DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs

Antibodies, a laboratory manual

(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262

Multiple sequence alignment with hierarchical clustering.

Corpet, F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.22.10881 · Cited by 5,575

Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer.

Frohman, M. A., Dush, M. K., & Martin, G. R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.23.8998 · Cited by 4,554

Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide-dependent protein kinase and protein kinase C

Hidaka, H., Inagaki, M., Kawamoto, S., & Sasaki, Y. (1984) · Biochemistry · doi:10.1021/bi00316a032 · Cited by 2,688

The role of general initiation factors in transcription by RNA polymerase II

ROEDER, R. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10050-5 · Cited by 1,009

Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitroPreprint

Zhu, Y., Peery, T., Peng, J., Ramanathan, Y., Marshall, N. F., Marshall, T. K., Amendt, B. A., Mathews, M. B., & Price, D. H. (1997) · Genes & Development · doi:10.1101/gad.11.20.2622 · Cited by 700

The RNA polymerase II molecule at the 5′ end of the uninduced hsp70 gene of D. melanogaster is transcriptionally engaged

Rougvie, A. E., & Lis, J. T. (1988) · Cell · doi:10.1016/s0092-8674(88)91087-2 · Cited by 680

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

Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection

Winston, F., & Carlson, M. (1992) · Trends in Genetics · doi:10.1016/0168-9525(92)90300-s · Cited by 574

Spt5 interacts genetically with Myc and is limiting for brain tumor growth in Drosophila

Hofstetter, J., Ogunleye, A. O., Kutschke, A., Buchholz, L. M., Wolf, E., Raabe, T., & Gallant, P. (2023) · Life Science Alliance · doi:10.26508/lsa.202302130 · Cited by 3

Transcription Through Chromatin

Smolle, M., & Venkatesh, S. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8624-4_11 · Cited by 3

Correction: Yeast Genetic Analysis Reveals the Involvement of Chromatin Reassembly Factors in Repressing HIV-1 Basal Transcription

Vanti, M., Gallastegui, E., Respaldiza, I., Rodríguez‐Gil, A., Gómez-Herreros, F., Jimeno-González, S., Jordan, A., & Chávez, S. (2009) · PLoS Genetics · doi:10.1371/annotation/45587774-5d7c-4023-97b0-96833be7ad9a · Cited by 3

Transcription machinery of the minimalist: comparative genomic analysis provides insights into the (de)regulated transcription mechanism of microsporidia — fungal-relative parasites

Chanarat, S. (2023) · Transcription · doi:10.1080/21541264.2023.2174765 · Cited by 3

Chromatin Regulatory Targets for Anticancer Therapeutics

Barta, P. A., Carter, T. R., & Erb, M. A. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00231 · Cited by 2

Single-cell profiling and genetic regulation of alternative polyadenylation in the human brain

Nan, J., Boix, C. A., Shi, S., Fan, X., Ni, J., Wang, K., Shuai, X., Ding, K., Wu, P., An, Y., et al. (2026) · Nature Genetics · doi:10.1038/s41588-026-02758-w · Cited by 1

Regulation of RNA transcript elongation in metazoans and its relevance to disease

Mimoso, C. A., Fianu, I., & Adelman, K. (2026) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-026-01003-w · Cited by 2

SPT5 affects the rate of mRNA degradation and physically interacts with CCR4 but does not control mRNA deadenylation

Cui, Y., Chiang, Y. C., Viswanathan, P., Lee, D. J., & Denis, C. L. (2012) · American Journal of Molecular Biology · doi:10.4236/ajmb.2012.21002 · Cited by 2

Promoting Gene Therapy: Expression Systems for Iransgenes and Post-transcriptional Gene Silencing

Unwalla, H. J., & Rossi, J. J. (2006) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.2006.10648079 · Cited by 2

Role of NELF‑B in supporting epithelial‑mesenchymal transition and cell proliferation during hepatocellular carcinoma progression

Ghouraba, M., Masad, R. J., Mpingirika, E. Z., Abdelraheem, O. M., Zeghlache, R., Alserw, A. M., & Amleh, A. (2021) · Oncology Letters · doi:10.3892/ol.2021.13022 · Cited by 2

NDF/GLYR1 Promotes RNA Polymerase II Processivity via Pol II Binding and Nucleosome Destabilization

Li, Z., & Fei, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104874 · Cited by 2

Expression of an RNA glycosidase inhibits HIV-1 transactivation of transcription

Kutky, M., & Hudak, K. A. (2017) · Biochemical Journal · doi:10.1042/bcj20170353 · Cited by 2

Dynamic regulation of promoter-proximal RNA polymerase II pausing

Guo, C., Luo, Z., & Lin, C. (2020) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2020-0581 · Cited by 2

Transcription Elongation Factors in Health and Disease

Dabas, P. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.103013 · Cited by 2

Molecular Mechanisms of AID Function

Begum, N. A., Nagaoka, H., Kobayashi, M., & Honjo, T. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397933-9.00018-7 · Cited by 3

Transcription Termination by RNA Polymerase II

Kim, M., & Buratowski, S. (2013) · doi:10.1002/9783527665433.ch2 · Cited by 2

Chromatin transcription: Clearing the gridlock

Geiduschek, E. P. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70240-4 · Cited by 2

Enhancers predominantly regulate gene expression in vivo via transcription initiationPreprint

Larke, M., Nojima, T., Telenius, J. M., Sharpe, J. A., Sloane-Stanley, J. A., Butler, S., Beagrie, R. A., Downes, D. J., Schweßinger, R., Oudelaar, A. M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/844191 · Cited by 2

Establishment of a Human RNA Pol II Pausing System and the Identification of O-GlcNAc Cycling Regulating Pol II Pausing and ElongationPreprint

Lewis, B. A., & Levens, D. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.23.917237 · Cited by 2

Type I PRMTs and PRMT5 Independently Regulate Both snRNP Arginine Methylation and Post-Transcriptional SplicingPreprint

Maron, M. I., Burgos, E. S., Gupta, V., Casill, A. D., Kosmyna, B., Chen, H., Gamble, M. J., Query, C. C., & Shechter, D. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.18.389288 · Cited by 2

A sequence-encoded promoter proximal super pause stabilizes an offline RNA polymerase II statePreprint

Nunez, R. J. V., Kesha, S., & Vos, S. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.18.706689 · Cited by 2

Glc7/PP1 triggers Paf1 complex dissociation from RNA polymerase II to enable transcription terminationPreprint

Namjilsuren, S., & Arndt, K. M. (2026) · Genes & Development · doi:10.1101/gad.353379.125 · Cited by 2

ELOF1 is a core component of the promoter-proximal paused RNA polymerase II complexPreprint

Nunez, R. J. V., Bressin, A., Shao, Z., Mayer, A., & Vos, S. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.26.728003 · Cited by 2

Transcriptional pause release at enhancers mediates cell identity

Ekstrom, T. L., & Johnsen, S. A. (2025) · NAR Cancer · doi:10.1093/narcan/zcaf039 · Cited by 1

Design of Space-Filling Antennas for Passive UHF RFID Tags

Benjamin, D., Gregory, J., & Robert, M. (2010) · InTech eBooks · doi:10.5772/7970 · Cited by 1

Phosphoserines of the Carboxy Terminal Domain of RNA Polymerase II Are Involved in the Interaction with Transcription-Associated Proteins (TAPs)

Vidyalakshmi, S., & Ramamurthy, V. (2013) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2012.0081 · Cited by 1

Transcriptional Regulation by HSF

Fujimoto, M. (2016) · Springer eBooks · doi:10.1007/978-4-431-55852-1_4 · Cited by 1

Mechanism and Regulation of Immunoglobulin Class Switch Recombination

Meng, F., Nair, L., Fernandez, K. C., Basu, U., & Chaudhuri, J. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95895-0.00021-0 · Cited by 1

Bioinformatics Insights on Viral Gene Expression Transactivation: From HIV-1 to SARS-CoV-2

Patarca, R., & Haseltine, W. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063378 · Cited by 1

The Integrator complex: an emerging complex structure involved in the regulation of gene expression by targeting RNA polymerase II

Li, T., Zeng, F., Li, Y., Li, H., & Wu, J. (2024) · Functional & Integrative Genomics · doi:10.1007/s10142-024-01479-9 · Cited by 1

Conserved protein Seb1 that interacts with RNA polymerase II and RNA is an antipausing transcription elongation factor

Kuś, K., Nielsen, S., Zenkin, N., & Vasiljeva, L. (2025) · RNA · doi:10.1261/rna.080765.125 · Cited by 1

The Dynamic Association of RNA Polymerase II with Initiation, Elongation, and RNA Processing Factors during the Transcription Cycle

Penheiter, K. L., & Jaehning, J. A. (2007) · Springer eBooks · doi:10.1007/978-0-387-40049-5_3 · Cited by 1

Iwr1 facilitates RNA polymerase II dynamics during transcription elongation

Gómez‐Navarro, N., Peiró-Chova, L., & Estruch, F. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.02.009 · Cited by 1

Transcriptional Control and Latency of Retroviruses

Nikolai, B. C., & Rice, A. P. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811185-7.00005-4 · Cited by 1

Peptidyl inhibition of Spt4‐Spt5: Protein‐protein inhibitors for targeting the transcriptional pathway related to C9orf72 expansion repeats

Rayevsky, A. V., Platonov, M. O., Hurmach, V. V., Yakovenko, A., & Volochnyuk, D. M. (2020) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29820 · Cited by 1

Involvement of the RNA polymerase II-associated Paf1 complex in transcriptional regulation and 3'-end formation of snoRNAs

Sheldon, K. E. (2006) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1

Transcription elongation factors are involved in programming hormone production in pituitary neuroendocrine GH4C1 cells

Fujita, T., Piuz, I., & Schlegel, W. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.01.020 · Cited by 1

The role of Schizosaccharomyces pombe cyclophilin Rct1 in RNA polymerase II transcription

Skrahina, T. (2009) · University of Vienna · doi:10.25365/thesis.8122 · Cited by 1

Guest Editor’s Introduction

Price, D. H. (2009) · Methods · doi:10.1016/j.ymeth.2009.07.003 · Cited by 1

Investigations into the regulation of histone H2B monoubiquitination

Shchebet, A. (2011) · doi:10.53846/goediss-507 · Cited by 1

Stochastic modeling of eukaryotic transcription at the single nucleotide level

Vashishtha, S. (2011) · Open ULeth Scholarship (OPUS) (University of Lethbridge) · Cited by 1

Timing polymerase pausing with TV-PRO-seq: dissecting the interplay of pausing duration and location, and gene expressionPreprint

Zhang, J., Cavallaro, M., & Hebenstreit, D. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/461442 · Cited by 1

Structural and functional basis of the universal transcription factor NusG pro-pausing activity in Mycobacterium tuberculosisPreprint

Delbeau, M., Omollo, E. O., Froom, R., Koh, S., Mooney, R. A., Lilić, M., Brewer, J. J., Rock, J. M., Darst, S. A., Campbell, E. A., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.21.513233 · Cited by 1

Rtf1-dependent transcriptional pausing regulates cardiogenesisPreprint

Langenbacher, A. D., Lu, F., Tsang, L., Huang, Z. Y. S., Keer, B., Tian, Z., Eide, A., Pellegrini, M. A., Nakano, H., Nakano, A., et al. (2024) · eLife · doi:10.7554/elife.94524 · Cited by 1

Enhancer/Enhanceosome/Super-enhancer and the promoter-proximate RNA Polymerase II (Pol II) pausing are coupledPreprint

Liu, H., Li, L., Zhang, Q., Ott, C. J., & Zhang, G. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.10.693453 · Cited by 1

Rtf1-dependent transcriptional pausing regulates cardiogenesisPreprint

Langenbacher, A. D., Lu, F., Tsang, L., Huang, Z. Y. S., Keer, B., Tian, Z., Eide, A., Pellegrini, M. A., Nakano, H., Nakano, A., et al. (2026) · eLife · doi:10.7554/elife.94524.2 · Cited by 1

Evolutionary conservation and innovations of RNA polymerase II transcription elongation factorsPreprint

Francette, A. M., Grover, A., Clark, N., & Arndt, K. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.11.698887 · Cited by 1

The Role of AF9 and AF9-Mediated Protein Interactions in Hematopoiesis and Leukemogenesis

Lokken, A. A. (2014) · Loyola eCommons (Loyola University of Chicago)

Regulated release of P-Tefb from the 7sk Snrnp

Krueger, B. J. (2009) · doi:10.17077/etd.n88s3gow

IDENTIFICATION AND CHARACTERIZATION OF FACTORS REQUIRED FOR REPRESSION OF THE YEAST SER3 GENE BY SRG1 INTERGENIC TRANSCRIPTION

Pruneski, J. A. (2011) · D-Scholarship@Pitt (University of Pittsburgh)

Moloney Murine Leukemia Virus RNA Recruitment.

Garcia, E. L. (2010) · Deep Blue (University of Michigan)

A Functional Genomics Approach to Identify Novel Breast Cancer Gene Targets in Yeast

Bennett, C. B. (2005) · Defense Technical Information Center (DTIC) · doi:10.21236/ada437737

Procesos que regulan la transcripción en eucariotas

Martínez, A. G. (2012) · Gredos (University of Salamanca) · doi:10.14201/gredos.121359

Gene Expression Control by Chromatin Binding Factors

Voets, O. (2013) · RePub (Erasmus University Rotterdam)

Unraveling Mechanisms of Transcriptional Repression: Novel Insights from Brinker

Upadhyai, P. (2013) · D-Scholarship@Pitt (University of Pittsburgh)

Utilization Of Drosophila Hsp70 Gene For Identification Of Genuine Pol Ii Elongation Factors: Identification Of Spt6 As A Factor That Enhances The Elongation Rate Of Pol Ii In Vivo

Mohseni, A. (2010) · eCommons (Cornell University)

NMR solution structure of the Set2 SRI domain and preparation of RNA polymerase II complexes with the elongation factor Spt4-Spt5

Vojnic, E. (2006) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.6976

Genome-wide occupancy profiling of the RNA polymerase II transcription machinery in S. cerevisiae

Lidschreiber, M. (2013) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.16965

Structure of the Mediator subunit Cyclin C and subunit interaction studies within the Mediator head module

Höppner, S. (2005) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.4693

Structure and requirement of the Spt6 SH2 domain and an in vitro system to test the “torpedo model” of transcription termination

Dengl, S. (2009) · MPG.PuRe (Max Planck Society) · doi:10.5282/edoc.9983

Identification of ebs1, lsm6 and nup159 as suppressors of spt10 effects at ADH2 in Saccharomyces cerevisiae suggests post-transcriptional defects affect mRNA synthesis

Anderson, B., May, C. A., & Denis, C. L. (2012) · American Journal of Molecular Biology · doi:10.4236/ajmb.2012.23029

Role of Noncoding RNAs in the Regulation of P-TEFb Availability and Enzymatic Activity

Napolitano, G., Lania, L., & Majello, B. (2014) · BioMed Research International · doi:10.1155/2014/643805

A Role for Histone Chaperones in Regulating RNA Polymerase II

Osborn, J. L., & Greer, S. F. (2015) · Advances in Biological Chemistry · doi:10.4236/abc.2015.52004

Investigating the Roles of Tat Specific Factor 1 in Both HIV-1 and Cellular Gene Expression

Miller, H. B. (2009) · DukeSpace (Duke University)

Role of the RNA polymerase II C-terminal domain in transcription termination and function of Spt5 in 3' RNA-processing factor recruitment

Schreieck, A. (2013) · MPG.PuRe (Max Planck Society) · doi:10.5282/edoc.16454

Quantitative analysis of the effect of leflunomide on neural crest cell gene regulation during early embryonic development

Ford, C. (2014) · UEA Digital Repository (University of East Anglia)

Protein Dynamics in Mammalian Genome Maintenance

Zotter, A. (2008) · RePub (Erasmus University Rotterdam)

The Negative Elongation Factor Complex – A Poorly Understood Multi-Faceted Transcript-Processing Complex

Baron, B. (2015) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.888130

Regulation of gene expression through post-initiation controls

Vidyalakshmi, S., & Ramamurthy, V. (2006)

A Co-Repressor of Transcription that Interacts with the Adenovirus E1A Protein

Sundqvist, A. (2001)

Promoter directionality is controlled by U1 snRNP and polyadenylation signals in mouse embryonic stem cells

Almada, A. E. (2013) · DSpace@MIT (Massachusetts Institute of Technology)

Warten auf die Transkription: Die humanen Elongationsfaktoren NELF und DSIF

Wenzel, S. (2009) · EPub Bayreuth (University of Bayreuth)

A mechanism for co-transcriptional recruitment of mRNA localization factor on nascent mRNAs in budding yeast

Shen, Z. F. (2010) · doi:10.71781/26303

Structure of the Mediator subunit Cyclin C and subunit interaction studies within the Mediator head module

München, P. D. L.-M.-U. (2005)

Epigenetic Regulation of Replication-Dependent Histone mRNA 3 End Processing

Pirngruber, J. (2010) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-354

RNA polymerase II during transcript elongation : dealing with DNA damage and staying phosphorylated

Kong, S. E. (2001) · UCL Discovery (University College London)

Transcription: The Never Ending Story

Goodrich, J. A., & Tjian, R. (2007) · Springer eBooks · doi:10.1007/978-0-387-40049-5_1 · Cited by 1

Role of the yeast histone methyltransferase Set2 and its regulatory domains in RNA polymerase II transcription

Kizer, K. O. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/td3e-0j91

Structural characterisation of the Saccharomyces cerevisiae transcription elongation factor Spt4/5 through RNA interactions

Blythe, A. J. (2014) · UWA Profiles and Research Repository (UWA)

BET Bromodomains and P-TEFb in Cardiac Transcription and Heart Failure Pathogenesis

Anand, P., Munir, A. Z., & Haldar, S. M. (2016) · Cardiac and vascular biology · doi:10.1007/978-3-319-41457-7_12

The regulation and function of mRNA cap methylation in pluripotency and differentiation

Grasso, L. (2015) · Discovery Research Portal (University of Dundee)

Capturing Transcriptional Dynamics using Nascent RNA Sequencing.

Kirkconnell, K. S. (2016) · Deep Blue (University of Michigan)

Molecular mechanisms of anti-inflammatory glucocorticoid action: Evidence for a role of glucocorticoid-inducible genes and implications for glucocorticoid insensitivity

Shah, S. (2016) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/26991

Involvement of the C-terminal Repeat (CTR) Domain in the Protein Interactions and Functions of Spt5

Kuo, W. H. W. (2014) · TSpace (University of Toronto)

Applicability of Multidimensional Fractionation to Affinity Purification Mass Spectrometry Samples and Protein Phosphatase 4 Substrate Identification

Dunham, W. H. (2012) · TSpace (University of Toronto)

The roles of transcription factors in Nucleotide excision repair in yeast

Ding, B. (2010) · Louisiana State University · doi:10.31390/gradschool_dissertations.3791

Investigating the role of mRNA capping enzyme in C-MYC function

Lombardi, O. (2017) · Discovery Research Portal (University of Dundee)

Application of affinity purification of drug target proteins with practical magnetic nanoparticles to drug development

Ito, T., Sakamoto, S., & Handa, H. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813629-4.00012-7

The enzymatic function of the CCR4 protein

Chen, J. (2001) · University of New Hampshire Scholars Repository (University of New Hampshire at Manchester)

Function of structure-specific recognition protein-1 in gene regulation and mitosis.

Li, Y. (2007) · doi:10.6083/m48k7715

Timing polymerase pausing with TV-PRO-seq

Zhang, J. (2026) · Warwick Research Archive Portal (University of Warwick) · doi:10.82444/warw.33834583

Latency reversing agents affect HIV RNA splicing

Mota, T. M. (2017) · Minerva Access (University of Melbourne)

Regulation of alternative polyadenylation in Drosophila melanogaster

Oliveira, M. (2019) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · doi:10.34626/zrjc-r941

Characterisation of THOC4 Response to Replicative Stress

Najib, M. I. M. (2018) · Queensland University of Technology · doi:10.5204/thesis.eprints.122562

Comparative study of Human Immunodeficiency Virus type 1 and type 2 single and dual infections

Yapo, A. V. D. P. (2020) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/83774

Pou5f1 Post-translational Modifications Modulate Gene Expression and Cell Fate

Campbell, P. (2012) · uO Research (University of Ottawa) · doi:10.20381/ruor-6280

Faculty Opinions recommendation of KAP1 Is a Chromatin Reader that Couples Steps of RNA Polymerase II Transcription to Sustain Oncogenic Programs.

Coulombe, B. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737944547.793574581

Faculty Opinions recommendation of c-Myc regulates transcriptional pause release.

Dalton, S., & Singh, A. V. (2010) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.3133963.2818061

Reconstitution of the Integrator complex and its interaction with paused transcription elongation complex of Pol II-DSIF-NELF

Fianu, I. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8866

Faculty Opinions recommendation of DHODH modulates transcriptional elongation in the neural crest and melanoma.

Kalcheim, C. (2011) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.9973956.10706054

DSIF, a novel negative transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs.

Handa, H. (1998) · Institutional Repositories DataBase (IRDB)

Structure and Function of the Human Transcription Elongation Factor DSIF

Yamaguchi, Y., Wada, T., Watanabe, D., Takagi, T., Hasegawa, J., & Handa, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8085 · Cited by 143

The small hSpt4 subunit of the human transcription elongation factor DSIF is a Zn-finger protein with α/β type topology

Wenzel, S., Schweimer, K., ROSCH, P. J., & Wöhrl, B. M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.080 · Cited by 8

DSIF contributes to transcriptional activation by DNA-binding activators by preventing pausing during transcription elongation

Zhu, W., Wada, T., Okabe, S., Taneda, T., Yamaguchi, Y., & Handa, H. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm430 · Cited by 27

Evidence that P‐TEFb alleviates the negative effect of DSIF on RNA polymerase II‐dependent transcription in vitro

Wada, T., Takagi, T., Yamaguchi, Y., Watanabe, D., & Handa, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7395 · Cited by 355