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Blenski M and Kehlenbach RH (2019). Targeting of LRRC59 to the endoplasmic reticulum and the inner nuclear membrane. Int J Mol Sci 20(2), 334

Baade I and Kehlenbach RH. (2019). The cargo spectrum of nuclear transport receptors. Curr Opin Cell Biol. In press

Bonnin E, Cabochette P, Filosa A, Jühlen R, Komatsuzaki S, Hezwani M, et al. (2018) Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia deformation sequence. PLoS Genet 14 (12): e1007845.

Wu K, Wang L, Chen Y, Pirooznia M, Singh K, Wälde S, Kehlenbach RH, Scott I, Gucek M and Sack MN (2018). GCN5L1 interacts with aTAT1 and RanBP2 to regulate hepatic a-tubulin acetylation and lysosome trafficking. J. Cell Sci. 131, jcs221036. doi:10.1242/jcs.221036

Komatsu T, Quentin-Froignant C, Carlon-Andres I, Lagadec F, Rayne F, Jessica Ragues J, Kehlenbach RH, Zhang W, Ehrhardt A, Bystricky K, Morin R, Lagarde JM, Gallardo F and Wodrich H (2018). In vivo labelling of adenovirus DNA identifies chromatin anchoring and biphasic genome replication. J Virol. JVI.00795-18. doi: 10.1128/JVI.00795-18

Baade I, Spillner C, Schmitt, K, Valerius, O and Kehlenbach RH (2018). Extensive identification and in-depth validation of importin 13 cargoes. Mol. Cell. Proteomics 17, 1337-1353.

Ederle H, Funk C, Abou-Ajram C, Hutten S, Funk EBE, Kehlenbach RH, Bailer SM and Dormann D (2018). Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1. Sci Rep. 8, 7084

Chizhik AM, Ruhlandt D, Pfaff J, Karedla N, Chizhik AI, Gregor I, Kehlenbach RH* and Enderlein J* (2017). Three-dimensional reconstruction of nuclear envelope architecture using Dual-Color Metal-Induced Energy Transfer imaging. ACS Nano 11, 11839-11846. doi: 10.1021/acsnano.7b04671. *, co-corresponding

Landry-Voyer AM, Bilodeau S, Bergeron D, Dionne KL, Port SA, Rouleau C, Boisvert FM, Kehlenbach RH and Bachand F (2016). Human PDCD2L is an export substrate of CRM1 that associates with 40S ribosomal subunit precursors. Mol. Cell Biol. 36, 3019-3032

Port SA, Mendes A, Valkova C, Spillner C, Fahrenkrog B, Kaether C and Kehlenbach RH (2016). The oncogenic fusion proteins SET-Nup214 and sequestosome-1 (SQSTM1)-Nup214 form dynamic nuclear bodies and differentially affect nuclear protein- and poly(A)+ RNA export. J. Biol. Chem. 291, 23068-23083

Wallbach M, Escobar JD, Babaeikelishomi R, Stahnke MJ, Blume R, Schröder S, Kruegel J, Maedler K, Kluth O, Kehlenbach RH, Miosge N and Oetjen E (2016). Distinct functions of the dual leucine zipper kinase depending on its subcellular localization. Cell Signal. 28, 272-283

Kehlenbach RH and Port SA (2016). Analysis of CRM1-dependent nuclear export in permeabilized cells. Methods Mol Biol. 1411, 489-501

Pfaff J, Rivera Monroy, J, Jamieson, C, Rajanala, K, Vilardi, F, Schwappach B* and Kehlenbach RH* (2016). Emery-Dreifuss muscular dystrophy mutations impair TRC40-mediated targeting of emerin to the inner nuclear membrane. J Cell Sci. 129, 502-516. *, co-corresponding

Monecke T, Dickmanns A, Weiss MS, Port SA, Kehlenbach RH and Ficner R (2015). Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1–RanGTP–SPN1–Nup214 quaternary nuclear export complex. Acta Crystallogr. F. 71, 1481-1487

Port SA, Monecke T, Dickmanns A, Spillner C, Hofele R, Urlaub H, Ficner R* and Kehlenbach, RH* (2015). Structural and functional characterization of CRM1-Nup214 interactions reveals multiple FG-binding sites involved in nuclear export. Cell Rep. 13, 690-702. *, co-corresponding

Dickmanns A, Kehlenbach RH and Fahrenkrog B. (2015). Nuclear pore complexes and nucleocytoplasmic transport: from structure to function to disease. Int. Rev. Cell Mol. Biol. 320, 171-233

Halder K, Dölker N, Van Q, Gregor I, Dickmanns A, Baade I, Kehlenbach RH, Ficner R, Enderlein J, Grubmüller H and Neumann H. (2015). MD Simulations and FRET Reveal an Environment-Sensitive Conformational Plasticity of Importin-β. Biophys J. 109, 277-286

Kimura M, Thakar K, Karaca S, Imamoto N and Kehlenbach RH. (2014). Novel approaches for the identification of nuclear transport receptor substrates. Methods Cell Biol. 122, 353-378.

Furuta M, Kose S, Kehlenbach RH and Imamoto N. (2014). Analysis of nucleocytoplasmic transport in digitonin-permeabilized cells under different cellular conditions. Methods Cell Biol. 122, 331-352.

Frohnert C, Hutten S, Wälde S, Nath A and Kehlenbach RH. (2014). Importin 7 and Nup358 promote nuclear import of the protein component of human telomerase. PLoS One. 9(2):e88887.

Schulz O, Pieper C., Clever M., Pfaff J, Ruhlandt A, Kehlenbach RH, Wouters FS, Großhans J, Bunt G and Enderlein J. (2013). Resolution doubling in fluorescence microscopy with confocal spinning-disk image scanning microscopy. Proc. Natl. Acad. Sci. USA. 110, 21000-21005.

Snow CJ, Dar A, Dutta A, Kehlenbach RH and Paschal BM. (2013). Defective nuclear import of Tpr in Progeria reflects the Ran sensitivity of large cargo transport. J. Cell Biol. 201, 541-557.

Roloff S, Spillner C and Kehlenbach RH. (2013). Several phenylalanine-glycine motives in the nucleoporin Nup214 are essential for binding of the nuclear export receptor CRM1. J. Biol. Chem. 288, 3952-3963.

Thakar K, Karaca S, Port SA, Urlaub H and Kehlenbach RH. (2013). Identification of CRM1-dependent nuclear export cargoes using quantitative mass spectrometry. Mol. Cell. Proteomics. 12, 664-678.

Ehlers C, Schirmer S, Kehlenbach RH, Hauber J and Chemnitz J. (2013). Posttranscriptional regulation of CD83 expression 1 by AUF1 proteins. Nucleic Acids Res. 41, 206-219.

Malik P, Tabarraei A,  Kehlenbach RH, Korfali N, Iwasawa R, Graham SV and Schirmer EC. (2012). Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through NUP62, inhibiting host nucleocytoplasmic transport pathways. J. Biol. Chem. 287, 12277-12292.

Wälde S, Thakar K, Hutten S, Spillner C, Nath A, Rothbauer U, Wiemann S and Kehlenbach RH. (2012). The nucleoporin Nup358/RanBP2 promotes nuclear import in a cargo- and transport receptor-specific manner. Traffic. 13, 218-233.

Waldmann I, Spillner C and Kehlenbach RH. (2012). The nucleoporin like protein NLP1/hCG1 promotes CRM1-dependent nuclear protein export. J. Cell Science. 124, 144-154.

Hamada M, Haeger A, Jeganathan KB, van Ree JH, Malureanu L, Wälde S, Joseph J, Kehlenbach RH and van Deursen JM. (2011). Ran-dependent docking of importin-beta to RanBP2/Nup358 filaments is essential for protein import and cell viability. J. Cell Biol. 194, 597-612.

Pieper D, Schirmer S, Prechtel AT, Kehlenbach RH, Hauber J and Chemnitz J. (2011). Functional characterization of the HuR:CD83 mRNA interaction. PLoS One 6, e23290.

Wälde S and Kehlenbach RH. (2010). The Part and the Whole: functions of nucleoporins in nucleocytoplasmic transport. Trends Cell Biol. 20, 461-469.

Hilliard M, Frohnert C, Spillner C, Nath A, Lampe T, Marcone, S, Fitzgerald D and Kehlenbach RH. (2010). The anti-inflammatory prostaglandin 15-Deoxy-D12,14PGJ2 inhibits CRM1-dependent nuclear protein export. J. Biol. Chem. 285, 22202-22210.

Huenniger K, Krämer A, Soom M, Chang I, Köhler M, Depping R, Kehlenbach RH and Kaether C. (2010). Notch1 signaling is mediated by importins alpha 3, 4 and 7. Cell. Mol. Life Sciences 67, 3187-3196.

Antony P,  Maentele S,  Mollenkopf P,  Boy J, Kehlenbach RH, Riess O and Schmidt T. (2009). Identification and functional dissection of localization signals within ataxin-3. Neurobiol Dis, 36, 280-292.

Hutten S, Wälde S, Spillner C, Hauber J and Kehlenbach RH. (2009). The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J. Cell Science. 122, 1100-1110.

Kehlenbach RH (2009). Nucleocytoplasmic transport: players, signals, regulators. In: Kehlenbach R.H., ed. Nuclear Transport. Austin: Landes Bioscience.

Hutten S, Flotho, A, Melchior F and Kehlenbach RH.  (2008). The Nup358-RanGAP complex is required for efficient importin a/b-dependent nuclear import. Mol. Biol. Cell.19, 2300-2310.

Waldmann I, Wälde S and Kehlenbach RH. (2007). Nuclear import of c-Jun is mediated by multiple transport receptors. J. Biol. Chem. 282: 27685-27692.

Hutten S and Kehlenbach RH. (2007). CRM1-mediated nuclear export: to the pore and beyond. Trends Cell Biol. 17: 193-201.

Fries B, Heukeshoven J, Hauber I, Gruttner C, Stocking C, Kehlenbach RH, Hauber J and Chemnitz J. (2007). Analysis of Nucleocytoplasmic Trafficking of the HuR Ligand APRIL and Its Influence on CD83 Expression. J. Biol. Chem. 282: 4504-4515.

Hutten S and Kehlenbach RH. (2006). Nup214 is required for CRM1-dependent nuclear protein export in vivo. Mol. Cell. Biol. 26: 6772-6785.

Arnold A, Nath A, Hauber J and Kehlenbach RH. (2006). Multiple importins function as nuclear transport receptors for the Rev protein of the human immunodeficiency virus type 1. J. Biol. Chem. 281: 20883-20890.

Schütz S, Chemnitz J, Frohme M, Hauber J and Kehlenbach, R.H. (2006). Stimulated expression of mRNAs in activated T cells depends on a functional CRM1 nuclear export pathway. J. Mol. Biol. 358, 997-1009.

Prechtel, AT, Chemnitz, J., Schirme, S, Langbein-Detsch, I, Stülke, J, Dabauvalle, MC, Kehlenbach RH and Hauber J. (2006). Expression of CD83 is regulated by HuR via a novel cis-active coding region RNA element. J. Biol. Chem. 281:10912-25.

Arnold A, Nath A, Wohlwend D and Kehlenbach RH. (2006). Transportin is a major nuclear import receptor for c-Fos: a novel mode of cargo-interaction. J. Biol. Chem. 281, 5492-5499.

Kehlenbach RH. and Paschal BM. (2005). Analysis of nuclear protein transport in vitro. Cell Biology: A Laboratory Handbook. 3rd Edition. J. Celis (Editor). Elsevier. Vol. 2, 267-276.

Kehlenbach RH. (2003) In vitro analysis of nuclear mRNA export using molecular beacons for target detection. Nucleic Acids Res, 31, e64

Kehlenbach RH and Gerace L. (2002) Analysis of nuclear protein import and export in vitro using fluorescent cargoes. Methods Mol Biol, 189, 231-245.

Klemke M, Kehlenbach RH and Huttner WB. (2001). Two overlapping reading frames in a single exon encode interacting proteins-a novel way of gene usage. Embo J, 20, 3849-3860.

Kehlenbach RH, Assheuer R, Kehlenbach A, Becker J and Gerace L. (2001). Stimulation of Nuclear Export and Inhibition of Nuclear Import by a Ran Mutant Deficient in Binding to Ran-binding Protein 1. J Biol Chem, 276, 14524-14531.

Pasolli HA, Klemke M, Kehlenbach RH, Wang Y and Huttner WB. (2000). Characterization of the extra-large G protein alpha -subunit XLas. I. Tissue distribution and subcellular localization. J Biol Chem, 275, 33622-33632.

Klemke M, Pasolli HA, Kehlenbach RH, Offermanns S, Schultz G and Huttner WB. (2000) Characterization of the extra-large G protein alpha -subunit XLa s. II. Signal transduction properties. J Biol Chem, 275, 33633-33640.

Guan T., Kehlenbach RH, Schirmer EC, Kehlenbach A, Fan F, Clurman BE, Arnheim N and Gerace L. (2000). Nup50, a nucleoplasmically oriented nucleoporin with a role in nuclear protein export. Mol. Cell Biol., 20, 5619-5630.

Kehlenbach RH and Gerace L. (2000) Phosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitro. J. Biol. Chem., 275, 17848-17856.

Kehlenbach RH, Dickmanns A, Kehlenbach A, Guan T and Gerace L. (1999). A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export. J. Cell. Biol, 145, 645-657.

Kehlenbach RH, Dickmanns A and Gerace L. (1998) Nucleocytoplasmic shuttling factors including Ran and CRM1 mediate nuclear export of NFAT in vitro. J. Cell Biol., 141, 863-874.

Huttner WB, Ohashi M, Kehlenbach RH, Barr FA, Bauerfeind R, Bräunling O, Corbeil D, Hannah M, Pasolli HA, Schmidt A et al. (1995) Biogenesis of neurosecretory vesicles. Cold Spring Harb Symp Quant Biol, 60, 315-327.

Kehlenbach RH, Matthey J and Huttner WB. (1994). XLas is a new type of G protein. Nature, 372, 804-809.

Leyte A, Barr FA, Kehlenbach RH and Huttner WB. (1992). Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation. Embo J, 11, 4795-4804.

Zakut H, Ehrlich G, Ayalon A, Prody CA, Malinger G, Seidman S, Ginzberg D, Kehlenbach RH and Soreq H. (1990). Acetylcholinesterase and butyrylcholinesterase genes coamplify in primary ovarian carcinomas. J Clin Invest, 86, 900-908.