato, K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.588-599.1993 · Cited by 192 · see citing works
PU.1 is a component of a multiprotein complex which binds an essential site in the murine immunoglobulin lambda 2-4 enhancer.
Eisenbeis, C. F., Singh, H., & Storb, U. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.10.6452 · Cited by 182 · see citing works
B-Cell-Specific DNA Binding by an E47 Homodimer
Shen, C.-P., & Kadesch, T. R. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4518 · Cited by 180 · 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
Molecular interactions between interferon consensus sequence binding protein and members of the interferon regulatory factor family.
Bovolenta, C., Driggers, P. H., Marks, M. S., Medin, J. A., Politis, A. D., Vogel, S. N., Levy, D. E., Sakaguchi, K., Appella, E., & Coligan, J. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.5046 · Cited by 167 · see citing works
Phosphorylation Events Modulate the Ability of Interferon Consensus Sequence Binding Protein to Interact with Interferon Regulatory Factors and to Bind DNA
Sharf, R., Meraro, D., Azriel, A., Thornton, A. M., Ozato, K., Petricoin, E. F., Larner, A. C., Schaper, F., Hauser, H., & Levi, B.-Z. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.9785 · Cited by 162 · see citing works
B-Cell- and Myocyte-Specific E2-Box-Binding Factors Contain E12/E47-Like Subunits
Murre, C., Voronova, A., & Baltimore, D. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.2.1156-1160.1991 · Cited by 161 · see citing works
Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84).
Shaknovich, R., Shue, G., & Kohtz, D. S. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5059 · Cited by 154 · see citing works
E2A and E2-2 are Subunits of B-Cell-Specific E2-Box DNA-Binding Proteins
Bain, G., Gruenwald, S., & Murre, C. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3522-3529.1993 · Cited by 149 · see citing works
Characterization of Functional Domains within the Multifunctional Transcription Factor, YY1
Bushmeyer, S., Park, K., & Atchison, M. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.50.30213 · Cited by 145 · see citing works
Self-citation
Repression of Immunoglobulin Enhancers by the Helix-Loop-Helix Protein Id: Implications for B-Lymphoid-Cell Development
Wilson, R. B., Kiledjian, M., Shen, C.-P., Benezra, R., Zwollo, P., Dymecki, S. M., Desiderio, S. V., & Kadesch, T. R. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.12.6185 · Cited by 145 · see citing works
A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-IPreprint
Grueneberg, D. A., Henry, R. W., Brauer, A. W., Novina, C. D., Cheriyath, V., Roy, A. L., & Gilman, M. (1997) · Genes & Development · doi:10.1101/gad.11.19.2482 · Cited by 131 · see citing works
Functional Characterization of the Developmentally Controlled Immunoglobulin Kappa 3′ Enhancer: Regulation by Id, a Repressor of Helix-Loop-Helix Transcription Factors
Pongubala, J. M. R., & Atchison, M. L. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.2.1040 · Cited by 123 · see citing works
Self-citation
PU.1 Recruits a Second Nuclear Factor to a Site Important for Immunoglobulin κ 3' Enhancer Activity
Pongubala, J. M. R., Nagulapalli, S., Klemsz, M. J., McKercher, S. R., Maki, R. A., & Atchison, M. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.1.368-378.1992 · Cited by 105 · see citing works
Self-citation
Functional Domain Analysis of Interferon Consensus Sequence Binding Protein (ICSBP) and Its Association with Interferon Regulatory Factors
Sharf, R., Azriel, A., Lejbkowicz, F., Winograd, S. S., Ehrlich, R., & Levi, B.-Z. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13063 · Cited by 100 · see citing works
An intermolecular disulfide bond stabilizes E2A homodimers and is required for DNA binding at physiological temperatures
Benezra, R. (1994) · Cell · doi:10.1016/0092-8674(94)90036-1 · Cited by 100 · see citing works
Ets Proteins: New Factors That Regulate Immunoglobulin Heavy-Chain Gene Expression
Rivera, R. R., Stuiver, M. H., Steenbergen, R. D. M., & Murre, C. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.11.7163 · Cited by 99 · see citing works
Phosphorylation of E47 as a Potential Determinant of B-Cell-Specific Activity
Sloan, S. R., Shen, C.-P., McCarrick-Walmsley, R., & Kadesch, T. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.6900 · Cited by 98 · see citing works
HEB, a Helix-Loop-Helix Protein Related to E2A and ITF2 That Can Modulate the DNA-Binding Ability of Myogenic Regulatory Factors
Hu, J., Olson, E. N., & Kingston, R. E. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.1031-1042.1992 · Cited by 94 · see citing works
Transcriptional Synergy between LIM-Homeodomain Proteins and Basic Helix-Loop-Helix Proteins: the LIM2 Domain Determines Specificity
Johnson, J. D., Zhang, W., Rudnick, A., Rutter, W. J., & German, M. S. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.7.3488 · Cited by 92 · see citing works
PU.1 can participate in an active enhancer complex without its transcriptional activation domain
Pongubala, J. M. R., & Atchison, M. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.1.127 · Cited by 86 · see citing works
Self-citation
Cloning of Human Lymphocyte-Specific Interferon Regulatory Factor (hLSIRF/hIRF4) and Mapping of the Gene to 6p23–p25
Grossman, A., Mittrücker, H.-W., Nicholl, J. K., Suzuki, A., Chung, S., Antonio, L., Suggs, S., Sutherland, G. R., Siderovski, D. P., & Mak, T. W. (1996) · Genomics · doi:10.1006/geno.1996.0547 · Cited by 76 · see citing works
Repression of Immunoglobulin Enhancers by the Helix-Loop-Helix Protein Id: Implications for B-Lymphoid-Cell Development
Wilson, R. B., Kiledjian, M., Shen, C.-P., et al. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.12.6185-6191.1991 · Cited by 43 · see citing works
Functional Characterization of the Developmentally Controlled Immunoglobulin Kappa 3′ Enhancer: Regulation by Id, a Repressor of Helix-Loop-Helix Transcription Factors
Pongubala, J. M. R., & Atchison, M. L. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.2.1040-1047.1991 · Cited by 39 · see citing works
Self-citation
Activating Transcription Factor 1 and Cyclic AMP Response Element Modulator Can Modulate the Activity of the Immunoglobulin κ 3′ Enhancer
Pongubala, J. M. R., & Atchison, M. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.10304 · Cited by 38 · see citing works
Self-citation
PU.1 is a Component of a Multiprotein Complex Which Binds an Essential Site in the Murine Immunoglobulin λ2-4 Enhancer
Eisenbeis, C. F., Singh, H., & Storb, U. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.10.6452-6461.1993 · Cited by 38 · see citing works
Kappa immunoglobulin promoters and enhancers display developmentally controlled interactions
Fulton, R. S., & Ness, B. V. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.21.4941 · Cited by 37 · see citing works
Selective synergy of immunoglobulin enhancer elements in B-cell development: a characteristic of kappa light chain enhancers, but not heavy chain enhancers.
Fulton, R., & Ness, B. V. V. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.20.4216 · Cited by 27 · see citing works
Ets Proteins: New Factors That Regulate Immunoglobulin Heavy-Chain Gene Expression
Rivera, R. R., Stuiver, M. H., Steenbergen, R. D. M., et al. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.11.7163-7169.1993 · Cited by 27 · see citing works
Conformational Activation of a Basic Helix-Loop-Helix Protein (MyoDl) by the C-Terminal Region of Murine HSP90 (HSP84)
Shaknovich, R., Shue, G., & Kohtz, D. S. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5059-5068.1992 · Cited by 27 · see citing works
Lymphopoiesis: Transcription factors controlling B-cell development
Desiderio, S. V. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00121-7 · Cited by 20 · see citing works

Flagged first, then by citations

Sorted by citations

Interferon regulatory factors: the next generation
Mamane, Y., Heylbroeck, C., Génin, P., Algarté-Génin, M., Servant, M. J., Page, C. L., DeLuca, C., Kwon, H., Lin, R., & Hiscott, J. B. (1999) · Gene · doi:10.1016/s0378-1119(99)00262-0 · Cited by 570 · see citing works
Graded Expression of Interferon Regulatory Factor-4 Coordinates Isotype Switching with Plasma Cell Differentiation
Sciammas, R., Shaffer, A. L., Schatz, J. H., Zhao, H., Staudt, L. M., & Singh, H. (2006) · Immunity · doi:10.1016/j.immuni.2006.07.009 · Cited by 564 · see citing works
Interferon Regulatory Factor 4 (IRF4) Interacts with NFATc2 to Modulate Interleukin 4 Gene Expression
Rengarajan, J., Mowen, K. A., McBride, K. D., Smith, E. D., Singh, H., & Glimcher, L. H. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20011128 · Cited by 332 · see citing works
E and ID proteins branch out
Kee, B. L. (2009) · Nature reviews. Immunology · doi:10.1038/nri2507 · Cited by 308 · see citing works
IRF4: Immunity. Malignancy! Therapy?
Shaffer, A. L., Emre, N. C. T., Romesser, P. B., & Staudt, L. M. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1845 · Cited by 189 · see citing works
Regulation of the germinal center gene program by interferon (IFN) regulatory factor 8/IFN consensus sequence-binding protein
Lee, C. H., Melchers, M., Wang, H., Torrey, T. A., Slota, R., Qi, C., Kim, J. Y., Lugar, P., Kong, H. J., Farrington, L. A., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051450 · Cited by 186 · see citing works
Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells
Tamura, T., & Ozato, K. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452755 · Cited by 183 · see citing works
Protein-Protein and DNA-Protein Interactions Affect the Activity of Lymphoid-Specific IFN Regulatory Factors
Meraro, D., Hashmueli, S., Koren, B., Azriel, A., Oumard, A., Kirchhoff, S., Hauser, H., Nagulapalli, S., Atchison, M. L., & Levi, B.-Z. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.12.6468 · Cited by 147 · see citing works
Self-citation
The diverse roles of IRF4 in late germinal center B‐cell differentiation
Silva, N. S. D., Simonetti, G., Heise, N., & Klein, U. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01113.x · Cited by 141 · see citing works
IRF8 regulates B-cell lineage specification, commitment, and differentiation
Wang, H., Lee, C. H., Qi, C., Tailor, P. B., Feng, J., Abbasi, S., Atsumi, T., & Morse, H. C. (2008) · Blood · doi:10.1182/blood-2008-01-129049 · Cited by 140 · see citing works
The IgH Locus 3′ Regulatory Region
Pinaud, E., Marquet, M., Fiancette, R., Péron, S., Vincent‐Fabert, C., Denizot, Y., & Cogné, M. (2011) · Advances in immunology · doi:10.1016/b978-0-12-387663-8.00002-8 · Cited by 134 · see citing works
Lineage-Specific Modulation of Interleukin 4 Signaling by Interferon Regulatory Factor 4
Gupta, S. K., Jiang, M., Anthony, A., & Pernis, A. B. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1837 · Cited by 128 · see citing works
IRF8 regulates myeloid and B lymphoid lineage diversification
Wang, H., & Morse, H. C. (2008) · Immunologic Research · doi:10.1007/s12026-008-8055-8 · Cited by 121 · see citing works
Interferon regulatory factors 4 and 8 induce the expression of Ikaros and Aiolos to down-regulate pre–B-cell receptor and promote cell-cycle withdrawal in pre–B-cell development
Ma, S., Pathak, S., Trinh, L. X., & Lu, R. (2007) · Blood · doi:10.1182/blood-2007-08-110106 · Cited by 117 · see citing works
Interferon regulatory factor 4 and 8 in B-cell development
Lu, R. (2008) · Trends in Immunology · doi:10.1016/j.it.2008.07.006 · Cited by 111 · see citing works
IFN-Stimulated Gene 15 Is Synergistically Activated Through Interactions Between the Myelocyte/Lymphocyte-Specific Transcription Factors, PU.1, IFN Regulatory Factor-8/IFN Consensus Sequence Binding Protein, and IFN Regulatory Factor-4: Characterization of a New Subtype of IFN-Stimulated Response Element
Meraro, D., Gleit-Kielmanowicz, M., Hauser, H., & Levi, B.-Z. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.12.6224 · Cited by 105 · see citing works
Spurious transcription factor binding: Non‐functional or genetically redundant?
Spivakov, M. (2014) · BioEssays · doi:10.1002/bies.201400036 · Cited by 96 · see citing works
IFN Regulatory Factor 4 and 8 Promote Ig Light Chain κ Locus Activation in Pre-B Cell Development
Ma, S., Turetsky, A., Trinh, L. X., & Lu, R. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7898 · Cited by 95 · see citing works
Differential Expression and Distinct Functions of IFN Regulatory Factor 4 and IFN Consensus Sequence Binding Protein in Macrophages
Marecki, S., Atchison, M. L., & Fenton, M. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.5.2713 · Cited by 87 · see citing works
Self-citation
Regulation of human β2-microglobulin transactivation in hematopoietic cells
Gobin, S. J. P., Biesta, P. J., & van den Elsen, P. J. (2003) · Blood · doi:10.1182/blood-2002-09-2924 · Cited by 86 · see citing works
Transcription Factors IRF8 and PU.1 Are Required for Follicular B Cell Development and BCL6‐driven Germinal Center Responses
Wang, H., Jain, S., Li, P., Lin, J.-X., Oh, J., Qi, C., Gao, Y., Sun, J., Sakai, T., Naghashfar, Z., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901258116 · Cited by 81 · see citing works
The Basic Helix-Loop-Helix Factor, HAND2, Functions as a Transcriptional Activator by Binding to E-boxes as a Heterodimer
Dai, Y., & Cserjesi, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200283200 · Cited by 76 · see citing works
Transcriptional control of B cell development and function
Bartholdy, B., & Matthias, P. (2003) · Gene · doi:10.1016/j.gene.2003.11.008 · Cited by 75 · see citing works
Overlapping Expression of Early B-Cell Factor and Basic Helix-Loop-Helix Proteins as a Mechanism To Dictate B-Lineage-Specific Activity of the λ 5 Promoter
Sigvardsson, M. (2000) · Molecular and Cellular Biology · doi:10.1128/.20.10.3640-3654.2000 · Cited by 70 · see citing works
Review: ICSBP/IRF-8 Transactivation: A Tale of Protein-Protein Interaction
Levi, B.-Z., Hashmueli, S., Gleit-Kielmanowicz, M., Azriel, A., & Meraro, D. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452764 · Cited by 70 · see citing works
E2A and IRF-4/Pip Promote Chromatin Modification and Transcription of the Immunoglobulin κ Locus in Pre-B Cells
Lazorchak, A. S., Schlissel, M. S., & Zhuang, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.3.810-821.2006 · Cited by 68 · see citing works
Review: The Role of IRF-4 in B and T Cell Activation and Differentiation
Pernis, A. B. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452728 · Cited by 62 · see citing works
IFN Regulatory Factor 8 Mediates Apoptosis in Nonhemopoietic Tumor Cells via Regulation of Fas Expression
Yang, D., Thangaraju, M., Browning, D. D., Dong, Z., Korchin, B., Lev, D. C., Ganapathy, V., & Liu, K. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.7.4775 · Cited by 55 · see citing works
Aberrant expression of ETS1 and ETS2 proteins in cancer
Fry, E. A., & Inoue, K. (2018) · Cancer Reports and Reviews · doi:10.15761/crr.1000151 · Cited by 52 · see citing works
Interferon regulatory factor 4 differentially regulates the production of Th2 cytokines in naïve vs. effector/memory CD4 + T cells
Honma, K., Kimura, D., Tominaga, N., Miyakoda, M., Matsuyama, T., & Yui, K. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803171105 · Cited by 50 · see citing works
Transcriptional Control of Mature B Cell Fates
Wang, H., Morse, H. C., & Bolland, S. M. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.04.011 · Cited by 48 · see citing works
Interaction between Interferon Consensus Sequence-binding Protein and COP9/Signalosome Subunit CSN2 (Trip15)
Cohen, H., Azriel, A., Cohen, T., Meraro, D., Hashmueli, S., Bech-Otschir, D., Kraft, R., Dubiel, W., & Levi, B.-Z. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004900200 · Cited by 45 · see citing works
B-cell receptor activation inhibits AID expression through calmodulin inhibition of E-proteins
Hauser, J., Sveshnikova, N., Wallenius, A., Baradaran, S., Saarikettu, J., & Grundström, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708220105 · Cited by 45 · see citing works
Rapid structural and epigenetic changes in polyploid and aneuploid genomes
Matzke, M. A., Scheid, O. M., & Matzke, A. J. M. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199909)21:9 · Cited by 151 · see citing works
Physical Interaction and Functional Synergy between Glucocorticoid Receptor and Ets2 Proteins for Transcription Activation of the Rat Cytochrome P-450c27 Promoter
Mullick, J., Anandatheerthavarada, H. K., Amuthan, G., Bhagwat, S. V., Biswas, G., Vijayasarathy, C., BHAT, N. K., Reddy, S. E. P., Rao, V. N., & Avadhani, N. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100671200 · Cited by 44 · see citing works
Preventing AID, a physiological mutator, from deleterious activation: regulation of the genomic instability that is associated with antibody diversity
Nagaoka, H., Tran, T. H., Kobayashi, M., Aida, M., & Honjo, T. (2010) · International Immunology · doi:10.1093/intimm/dxq023 · Cited by 42 · see citing works
Imipramine Exploits Histone Deacetylase 11 To Increase the IL-12/IL-10 Ratio in Macrophages Infected with Antimony-Resistant Leishmania donovani and Clears Organ Parasites in Experimental Infection
Mukherjee, S., Mukherjee, B., Mukhopadhyay, R., Naskar, K., Sundar, S., Dujardin, J., & Roy, S. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400710 · Cited by 41 · see citing works
Specificity and Function of IRF Family Transcription Factors: Insights from Genomics
Mancino, A., & Natoli, G. (2016) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2016.0004 · Cited by 39 · see citing works
Protein Acetylation Regulates Both PU.1 Transactivation and Igκ 3′ Enhancer Activity
Bai, Y., Srinivasan, L., Perkins, L., & Atchison, M. L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.8.5160 · Cited by 38 · see citing works
Self-citation
Interferon Regulatory Factor 4 Contributes to Transformation of v-Rel-Expressing Fibroblasts
Hrdličková, R., Nehyba, J., & Bose, H. R. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.19.6369-6386.2001 · Cited by 35 · see citing works
Repression of IRF-4 target genes in human T cell leukemia virus-1 infection
Mamane, Y., Grandvaux, N., Hernandez, E., Sharma, S., Innocente, S. A., Lee, J. M., Azimi, N., Lin, R., & Hiscott, J. B. (2002) · Oncogene · doi:10.1038/sj.onc.1205843 · Cited by 35 · see citing works
Dynamic Control of Long-Range Genomic Interactions at the Immunoglobulin κ Light-Chain Locus
de Almeida, C. R., Hendriks, R. W., & Stadhouders, R. (2015) · Advances in immunology · doi:10.1016/bs.ai.2015.07.004 · Cited by 33 · see citing works
A Role for Interferon Regulatory Factor 4 in Receptor Editing
Pathak, S., Ma, S., Trinh, L., & Lu, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01946-07 · Cited by 33 · see citing works
Regulation of Lymphocyte Apoptosis by Interferon Regulatory Factor 4 (IRF-4)
Fanzo, J., Hu, C.-M., Jang, S. Y., & Pernis, A. B. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20020717 · Cited by 31 · see citing works
PU.1 Can Recruit BCL6 to DNA To Repress Gene Expression in Germinal Center B Cells
Wei, F., Zápražná, K., Wang, J., & Atchison, M. L. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00234-09 · Cited by 30 · see citing works
Self-citation
Review: IRF-4 Activities in HTLV-I-Induced T Cell Leukemogenesis
Mamane, Y., Sharma, S., Grandvaux, N., Hernandez, E., & Hiscott, J. B. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452746 · Cited by 28 · see citing works
PU.1 as a chromatin accessibility factor for immunoglobulin genes
Marecki, S., McCarthy, K. M., & Nikolajczyk, B. S. (2004) · Molecular Immunology · doi:10.1016/j.molimm.2003.08.007 · Cited by 25 · see citing works
A Synchronous IRF4-Dependent Gene Regulatory Network in B and Helper T Cells Orchestrating the Antibody Response
Cook, S. L., Franke, M. C., Sievert, E. P., & Sciammas, R. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.05.001 · Cited by 24 · see citing works
Active repression of IFN regulatory factor-1-mediated transactivation by IFN regulatory factor-4
Yoshida, K., Yamamoto, K., Kohno, T., Hironaka, N., Yasui, K., Kojima, C., Mukae, H., Kadota, J., Suzuki, S., Honma, K., et al. (2005) · International Immunology · doi:10.1093/intimm/dxh324 · Cited by 24 · see citing works
Mechanism of E47-Pip Interaction on DNA Resulting in Transcriptional Synergy and Activation of Immunoglobulin Germ Line Sterile Transcripts
Nagulapalli, S., Goheer, A., Pitt, L. K., McIntosh, L. P., & Atchison, M. L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7337-7350.2002 · Cited by 20 · see citing works
Self-citation
Regulation of Class Switch Recombination
Cogné, M., & Birshtein, B. K. (2004) · Elsevier eBooks · doi:10.1016/b978-012053641-2/50020-4 · Cited by 19 · see citing works
Transcription factors PU.1 and IRF4 regulate activation induced cytidine deaminase in chicken B cells
Luo, H., & Tian, M. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.02.016 · Cited by 15 · see citing works
Calmodulin inhibition of E2A stops expression of surrogate light chains of the pre-B-cell receptor and CD19
Hauser, J., Wallenius, A., Sveshnikova, N., Saarikettu, J., & Grundström, T. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.11.015 · Cited by 14 · see citing works
Transcription of Immunoglobulin Genes
Calame, K. L., & Sen, R. (2004) · Elsevier eBooks · doi:10.1016/b978-012053641-2/50007-1 · Cited by 11 · see citing works
The Roles of IRF-8 in Regulating IL-9-Mediated Immunologic Mechanisms in the Development of DLBCL: A State-of-the-Art Literature Review
Cai, M., & Chen, N. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.817069 · Cited by 10 · see citing works
A Developmentally Controlled Competitive STAT5–PU.1 DNA Binding Mechanism Regulates Activity of the Ig κE3′ Enhancer
Hodawadekar, S., Park, K., Farrar, M. A., & Atchison, M. L. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102239 · Cited by 10 · see citing works
Self-citation
A truncated IFN-regulatory factor-8\IFN consensus sequence-binding protein acts as dominant-negative, interferes with endogenous protein-protein interactions and leads to apoptosis of immune cells
Hashmueli, S. (2003) · International Immunology · doi:10.1093/intimm/dxg077 · Cited by 9 · see citing works
Epigenetic Histone Modifications Do Not Control Igκ Locus Contraction and Intranuclear Localization in Cells with Dual B Cell-Macrophage Potential
Hodawadekar, S., Wei, F., Yu, D., Thomas‐Tikhonenko, A., & Atchison, M. L. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.9.6165 · Cited by 7 · see citing works
Self-citation
Helix-Loop-Helix Proteins in Adaptive Immune Development
Aubrey, M., Warburg, Z. J., & Murre, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.881656 · Cited by 5 · see citing works
Transcriptional Regulation of Early B-Cell Development
Ng, A. P., Morris, R., & Nutt, S. L. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95895-0.00014-3 · Cited by 2 · see citing works
Chapter 7 – DNA Sequence-Specific Transcription Factors
Auron, P. (2005) · Elsevier eBooks · doi:10.1016/b978-012455900-4/50269-5 · Cited by 2 · see citing works
The Molecular Basis of B Cell Development and the Role of Deregulated Transcription and Epigenetics in Leukaemia and Lymphoma
Kirkham, C. M., Scott, J. N., Boyes, J., & Bevington, S. L. (2014) · Epigenetics and human health · doi:10.1007/978-3-642-45198-0_13
IRF- 1 and IRF-4 Regulate Target Gene Expression via Interaction with DMP 1
Yamamoto, Y., Yamamoto, K., Yoshida, K., Kohno, T., Nogi, Y., & Matsuyama, T. (2003) · Nagasaki University's Academic Output SITE (Nagasaki University)
A Role of IRF8 in Transcriptional Control of B-Cell Development
Wang, H., Lee, C. H., & Morse, H. C. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-512-5_25
Epigenetic regulation of gene transcription in hematopoietic tumors.
Tshuikina, M. (2008) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Mechanism of E47-Pip Interaction on DNA Resulting in Transcriptional Synergy and Activation of Immunoglobulin Germ Line Sterile Transcripts
Nagulapalli, S., Goheer, A., Pitt, L. K., McIntosh, L. P., & Atchison, M. L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7337-7350.2002 · Cited by 20 · see citing works
Self-citation
Transcriptional Synergy and Activation of Immunoglobulin Germ Line Sterile Transcripts
Atchison, M., & Atchison, M. L. (2002)
Self-citation
A Two-Step Mechanism for Recruitment of Pip by PU.1
Perkel, J. M., & Atchison, M. L. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.1.241 · Cited by 77 · see citing works
Self-citation
Analysis of the physical interactions between PU.1 and Pip, two immunoglobulin kappa 3' enhancer binding proteins
Perkel, J. M. (1997) · Scholarly Commons (University of Pennsylvania)
Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.
Eisenbeis, C. F., Singh, H., & Storb, U. (1995) · Genes & Development · doi:10.1101/gad.9.11.1377 · Cited by 447 · see citing works

Authors: Nagulapalli, S., & Atchison, M. L.
Affiliations: University of Pennsylvania (US)
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1998-08
Volume: 18
Issue: 8
Pages: 4639-4650
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.18.8.4639
PMC: PMC109050
OpenAlex: W2129093323
Cited by: 66
References: 69
Citations by year: 2024: 1 · 2022: 2 · 2020: 2 · 2019: 1 · 2018: 1 · 2016: 1 · 2015: 1 · 2014: 3 · 2012: 2
FWCI: 1.16
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM-42415, R01GM042415)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords: E47, E2A, transcriptional synergy, DNA binding, enhancer activity, PU.1, B cell development, protein-protein interaction, transcriptional activation, protein conformational change
MeSH terms: Interferon Regulatory Factor-8, Interferon Regulatory Factor-4, Animals, Binding Sites, DNA-Binding Proteins, Enhancer Elements, Genetic, Immunoglobulin kappa-Chains, Recombinant Fusion Proteins, Repressor Proteins, Structure-Activity Relationship, Transcription Factors, Transcription, Genetic, Tumor Cells, Cultured, Transcriptional Activation, Trans-Activators, 3T3 Cells, Interferon Regulatory Factors, Mice, TCF Transcription Factors, Transcription Factor 7-Like 1 Protein

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Transcription Factor Pip Can Enhance DNA Binding by E47, Leading to Transcriptional Synergy Involving Multiple Protein Domains

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks