Cited by 347

The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.

Human Mediator Subunit MED26 Functions as a Docking Site for Transcription Elongation Factors

Open access

Takahashi, Hidehisa, Parmely, Tari J., Sato, Shigeo, Tomomori-Sato, Chieri, Banks, Charles A.S., Kong, Stephanie E., Szutorisz, Henrietta, Swanson, Selene K., Martin-Brown, Skylar, Washburn, Michael P., Florens, Laurence, Seidel, Chris W., Lin, Chengqi, Smith, Edwin R., Shilatifard, Ali, Conaway, Ronald C., Conaway, Joan W.·2011·Cell

DOI 10.1016/j.cell.2011.06.005

Open this paper in CoChat — free account

Abstract

Summary Promoter proximal pausing by initiated RNA polymerase II (Pol II) and regulated release of paused polymerase into productive elongation has emerged as a major mechanism of transcription activation. Reactivation of paused Pol II correlates with recruitment of SuperElongationComplexes (SECs) containing ELL/EAF family members, P-TEFb, and other proteins, but the mechanism of their recruitment is currently a major unanswered question. Here, we present evidence for a role of human Mediator subunit Med26 in this process. We identify in the conserved N-terminal domain of Med26 overlapping docking sites for SEC and a second ELL/EAF-containing complex, as well as general initiation factor TFIID. In addition, we present evidence consistent with the model that Med26 can function as a molecular switch that interacts first with TFIID in the Pol II initiation complex and then exchanges TFIID for complexes containing ELL/EAF and P-TEFb to facilitate transition of Pol II into the elongation stage of transcription.

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 · 10.1016/j.cell.2011.06.005

Cites

74 of 74 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.

Self-check

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

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

Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482
Linear Models and Empirical Bayes Methods for Assessing Differential Expression in Microarray Experiments
Smyth, G. K. (2004) · Statistical Applications in Genetics and Molecular Biology · doi:10.2202/1544-6115.1027 · Cited by 11,829
Exploration, normalization, and summaries of high density oligonucleotide array probe level data
Irizarry, R. A. (2003) · Biostatistics · doi:10.1093/biostatistics/4.2.249 · Cited by 10,603
An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
Eng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484
Large-scale analysis of the yeast proteome by multidimensional protein identification technology
Washburn, M. P., Wolters, D., & Yates, J. R. (2001) · Nature Biotechnology · doi:10.1038/85686 · Cited by 4,752
Self-citation
A Chromatin Landmark and Transcription Initiation at Most Promoters in Human Cells
Guenther, M. G., Levine, S. S., Boyer, L. A., Jaenisch, R., & Young, R. A. (2007) · Cell · doi:10.1016/j.cell.2007.05.042 · Cited by 1,944
DTASelect and Contrast: Tools for Assembling and Comparing Protein Identifications from Shotgun Proteomics
Tabb, D. L., McDonald, W. H., & Yates, J. R. (2002) · Journal of Proteome Research · doi:10.1021/pr015504q · Cited by 1,367
c-Myc Regulates Transcriptional Pause Release
Rahl, P. B., Lin, C. Y., Seila, A. C., Flynn, R. A., McCuine, S., Burge, C. B., Sharp, P. A., & Young, R. A. (2010) · Cell · doi:10.1016/j.cell.2010.03.030 · Cited by 1,279
Self-citation
A Novel CDK9-Associated C-Type Cyclin Interacts Directly with HIV-1 Tat and Mediates Its High-Affinity, Loop-Specific Binding to TAR RNA
Wei, P., Garber, M. E., Fang, S.-M., Fischer, W. H., & Jones, K. A. (1998) · Cell · doi:10.1016/s0092-8674(00)80939-3 · Cited by 1,249
Controlling the elongation phase of transcription with P-TEFb
Peterlin, B. M., & Price, D. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.014 · Cited by 1,144
A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II
Kim, Y.-J., Björklund, S., Li, Y., Sayre, M. H., & Kornberg, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90221-6 · Cited by 1,090
Statistical Analysis of Membrane Proteome Expression Changes in Saccharomyces cerevisiae
Zybailov, B., Mosley, A. L., Sardiu, M. E., Coleman, M. K., Florens, L., & Washburn, M. P. (2006) · Journal of Proteome Research · doi:10.1021/pr060161n · Cited by 1,029
Self-citation
NELF, a Multisubunit Complex Containing RD, Cooperates with DSIF to Repress RNA Polymerase II Elongation
Yamaguchi, Y., Takagi, T., Wada, T., Yano, K., Furuya, A., Sugimoto, S., Hasegawa, J., & Handa, H. (1999) · Cell · doi:10.1016/s0092-8674(00)80713-8 · Cited by 841
Progression through the RNA Polymerase II CTD Cycle
Buratowski, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.019 · Cited by 772
RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo
Zeitlinger, J., Stark, A., Kellis, M., Hong, J.-W., Nechaev, S., Adelman, K., Levine, M., & Young, R. A. (2007) · Nature Genetics · doi:10.1038/ng.2007.26 · Cited by 765
RNA polymerase is poised for activation across the genome
Muse, G. W., Gilchrist, D. A., Nechaev, S., Shah, R., Parker, J. S., Grissom, S. F., Zeitlinger, J., & Adelman, K. (2007) · Nature Genetics · doi:10.1038/ng.2007.21 · Cited by 761
DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs
Wada, T., Takagi, T., Yamaguchi, Y., Ferdous, A., Imai, T., Hirose, S., Sugimoto, S., Yano, K., Hartzog, G. A., Winston, F., et al. (1998) · Genes & Development · doi:10.1101/gad.12.3.343 · Cited by 750
A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection
Albritton, L. M., Tseng, L., Scadden, D., & Cunningham, J. M. (1989) · Cell · doi:10.1016/0092-8674(89)90134-7 · Cited by 688
Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
Marshall, N. F., Peng, J., Xie, Z., & Price, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.27176 · Cited by 662 · cited 3×
“Promoter escape and transcript elongation by Pol II are associated with phosphorylation of the Pol II CTD by P-TEFb and other kinases (Bartkowiak et al., 2010; Buratowski, 2009; Kim et al., 2002; Marshall et al., 1996).”
An RNA polymerase II holoenzyme responsive to activators
Koleske, A. J., & Young, R. A. (1994) · Nature · doi:10.1038/368466a0 · Cited by 592
AFF4, a Component of the ELL/P-TEFb Elongation Complex and a Shared Subunit of MLL Chimeras, Can Link Transcription Elongation to Leukemia
Lin, C., Smith, E. R., Takahashi, H., Lai, K. C., Martin-Brown, S., Florens, L., Washburn, M. P., Conaway, J. W., Conaway, R. C., & Shilatifard, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.026 · Cited by 573
Self-citation
Quantitative proteomic analysis of distinct mammalian Mediator complexes using normalized spectral abundance factors
Paoletti, A. C., Parmely, T. J., Tomomori-Sato, C., Sato, S., Zhu, D., Conaway, R. C., Conaway, J. W., Florens, L., & Washburn, M. P. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606379103 · Cited by 538
Self-citation
Breaking barriers to transcription elongation
Saunders, A., Core, L. J., & Lis, J. T. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1981 · Cited by 506
Global Analysis of Short RNAs Reveals Widespread Promoter-Proximal Stalling and Arrest of Pol II in Drosophila
Nechaev, S., Fargo, D. C., dos Santos, G., Liu, L., Gao, Y., & Adelman, K. (2010) · Science · doi:10.1126/science.1181421 · Cited by 424
Transcription Regulation Through Promoter-Proximal Pausing of RNA Polymerase II
Core, L. J., & Lis, J. T. (2008) · Science · doi:10.1126/science.1150843 · Cited by 405
CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1
Bartkowiak, B., Liu, P., Phatnani, H. P., Fuda, N. J., Cooper, J. J., Price, D. H., Adelman, K., Lis, J. T., & Greenleaf, A. L. (2010) · Genes & Development · doi:10.1101/gad.1968210 · Cited by 400
HIV-1 Tat and Host AFF4 Recruit Two Transcription Elongation Factors into a Bifunctional Complex for Coordinated Activation of HIV-1 Transcription
He, N., Liu, M., Hsu, J., Xue, Y., Chou, S., Burlingame, A., Krogan, N. J., Alber, T., & Zhou, Q. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.013 · Cited by 395
Refinements to Label Free Proteome Quantitation: How to Deal with Peptides Shared by Multiple Proteins
Zhang, Y., Wen, Z., Washburn, M. P., & Florens, L. (2010) · Analytical Chemistry · doi:10.1021/ac9023999 · Cited by 385
Self-citation
HIV-1 Tat Assembles a Multifunctional Transcription Elongation Complex and Stably Associates with the 7SK snRNP
Sobhian, B., Laguette, N., Yatim, A., Nakamura, M., Levy, Y., Kiernan, R., & Benkirane, M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.012 · Cited by 381
A Higher-Order Complex Containing AF4 and ENL Family Proteins with P-TEFb Facilitates Oncogenic and Physiologic MLL-Dependent Transcription
Yokoyama, A., Lin, M., Naresh, A., Kitabayashi, I., & Cleary, M. L. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.040 · Cited by 374
CDK8 is a positive regulator of transcriptional elongation within the serum response network
Donner, A. J., Ebmeier, C. C., Taatjes, D. J., & Espinosa, J. M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1752 · Cited by 371
Comparative genomics supports a deep evolutionary origin for the large, four-module transcriptional mediator complex
Bourbon, H.-M. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn349 · Cited by 361
The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1
Ryu, S., Zhou, S., Ladurner, A. G., & Tjian, R. (1999) · Nature · doi:10.1038/17141 · Cited by 351
TFIIH-Associated Cdk7 Kinase Functions in Phosphorylation of C-Terminal Domain Ser7 Residues, Promoter-Proximal Pausing, and Termination by RNA Polymerase II
Glover-Cutter, K., Larochelle, S., Erickson, B., Zhang, C., Shokat, K., Fisher, R. P., & Bentley, D. L. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00637-09 · Cited by 350
MS1, MS2, and SQT—three unified, compact, and easily parsed file formats for the storage of shotgun proteomic spectra and identifications
McDonald, W. H., Tabb, D. L., Sadygov, R. G., MacCoss, M. J., Venable, J., Graumann, J., Johnson, J. R., Cociorva, D., & Yates, J. R. (2004) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1603 · Cited by 345
Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors
FLORENS, L., CAROZZA, M., SWANSON, S., FOURNIER, M., COLEMAN, M., WORKMAN, J., & WASHBURN, M. (2006) · Methods · doi:10.1016/j.ymeth.2006.07.028 · Cited by 344
Self-citation
Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
Yao, T., Song, L., Xu, W., DeMartino, G. N., Florens, L., Swanson, S. K., Washburn, M. P., Conaway, R. C., Conaway, J. W., & Cohen, R. E. (2006) · Nature Cell Biology · doi:10.1038/ncb1460 · Cited by 336
Self-citation
The human Mediator complex: a versatile, genome-wide regulator of transcription
Taatjes, D. J. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.02.004 · Cited by 326
An RNA Polymerase II Elongation Factor Encoded by the Human ELL Gene
Shilatifard, A., Lane, W. S., Jackson, K. W., Conaway, R. C., & Conaway, J. W. (1996) · Science · doi:10.1126/science.271.5257.1873 · Cited by 324
Self-citation
P-TEFb kinase recruitment and function at heat shock loci
Lis, J. T., Mason, P., Peng, J., Price, D. H., & Werner, J. (2000) · Genes & Development · doi:10.1101/gad.14.7.792 · Cited by 313
A Set of Consensus Mammalian Mediator Subunits Identified by Multidimensional Protein Identification Technology
Sato, S., Tomomori-Sato, C., Parmely, T. J., Florens, L., Zybailov, B., Swanson, S. K., Banks, C. A. S., Jin, J., Cai, Y., Washburn, M. P., et al. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.05.006 · Cited by 311
Self-citation
Structure, Function, and Activator-Induced Conformations of the CRSP Coactivator
Taatjes, D. J., Näär, A. M., Andel, F., Nogales, E., & Tjian, R. (2002) · Science · doi:10.1126/science.1065249 · Cited by 277
An RNA polymerase II elongation factor encoded by the human ELL gene
(1996) · Trends in Genetics · doi:10.1016/0168-9525(96)81441-7 · Cited by 276
CDK8 Is a Stimulus-Specific Positive Coregulator of p53 Target Genes
Donner, A. J., Szostek, S., Hoover, J. M., & Espinosa, J. M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.026 · Cited by 252
Coordination of Transcription, RNA Processing, and Surveillance by P-TEFb Kinase on Heat Shock Genes
Ni, Z., Schwartz, B. E., Werner, J., Suarez, J.-R., & Lis, J. T. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00526-4 · Cited by 240
Proteomic Analysis by Multidimensional Protein Identification Technology
Florens, L., & Washburn, M. P. (2006) · New and Emerging Proteomic Techniques · doi:10.1385/1-59745-026-x:159 · Cited by 240
Self-citation
Transcription Factor and Polymerase Recruitment, Modification, and Movement on dhsp70 In Vivo in the Minutes following Heat Shock
Boehm, A. K., Saunders, A., Werner, J., & Lis, J. T. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7628-7637.2003 · Cited by 212
Mediator Requirement for Both Recruitment and Postrecruitment Steps in Transcription Initiation
Wang, G., Balamotis, M. A., Stevens, J. L., Yamaguchi, Y., Handa, H., & Berk, A. J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.010 · Cited by 210
Misguided Transcriptional Elongation Causes Mixed Lineage Leukemia
Mueller, D., García-Cuéllar, M.-P., Bach, C., Buhl, S., Maethner, E., & Slany, R. K. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000249 · Cited by 203
YY1 functions with INO80 to activate transcription
Cai, Y., Jin, J., Yao, T., Gottschalk, A. J., Swanson, S. K., Wu, S., Shi, Y., Washburn, M. P., Florens, L., Conaway, R. C., et al. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1276 · Cited by 189
Self-citation
Phosphorylation of the RNA Polymerase II Carboxyl-Terminal Domain by CDK9 Is Directly Responsible for Human Immunodeficiency Virus Type 1 Tat-Activated Transcriptional Elongation
Kim, Y. K., Bourgeois, C. F., Isel, C., Churcher, M. J., & Karn, J. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4622-4637.2002 · Cited by 178
Promoter-associated Pausing in Promoter Architecture and Postinitiation Transcriptional Regulation
LIS, J. (1998) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1998.63.347 · Cited by 172
Ras Induces Mediator Complex Exchange on C/EBPβ
Mo, X., Kowenz-Leutz, E., Xu, H., & Leutz, A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00521-5 · Cited by 169
Efficient Release from Promoter-Proximal Stall Sites Requires Transcript Cleavage Factor TFIIS
Adelman, K., Marr, M. T., Werner, J., Saunders, A., Ni, Z., Andrulis, E. D., & Lis, J. T. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.028 · Cited by 168
Genome-Wide Location of the Coactivator Mediator: Binding without Activation and Transient Cdk8 Interaction on DNA
Andrau, J.-C., van de Pasch, L., Lijnzaad, P., Bijma, T., Koerkamp, M. G., van de Peppel, J., Werner, M., & Holstege, F. C. P. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.023 · Cited by 159
Human CRSP interacts with RNA polymerase II CTD and adopts a specific CTD-bound conformationPreprint
Näär, A. M., Taatjes, D. J., Zhai, W., Nogales, E., & Tjian, R. (2002) · Genes & Development · doi:10.1101/gad.987602 · Cited by 156
Mediator, Not Holoenzyme, Is Directly Recruited to the Heat Shock Promoter by HSF upon Heat Shock
Park, J. M., Werner, J. K., Kim, J. M., Lis, J. T., & Kim, Y.-J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00296-9 · Cited by 153
Transcription elongation factor ELL2 directs immunoglobulin secretion in plasma cells by stimulating altered RNA processing
Martincic, K., Alkan, S., Jarvela, A. M. C., Borghesi, L., & Milcarek, C. (2009) · Nature Immunology · doi:10.1038/ni.1786 · Cited by 146
Novel critical role of a human Mediator complex for basal RNA polymerase II transcription
Mittler, G., Kremmer, E., Timmers, H. T. M., & Meisterernst, M. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve186 · Cited by 124
A carboxyl-terminal-domain kinase associated with RNA polymerase II transcription factor delta from rat liver.
Serizawa, H., Conaway, R. C., & Conaway, J. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7476 · Cited by 121
Self-citation
Structure and TBP binding of the Mediator head subcomplex Med8–Med18–Med20
Larivière, L., Geiger, S., Hoeppner, S., Röther, S., Sträßer, K., & Cramer, P. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1143 · Cited by 119
Genome-Wide Occupancy Profile of Mediator and the Srb8-11 Module Reveals Interactions with Coding Regions
Zhu, X., Wirén, M., Sinha, I., Rasmussen, N. N., Linder, T., Holmberg, S., Ekwall, K., & Gustafsson, C. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.032 · Cited by 116
Mediator Head module structure and functional interactions
Cai, G., Imasaki, T., Yamada, K., Cardelli, F., Takagi, Y., & Asturias, F. (2010) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1757 · Cited by 108
TFIID and human mediator coactivator complexes assemble cooperatively on promoter DNAPreprint
Johnson, K. M., Wang, J., Smallwood, A., Arayata, C., & Carey, M. (2002) · Genes & Development · doi:10.1101/gad.995702 · Cited by 108
ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL
Kong, S. E., Banks, C. A. S., Shilatifard, A., Conaway, J. W., & Conaway, R. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503017102 · Cited by 93
Self-citation
Postrecruitment Regulation of RNA Polymerase II Directs Rapid Signaling Responses at the Promoters of Estrogen Target Genes
Kininis, M., Isaacs, G. D., Core, L. J., Hah, N., & Kraus, W. L. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00841-08 · Cited by 88
Complexity in Transcription Control at the Activation Domain–Mediator Interface
Balamotis, M. A., Pennella, M. A., Stevens, J. L., Wasylyk, B., Belmont, A. S., & Berk, A. J. (2009) · Science Signaling · doi:10.1126/scisignal.1164302 · Cited by 84
Structure and Function of RNA Polymerase II Elongation Factor ELL
Shilatifard, A., Haque, D., Conaway, R., & Conaway, J. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22355 · Cited by 74
Self-citation
Cyclin-Dependent Kinase 8 Positively Cooperates with Mediator To Promote Thyroid Hormone Receptor-Dependent Transcriptional Activation
Belakavadi, M., & Fondell, J. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01541-09 · Cited by 69
Structure of a Conserved Domain Common to the Transcription Factors TFIIS, Elongin A, and CRSP70
Booth, V. K., Koth, C. M., Edwards, A. M., & Arrowsmith, C. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002595200 · Cited by 66
Dynamic bookmarking of primary response genes by p300 and RNA polymerase II complexes
Byun, J. S., Wong, M., Cui, W., Idelman, G., Li, Q., Siervi, A. D., Bilke, S., Haggerty, C. M., Player, A. N., Wang, Y. H., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905469106 · Cited by 61
Regulation of the transcriptional activity of poised RNA polymerase II by the elongation factor ELL
Smith, E. R., Winter, B., Eissenberg, J. C., & Shilatifard, A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804379105 · Cited by 42
Self-citation
Promoter Influences Transcription Elongation
Montanuy, I., Torremocha, R., Hernández-Munaín, C., & Suñé, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706243200 · Cited by 34
Proteomics Reveals a Physical and Functional Link between Hepatocyte Nuclear Factor 4α and Transcription Factor IID
Takahashi, H., Martin‐Brown, S., Washburn, M. P., Florens, L. A., Conaway, J. W., & Conaway, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.017954 · Cited by 11
Self-citation

The Mediator complex: a central integrator of transcription
Allen, B. L., & Taatjes, D. J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3951 · Cited by 922
Getting up to speed with transcription elongation by RNA polymerase II
Jonkers, I., & Lis, J. T. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3953 · Cited by 876
Mammalian heat shock response and mechanisms underlying its genome-wide transcriptional regulation
Mahat, D. B., Salamanca, H. H., Duarte, F. M., Danko, C. G., & Lis, J. T. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.025 · Cited by 426
Born to run: control of transcription elongation by RNA polymerase II
Chen, F. X., Smith, E. R., & Shilatifard, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0010-5 · Cited by 447
Self-citation
Inhibitors of cyclin-dependent kinases as cancer therapeutics.
Whittaker, S. R., Mallinger, A., Workman, P., & Clarke, P. A. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.008 · Cited by 384

See all 347

Authors: Takahashi, H., Parmely, T. J., Sato, S., Tomomori-Sato, C., Banks, C. A. S., Kong, S. E., Szutorisz, H., Swanson, S. K., Martin-Brown, S., Washburn, M. P., Florens, L., Seidel, C. W., Lin, C., Smith, E. R., Shilatifard, A., Conaway, R. C., & Conaway, J. W.
Venue: Cell
Publisher: Elsevier BV
Published: 2011-07
Volume: 146
Issue: 1
Pages: 92-104
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2011.06.005
OpenAlex: W1984901090
Cited by: 347
References: 74
FWCI: 13.40
Type: journal article
Language: en
Open access: bronze

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

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Human Mediator Subunit MED26 Functions as a Docking Site for Transcription Elongation Factors

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources