The Specificity of the CRM1-Rev Nuclear Export Signal Interaction Is Mediated by RanGTP

CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals

Fornerod, M. W. J., Ohno, M., Yoshida, M., & Mattaj, I. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80371-2 · Cited by 2,086

CRM1 is responsible for intracellular transport mediated by the nuclear export signal

Fukuda, M., Asano, S., Nakamura, T., Adachi, M., Yoshida, M., Yanagida, M., & Nishida, E. (1997) · Nature · doi:10.1038/36894 · Cited by 1,213

Identification of a signal for rapid export of proteins from the nucleus

Wen, W., Meinkotht, J. L., Tsien, R. Y., & Taylor, S. S. (1995) · Cell · doi:10.1016/0092-8674(95)90435-2 · Cited by 1,190

Nucleocytoplasmic transport: the soluble phase

Mattaj, I. W., & Englmeier, L. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.265 · Cited by 1,175

Exportin 1 (Crm1p) Is an Essential Nuclear Export Factor

Stade, K., Ford, C. S., Guthrie, C., & Weis, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80370-0 · Cited by 1,145

The HIV-1 Rev Activation Domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs

Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W., & Lührmann, R. (1995) · Cell · doi:10.1016/0092-8674(95)90436-0 · Cited by 1,140

Functional dissection of the HIV-1 Rev trans-activator—Derivation of a trans-dominant repressor of Rev function

Malim, M. H., Böhnlein, S., Hauber, J., & Cullen, B. R. (1989) · Cell · doi:10.1016/0092-8674(89)90416-9 · Cited by 732

Evidence for a Role of CRM1 in Signal-Mediated Nuclear Protein Export

Ossareh‐Nazari, B., Bachelerie, F., & Dargemont, C. (1997) · Science · doi:10.1126/science.278.5335.141 · Cited by 713

Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1

Bischoff, F. R., & Ponstingl, H. (1991) · Nature · doi:10.1038/354080a0 · Cited by 711

Isolation of a protein that is essential for the first step of nuclear protein import

Görlich, D. (1994) · Cell · doi:10.1016/0092-8674(94)90067-1 · Cited by 695

Nucleocytoplasmic RNA Transport in Retroviral Replication

Wodrich, H., & Kräusslich, H. (2001) · Results and problems in cell differentiation · doi:10.1007/978-3-540-40025-7_12 · Cited by 35

Nuclear Factor 90, a cellular dsRNA binding protein inhibits the HIV Rev-export function

Inchima, S. U., Castaño, M. E., Hernandez‐Verdun, D., Laurent, G. C. S., & Kumar, A. (2006) · Retrovirology · doi:10.1186/1742-4690-3-83 · Cited by 34

Branched peptideboronic acids (BPBAs): a novel mode of binding towards RNA

Zhang, W., Bryson, D. I., Crumpton, J. B., Wynn, J. E., & Santos, W. L. (2013) · Chemical Communications · doi:10.1039/c3cc00243h · Cited by 33

Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: Novel insights into the regulation of Rev nuclear import

Gu, L., Tsuji, T., Jarboui, M. A., Yeo, G. P., Sheehy, N., Hall, W. W., & Gautier, V. (2011) · Retrovirology · doi:10.1186/1742-4690-8-17 · Cited by 33

Domains of Crm1 Involved in the Formation of the Crm1, RanGTP, and Leucine-Rich Nuclear Export Sequences Trimeric Complex

Ossareh‐Nazari, B., & Dargemont, C. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4599 · Cited by 33

RNA helicase MOV10 functions as a co-factor of HIV-1 Rev to facilitate Rev/RRE-dependent nuclear export of viral mRNAs

Huang, F., Zhang, J., Zhang, Y., Geng, G., Liang, J., Li, Y., Chen, J., Liu, C., & Zhang, H. (2015) · Virology · doi:10.1016/j.virol.2015.08.026 · Cited by 33

A HIV-1 Tat mutant protein disrupts HIV-1 Rev function by targeting the DEAD-box RNA helicase DDX1

Lin, M., Sivakumaran, H., Jones, A., Li, D., Harper, C. B., Wei, T., Jin, H., Rustanti, L., Meunier, F. A., Spann, K. M., et al. (2014) · Retrovirology · doi:10.1186/preaccept-7500780551442434 · Cited by 32

The N-terminal Nuclear Export Sequence of IκBα Is Required for RanGTP-dependent Binding to CRM1

Lee, S., & Hannink, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011197200 · Cited by 32

Strength in Diversity: Nuclear Export of Viral RNAs

Gales, J. P., Kubina, J., Geldreich, A., & Dimitrova, M. (2020) · Viruses · doi:10.3390/v12091014 · Cited by 31

Human Retrovirus Genomic RNA Packaging

Hanson, H. M., Willkomm, N. A., Yang, H., & Mansky, L. M. (2022) · Viruses · doi:10.3390/v14051094 · Cited by 33

Evolution of a Species-Specific Determinant within Human CRM1 that Regulates the Post-transcriptional Phases of HIV-1 Replication

Sherer, N. M., Swanson, C. M., Hué, S., Roberts, R. G., Bergeron, J. R. C., & Malim, M. H. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002395 · Cited by 31

Inhibition of HIV-1 Replication by Cell-penetrating Peptides Binding Rev

Roisin, A., Robin, J.-P., Dereuddre‐Bosquet, N., Vitte, A.-L., Dormont, D., Clayette, P., & Jalinot, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311594200 · Cited by 30

Signaling from the Cytoplasm to the Nucleus in Striatal Medium-Sized Spiny Neurons

Matamales, M., & Girault, J. (2011) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2011.00037 · Cited by 37

Constitutive Transport Element-Mediated Nuclear Export

Hammarskjöld, M. L. (2001) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-56597-7_4 · Cited by 30

Nuclear Import of Upf3p Is Mediated by Importin-α/-β and Export to the Cytoplasm Is Required for a Functional Nonsense-Mediated mRNA Decay Pathway in Yeast

Shirley, R. L., Ford, A., Richards, M. R., Albertini, M., & Culbertson, M. R. (2002) · Genetics · doi:10.1093/genetics/161.4.1465 · Cited by 29

Rev Inhibition Strongly Affects Intracellular Distribution of Human Immunodeficiency Virus Type 1 RNAs

Cmarko, D., Bøe, S.-O., Scassellati, C., Szilvay, A. M., Davanger, S., Fu, X., Haukenes, G., Kalland, K.-H., & Fakan, S. (2002) · Journal of Virology · doi:10.1128/jvi.76.20.10473-10484.2002 · Cited by 28

Structure of the HIV‐1 Rev response element alone and in complex with regulator of virion (Rev) studied by atomic force microscopy

Pallesen, J., Dong, M., Besenbacher, F., & Kjems, J. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07130.x · Cited by 28

Mapping of the Functional Boundaries and Secondary Structure of the Mouse Mammary Tumor Virus Rem-responsive Element

Mertz, J. A., Chadee, A. B., Byun, H., Russell, R., & Dudley, J. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.012476 · Cited by 26

The neural F-box protein NFB42 mediates the nuclear export of the herpes simplex virus type 1 replication initiator protein (UL9 protein) after viral infection

Eom, C., Heo, W. D., Craske, M., Meyer, T., & Lehman, I. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400738101 · Cited by 27

Identification of a novel Rev-interacting cellular protein

Kramer-Hämmerle, S., Ceccherini‐Silberstein, F., Bickel, C., Wolff, H., Vincendeau, M., Werner, T., Erfle, V., & Brack‐Werner, R. (2005) · BMC Cell Biology · doi:10.1186/1471-2121-6-20 · Cited by 27

New regulatory mechanisms for the intracellular localization and trafficking of influenza A virus NS1 protein revealed by comparative analysis of A/PR/8/34 and A/Sydney/5/97

Han, H., Cui, Z., Wang, W., Zhang, Z.-P., Wei, H.-P., Zhou, Y., & Zhang, X. (2010) · Journal of General Virology · doi:10.1099/vir.0.024943-0 · Cited by 26

The Carboxy-Terminal Region of the Human Immunodeficiency Virus Type 1 Protein Rev Has Multiple Roles in Mediating CRM1-Related Rev Functions

Hakata, Y., Yamada, M., Mabuchi, N., & Shida, H. (2002) · Journal of Virology · doi:10.1128/jvi.76.16.8079-8089.2002 · Cited by 26

A structurally plastic ribonucleoprotein complex mediates post‐transcriptional gene regulation in HIV ‐1

Fernandes, J. D., Booth, D. S., & Frankel, A. D. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1342 · Cited by 25

The dependence of Ig class‐switching on the nuclear export sequence of AID likely reflects interaction with factors additional to Crm1 exportin

Ellyard, J. I., Benk, A. S., Taylor, B., Rada, C. A., & Neuberger, M. S. (2010) · European Journal of Immunology · doi:10.1002/eji.201041011 · Cited by 25

Exportin-1-Dependent Nuclear Export of DEAD-box Helicase DDX3X is Central to its Role in Antiviral Immunity

Heaton, S. M., Atkinson, S. C., Sweeney, M., Yang, S. N. Y., Jans, D. A., & Borg, N. A. (2019) · Cells · doi:10.3390/cells8101181 · Cited by 25

Characterization of signal sequences determining the nuclear export of Newcastle disease virus matrix protein

Duan, Z., Song, Q., Wang, Y., He, L., Chen, J., Zhu, Y., Hu, S., & Liu, X. (2013) · Archives of Virology · doi:10.1007/s00705-013-1769-5 · Cited by 24

The Coiled Coil Region (Amino Acids 129–250) of the Tumor Suppressor Protein Adenomatous Polyposis Coli (APC)

Tickenbrock, L., Cramer, J., Vetter, I. R., & Müller, O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203990200 · Cited by 23

Single-Nucleotide Changes in the HIV Rev-Response Element Mediate Resistance to Compounds That Inhibit Rev Function

Shuck-Lee, D., Chang, H., Sloan, E. A., Hammarskjöld, M., & Rekosh, D. M. (2011) · Journal of Virology · doi:10.1128/jvi.02683-10 · Cited by 21

A Single Amino Acid Substitution in the ICP27 Protein of Herpes Simplex Virus Type 1 Is Responsible for Its Resistance to Leptomycin B

Murata, T., Goshima, F., Koshizuka, T., Takakuwa, H., & Nishiyama, Y. (2001) · Journal of Virology · doi:10.1128/jvi.75.2.1039-1043.2001 · Cited by 21

A Carboxyl Leucine-Rich Region of Parathyroid Hormone-Related Protein Is Critical for Nuclear Export

Pache, J. C., Burton, D. W., Deftos, L. J., & Hastings, R. H. (2005) · Endocrinology · doi:10.1210/en.2005-0663 · Cited by 20

Nuclear Export of the Oncoprotein v-ErbA Is Mediated by Acquisition of a Viral Nuclear Export Sequence

Wood, L. D., Bonamy, G. M. C., Fink, E. N., & Allison, L. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308214200 · Cited by 20

HibeRNAtion: HIV-1 RNA Metabolism and Viral Latency

Crespo, R., Rao, S., & Mahmoudi, T. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.855092 · Cited by 22

Random Mutagenesis and Functional Analysis of the Ran-binding Protein, RanBP1

Petersen, C. D., Orem, N. R., Trueheart, J., Thorner, J. W., & Macara, I. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4081 · Cited by 19

Nuclear Export of Simian Immunodeficiency Virus Vpx Protein

Singhal, P. K., Kumar, P. R., Malireddi, R. K. S., & Mahalingam, S. (2006) · Journal of Virology · doi:10.1128/jvi.00563-06 · Cited by 18

Replication of Human Immunodeficiency Virus Type 1 from Entry to Exit

Lever, A. M. L., & Jeang, K. (2006) · International Journal of Hematology · doi:10.1532/ijh97.06112 · Cited by 18

Insights into a CRM1-mediated RNA-nuclear export pathway in Trypanosoma cruzi

Cuevas, I., Frasch, A. C. C., & D’Orso, I. (2004) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2004.11.002 · Cited by 18

Structural and computational studies of HIV-1 RNA

Levintov, L., & Vashisth, H. (2023) · RNA Biology · doi:10.1080/15476286.2023.2289709 · Cited by 18

Human CRM1 Augments Production of Infectious Human and Feline Immunodeficiency Viruses from Murine Cells

Elinav, H., Wu, Y., Coskun, A. K., Hryckiewicz, K., Kemler, I., Hu, Y., Rogers, H., Hao, B., Mamoun, C. B., Poeschla, E. M., et al. (2012) · Journal of Virology · doi:10.1128/jvi.01970-12 · Cited by 17

TNF Stimulates Nuclear Export and Secretion of IL-15 by Acting on CRM1 and ARF6

Ouyang, S., Hsuchou, H., Kastin, A. J., & Pan, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069356 · Cited by 17

Exchange of the Basic Domain of Human Immunodeficiency Virus Type 1 Rev for a Polyarginine Stretch Expands the RNA Binding Specificity, and a Minimal Arginine Cluster Is Required for Optimal RRE RNA Binding Affinity, Nuclear Accumulation, and trans -Activation

Nam, Y.-S., Petrovic, A., Jeong, K., & Venkatesan, S. (2001) · Journal of Virology · doi:10.1128/jvi.75.6.2957-2971.2001 · Cited by 17

Probing the Structures of Viral RNA Regulatory Elements with SHAPE and Related Methodologies

Rausch, J. W., Sztuba-Solińska, J., & Grice, S. F. J. L. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02634 · Cited by 18

A Role for the Basic Patch and the C Terminus of RanGTP in Regulating the Dynamic Interactions with Importin β, CRM1 and RanBP1

Nilsson, J., Askjaer, P., & Kjems, J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4313 · Cited by 17

Human T Lymphotropic Virus Type 1 Regulatory and Accessory Gene Transcript Expression and Export Are Not Rex Dependent

Li, M., Kannian, P., Yin, H., Kesic, M. J., & Green, P. L. (2011) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2011.0130 · Cited by 16

Potential nuclease-based strategies for HIV gene therapy.

Singwi, S., & Joshi, S. (2000) · Frontiers in Bioscience · doi:10.2741/singwi · Cited by 21

Structure of HIV-1 RRE stem-loop II identifies two conformational states of the high-affinity Rev binding site

Tipo, J., Gottipati, K., Slaton, M., González-Gutiérrez, G., & Choi, K. H. (2024) · Nature Communications · doi:10.1038/s41467-024-48162-y · Cited by 15

Sequence and Functional Variation in the HIV-1 Rev Regulatory Axis

Jackson, P., Dzhivhuho, G. A., Rekosh, D. M., & Hammarskjöld, M. (2020) · Current HIV Research · doi:10.2174/1570162x18666200106112842 · Cited by 13

Unperturbed Posttranscriptional Regulatory Rev Protein Function and HIV-1 Replication in Astrocytes

Chauhan, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106910 · Cited by 14

Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

Bacot-Davis, V. R., Ciomperlik, J. J., Basta, H. A., Cornilescu, C. C., & Palmenberg, A. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411098111 · Cited by 14

The First Identified Nucleocytoplasmic Shuttling Herpesviral Capsid Protein: Herpes Simplex Virus Type 1 VP19C

Zhao, L., & Zheng, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041825 · Cited by 13

Specificity of RSG-1.2 Peptide Binding to RRE-IIB RNA Element of HIV-1 over Rev Peptide Is Mainly Enthalpic in Origin

Kumar, S., Bose, D., Suryawanshi, H., Sabharwal, H., Mapa, K., & Maiti, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023300 · Cited by 13

Impact of Nuclear Export Pathway on Cytoplasmic HIV-1 RNA Transport Mechanism and Distribution

Chen, J., Umunnakwe, C. N., Sun, D., Nikolaitchik, O. A., Pathak, V. K., Berkhout, B., Das, A. T., & Hu, W.-S. (2020) · mBio · doi:10.1128/mbio.01578-20 · Cited by 12

Evolutionary Constraints Acting on DDX3X Protein Potentially Interferes with Rev-Mediated Nuclear Export of HIV-1 RNA

Sharma, D., & Bhattacharya, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009613 · Cited by 13

Analysis of nuclear targeting activities of transport signals in the human immunodeficiency virus Rev protein

Demart, S., Ceccherini‐Silberstein, F., Schlicht, S., Walcher, S., Wolff, H., Neumann, M., Erfle, V., & Brack‐Werner, R. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.07.011 · Cited by 13

Structural Fluidity of the Human Immunodeficiency Virus Rev Response Element

Sherpa, C., & Grice, S. F. J. L. (2020) · Viruses · doi:10.3390/v12010086 · Cited by 12

Tough Way In, Tough Way Out: The Complex Interplay of Host and Viral Factors in Nucleocytoplasmic Trafficking during HIV-1 Infection

Sarkar, S., Balakrishnan, K., Chintala, K., Mohareer, K., Luedde, T., Vasudevan, A. A. J., Münk, C., & Banerjee, S. (2022) · Viruses · doi:10.3390/v14112503 · Cited by 13

Dynamic Post-Transcriptional Regulation of HIV-1 Gene Expression

Kula, A., & Marcello, A. (2012) · Biology · doi:10.3390/biology1020116 · Cited by 12

Anti-idiotype RNAs that mimic the leucine-rich nuclear export signal and specifically bind to CRM1/exportin 1

Hamm, J., & Fornerod, M. W. J. (2000) · Chemistry & Biology · doi:10.1016/s1074-5521(00)00112-5 · Cited by 12

Production of HIV Particles Is Regulated by Altering Sub-Cellular Localization and Dynamics of Rev Induced by Double-Strand RNA Binding Protein

Inchima, S. U., Patiño, C., Zapata, X., García, M. P., Arteaga, H. J., Chamot, C., Kumar, A., & Hernandez‐Verdun, D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016686 · Cited by 12

CRM1 and Ran are present but a NES-CRM1-RanGTP complex is not required in Balbiani ring mRNP particles from the gene to the cytoplasm

Zhao, J., Jin, S., & Wieslander, L. (2004) · Journal of Cell Science · doi:10.1242/jcs.00992 · Cited by 12

HIV-1 Rev can specifically interact with MMTV RNA and upregulate gene expression

Dangerfield, J. A., Hohenadl, C., Egerbacher, M., Kodajova, P., Salmons, B., & Günzburg, W. H. (2005) · Gene · doi:10.1016/j.gene.2005.05.018 · Cited by 12

HIV-1 Hijacking of Host ATPases and GTPases That Control Protein Trafficking

Tavares, L., Januário, Y. C., & daSilva, L. L. P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.622610 · Cited by 12

Binding Affinity Measurement of Nuclear Export Signal Peptides to Their Exporter CRM1

Fung, H. Y. J., & Chook, Y. M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2337-4_16 · Cited by 11

Over-expression of the HIV-1 Rev promotes death of nondividing eukaryotic cells

Levin, A., Hayouka, Z., Friedler, A., & Loyter, A. (2010) · Virus Genes · doi:10.1007/s11262-010-0458-7 · Cited by 11

Calcium-calmodulin kinase I cooperatively regulates nucleocytoplasmic shuttling of CCTα by accessing a nuclear export signal

Agassandian, M., Chen, B. B., Pulijala, R., Kaercher, L., Glasser, J. R., & Mallampalli, R. K. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-10-0863 · Cited by 10

Peripheral blood mononuclear cell microRNA profiles in syphilitic patients with serofast status

Jia, X., Wang, Z., Liu, X., Zheng, H., & Li, J. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05421-7 · Cited by 9

Staufen‐2 functions as a cofactor for enhanced Rev‐mediated nucleocytoplasmic trafficking of HIV ‐1 genomic RNA via the CRM1 pathway

Balakrishnan, K., Munusami, P., Mohareer, K., Priyakumar, U. D., Banerjee, A., Luedde, T., Mande, S. C., Münk, C., & Banerjee, S. (2022) · FEBS Journal · doi:10.1111/febs.16546 · Cited by 9

Improving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource

Druce, M., Hulo, C., Masson, P., Sommer, P., Xénarios, I., Mercier, P. L., & de Oliveira, T. (2016) · Database · doi:10.1093/database/baw045 · Cited by 9

Differential interaction between human and murine Crm1 and lentiviral Rev proteins

Yue, Y., Coskun, A. K., Jawanda, N., Auer, J., & Sutton, R. E. (2017) · Virology · doi:10.1016/j.virol.2017.09.027 · Cited by 9

Novel—and Not So Novel—Inhibitors of the Multifunctional CRM1 Protein

Aumann, W. K., Kazi, R. R., Harrington, A. M., & Wechsler, D. S. (2024) · Oncology Reviews · doi:10.3389/or.2024.1427497 · Cited by 8

Neglected Issues in T Lymphocyte Metabolism: Purine Metabolism and Control of Nuclear Envelope Regulatory Processes. New Insights into Triggering Potential Metabolic Fragilities

Torchia, N., Brescia, C., Chiarella, E., Audia, S., Trapasso, F., & Amato, R. (2024) · Immuno · doi:10.3390/immuno4040032 · Cited by 8

The Jembrana disease virus Rev protein: Identification of nuclear and novel lentiviral nucleolar localization and nuclear export signals

Marchand, C., Lemay, G., & Archambault, D. (2019) · PLoS ONE · doi:10.1371/journal.pone.0221505 · Cited by 7

Hyperosmotic stress sustains cytokine-stimulated phosphorylation of STAT3, but slows its nuclear trafficking and impairs STAT3-dependent transcription

Ng, I. H. W., Jans, D. A., & Bogoyevitch, M. A. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2013.12.012 · Cited by 6

Retroviral hijacking of host transport pathways for genome nuclear export

Behrens, R. T., & Sherer, N. M. (2023) · mBio · doi:10.1128/mbio.00070-23 · Cited by 6

Help or Hinder: Protein Host Factors That Impact HIV-1 Replication

Moezpoor, M. R., & Stevenson, M. (2024) · Viruses · doi:10.3390/v16081281 · Cited by 7

Protein Transport Between the Nucleus and Cytoplasm

Miyamoto, Y., Yoneda, Y., & Oka, M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803480-4.00025-9 · Cited by 6

Interferon-Regulated Expression of Cellular Splicing Factors Modulates Multiple Levels of HIV-1 Gene Expression and Replication

Roesmann, F., Müller, L., Klaassen, K., Heß, S., & Widera, M. (2024) · Viruses · doi:10.3390/v16060938 · Cited by 7

HIV-1 Rev function as target for antiretroviral drug development

Daelemans, D., & Pannecouque, C. C. (2006) · Current Opinion in HIV and AIDS · doi:10.1097/01.coh.0000239851.22614.6a · Cited by 5

Direct and Indirect Roles of Ran-GTP in Nuclear Export of RNAS in Higher Eukaryotes

Lund, E., & Dahlberg, J. E. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1501-2_4 · Cited by 5

Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication

Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5

Novel Vpx virus-like particles to improve cytarabine treatment response against acute myeloid leukemia

Nair, R., Salinas-Illarena, A., Sponheimer, M., Wullkopf, I., Schreiber, Y., Côrte‐Real, J. V., Ben, A. D. P., Marterer, H., Thomas, D., Geißlinger, G., et al. (2024) · Clinical and Experimental Medicine · doi:10.1007/s10238-024-01425-w · Cited by 3

The Molecular Mechanisms of mRNA Export

Taura, T., Siomi, M. C., & Siomi, H. (2007) · Springer eBooks · doi:10.1007/0-387-27747-1_10 · Cited by 2

Gene Regulation through mRNA Expression

Inose, H., Mukai, K., Ito, M., & Masuda, S. (2015) · Advances in Biological Chemistry · doi:10.4236/abc.2015.52005 · Cited by 2

Cell-based and cell-free firefly luciferase complementation assay to quantify Human Immunodeficiency Virus type 1 Rev-Rev interaction

Hansen, T., Baris, J., Zhao, M., & Sutton, R. E. (2022) · Virology · doi:10.1016/j.virol.2022.08.011 · Cited by 2

Domain- and nucleotide-specific Rev response element regulation of feline immunodeficiency virus production

Na, H., Huisman, W., Ellestad, K. K., Phillips, T. R., & Power, C. (2010) · Virology · doi:10.1016/j.virol.2010.04.009 · Cited by 2

HIV-1 Cis Enhancing Sequence (CES) enhances CTE-dependent Gag expression

Suptawiwat, O., Lee, T., & Auewarakul, P. (2005) · Virology · doi:10.1016/j.virol.2005.07.027 · Cited by 2

Cleavage of AUF1 by Coxsackievirus B Affects DDX5 Regulatory on Viral Replication through iTRAQ Proteomics Analysis

Wang, T., Qin, Y., Chen, J., Chen, S., Wu, J., Chen, X., Chen, X., Zhou, S., Zou, J., & Guan, J. (2022) · BioMed Research International · doi:10.1155/2022/8610467 · Cited by 1

Rev-RRE activity modulates HIV-1 replication and latency reactivation: Implications for viral persistence and cure strategies

Dzhivhuho, G. A., Jackson, P., Honeycutt, E., Mesquita, F. D. S., Huang, J., Hammarskjöld, M., & Rekosh, D. M. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012885 · Cited by 1

Strain-Specific Protein Interaction and Localization of Two Strains of Potato Yellow Dwarf Virus and Functional Domains of Their Matrix Protein

Jang, C. (2019) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2019.008 · Cited by 1

The scientific basis of pediatric HIV care

Smith, S., Melvin, A. J., Zeichner, S. L., McFarland, E. J., Palumbo, P. E., & Aldrovandi, G. M. (2006) · Cambridge University Press eBooks · doi:10.1017/cbo9780511544781.003 · Cited by 1

Proteínas celulares cómplices de las proteínas regulatorias y accesorias del VIH-1.

Castaño, M. E., & Inchima, S. U. (2004) · Colombia medica · doi:10.25100/cm.v35i.2.296 · Cited by 1

Tight Junction Protein Expression in Human Astrocytes

Morgan, S. V. (2016) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York) · Cited by 1

Conformational Changes in Ligand Binding Processes

Voß, B. (2015) · doi:10.53846/goediss-4927 · Cited by 1

Synthetic Genes for Prevention and Therapy: Implications on Safety and Efficacy of DNA Vaccines and Lentiviral Vectors

Bieler, K., & Wagner, R. (2001) · doi:10.1002/9783527612833.ch09

The proteasome activator Blm10 facilitates nuclear import of mature proteasome core particles in yeast

Weberruss, M. H. (2014) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-1417

Funktionelle Analyse der Rev Transaktivierung des Humanen Immundefizienzvirus Typ 1

Hoffmann, D. (2012)

Sam68, Stress Granules, and translational control of HIV-1 nef mRNA

Henao‐Mejia, J. (2009) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1690

Inibição de cinases e/ou fosfatases celulares por bibliotecas de siRNA:aplicação na infecção do HIV-1

Resende, L. (2008) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

HIV-1 NEF: THERAPEUTIC STRATEGIES AND VIROLOGICAL SYNAPSE-MEDIATED INFECTION

Green, L. A. (2011) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1705

Ran GTPASE Regulation of the CRM1-Dependent Export Pathway

Paschal, B. M., & Dargemont, C. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1501-2_2

Characteristics and Relevance of the Interaction Between Staufen-1 and Rev- related Retroviral Proteins

Mostafa, S. (2016) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-10373

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Smith, A. M., Li, Y., Velarde, A., Cheng, Y., & Frankel, A. D. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.07.015 · Cited by 12

Putative Reaction Intermediates in Crm1-mediated Nuclear Protein Export

Floer, M., & Blobel, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16279 · Cited by 62

CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals

Fornerod, M. W. J., Ohno, M., Yoshida, M., & Mattaj, I. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80371-2 · Cited by 2,086

The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export

Neville, M., Stutz, F., Lee, L., Davis, L. I., & Rosbash, M. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00335-6 · Cited by 439

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Booth, D. S., Cheng, Y., & Frankel, A. D. (2014) · eLife · doi:10.7554/elife.04121 · Cited by 70