B. Kavcic, G. Tkadik, and M. T. Bollenbach, “Minimal biophysical model of combined antibiotic action,” PLOS Computational Biology, vol. 17. Public Library of Science, 2021.

A. A. Nagy-Staron et al., “Local genetic context shapes the function of a gene regulatory network,” eLife, vol. 10. eLife Sciences Publications, 2021.

A. K. Michael and N. H. Thomä, “Reading the chromatinized genome,” Cell, vol. 184, no. 14. Elsevier, pp. 3599–3611, 2021.

A. Fuchs et al., “Targeting alternative splicing by RNAi: From the differential impact on splice variants to triggering artificial pre-mRNA splicing,” Nucleic Acids Research, vol. 49, no. 2. Oxford University Press, pp. 1133–1151, 2021.

F. Navarrete et al., “The Pleiades are a cluster of fungal effectors that inhibit host defenses,” PLOS Pathogens, vol. 17, no. 6. Public Library of Science, 2021.

T. S. Balmer, C. Borges Merjane, and L. O. Trussell, “Incomplete removal of extracellular glutamate controls synaptic transmission and integration at a cerebellar synapse,” eLife, vol. 10. eLife Sciences Publications, 2021.

L. T. H. Tang et al., “The CATP-8/A-type ATPase functions in multiple pathways during neuronal patterning,” PLOS Genetics, vol. 17, no. 7. Public Library of Science, 2021.

J. Morandell et al., “Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development,” Nature Communications, vol. 12, no. 1. Springer Nature, 2021.

Z. Gelová et al., “Developmental roles of auxin binding protein 1 in Arabidopsis thaliana,” Plant Science, vol. 303. Elsevier, 2021.

A.-K. Pfitzner et al., “An ESCRT-III polymerization sequence drives membrane deformation and fission,” Cell, vol. 182, no. 5. Elsevier, p. 1140–1155.e18, 2020.

S. Bersini, R. Arrojo e Drigo, L. Huang, M. N. Shokhirev, and M. Hetzer, “Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease,” Advanced Biosystems, vol. 4, no. 5. Wiley, 2020.

S. Bersini, R. Schulte, L. Huang, H. Tsai, and M. Hetzer, “Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome,” eLife, vol. 9. eLife Sciences Publications, 2020.

H. Kang, M. N. Shokhirev, Z. Xu, S. Chandran, J. R. Dixon, and M. Hetzer, “Dynamic regulation of histone modifications and long-range chromosomal interactions during postmitotic transcriptional reactivation,” Genes &; Development, vol. 34, no. 13–14. Cold Spring Harbor Laboratory Press, pp. 913–930, 2020.

S. Bersini, N. K. Lytle, R. Schulte, L. Huang, G. M. Wahl, and M. Hetzer, “Nu regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling,” Life Science Alliance, vol. 3, no. 1. Life Science Alliance, 2020.

H. Rampelt et al., “The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments,” BMC Biology, vol. 18. Springer Nature, 2020.

N. Christophorou et al., “AX affects DNA methylation independently of its role in regulating meiotic crossover localization,” PLOS Genetics, vol. 16, no. 6. Public Library of Science (PLoS), 2020.

G. M. Arnold et al., “Converting microwave and telecom photons with a silicon photonic nanomechanical interface,” Nature Communications, vol. 11. Springer Nature, 2020.

A. Tian et al., “Oncogenic state and cell identity combinatorially dictate the susceptibility of cells within glioma development hierarchy to IGR targeting,” Advanced Science, vol. 7, no. 21. Wiley, 2020.

C. Prehal et al., “Persistent and reversible solid iodine electrodeposition in nanoporous carbons,” Nature Communications, vol. 11. Springer Nature, 2020.

L. Schulte et al., “Cysteine oxidation and disulfide formation in the ribosomal exit tunnel,” Nature Communications, vol. 11. Springer Nature, 2020.

K. Kaveh, A. McAvoy, K. Chatterjee, and M. A. Nowak, “The Moran process on 2-chromatic graphs,” PLOS Computational Biology, vol. 16, no. 11. Public Library of Science, 2020.

F. Fäßler, G. A. Dimchev, V.-V. Hodirnau, W. Wan, and F. K. Schur, “Cryo-electron tomography structure of Ar/3 complex in cells reveals new insights into the branch junction,” Nature Communications, vol. 11. Springer Nature, 2020.

J. L. Fribourgh et al., “Dynamics at the serine loop underlie differential affinity of cryptochromes for CLOCK:BMAL1 to control circadian timing,” eLife, vol. 9. eLife Sciences Publications, 2020.

A. Buchwalter, J. M. Kaneshiro, and M. Hetzer, “Coaching from the sidelines: The nuclear periphery in genome regulation,” Nature Reviews Genetics, vol. 20, no. 1. Springer Nature, pp. 39–50, 2019.

D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” Nature Communications, vol. 10. Springer Nature, 2019.

S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing of colloidal monolayers,” Nature Communications, vol. 10, no. 1. Springer Nature, 2019.

S. He, M. Vickers, J. Zhang, and X. Feng, “Natural depletion of histone  in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation,” eLife, vol. 8. eLife Sciences Publications, Ltd, 2019.

E. J. Lawrence et al., “Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis,” Current Biology, vol. 29, no. 16. Elsevier BV, p. 2676–2686.e3, 2019.

A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress,” eLife, vol. 8. eLife Sciences Publications, 2019.

A. McCloskey, A. Ibarra, and M. Hetzer, “Tpr regulates the total number of nuclear pore complexes per cell nucleus,” Genes &; Development, vol. 32, no. 19–20. Cold Spring Harbor Laboratory, pp. 1321–1331, 2018.

K. Weinhäupl et al., “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.

D. Samanta et al., “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” Nature Communications, vol. 9. Springer Nature, 2018.

M. Yuuta and K. Koshiba-Takeuchi, “Significance of whole-genome duplications on the emergence of evolutionary novelties,” Briefings in Functional Genomics, vol. 17, no. 5. Oxford University Press, pp. 329–338, 2018.

B. Bräuning et al., “Structure and mechanism of the two-component ;1-helical pore-forming toxin YaxAB,” Nature Communications, vol. 9. Springer Nature, 2018.

J. P. K. Bravo et al., “Stability of local secondary structure determines selectivity of viral RNA chaperones,” Nucleic Acids Research, vol. 46, no. 15. Oxford University Press, pp. 7924–7937, 2018.

S. C. J. Helle et al., “Mechanical force induces mitochondrial fission,” eLife, vol. 6. eLife Sciences Publications, 2017.

T. M. Franks, A. McCloskey, M. N. Shokhirev, C. Benner, A. Rathore, and M. Hetzer, “Nu recruits the Wdr82–Set1A/COMPASS complex to promoters to regulate K4 trimethylation in hematopoietic progenitor cells,” Genes &; Development, vol. 31, no. 22. Cold Spring Harbor Laboratory, pp. 2222–2234, 2017.

T. Toda et al., “Nu3 interacts with So to enable bimodal gene regulation and maintenance of neural progenitor cells,” Cell Stem Cell, vol. 21, no. 5. Elsevier, p. 618–634.e7, 2017.

A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” Nature Communications, vol. 8. Springer Nature, 2017.

S. G. Walt et al., “Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering,” Nature Communications, vol. 8. Springer Nature, 2017.

J. Walker et al., “Sexual-lineage-specific DNA methylation regulates meiosis in Arabidopsis,” Nature Genetics, vol. 50, no. 1. Nature Research, pp. 130–137, 2017.

J. C. Fong et al., “Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms,” eLife, vol. 6. eLife Sciences Publications, 2017.

R. A. H. van de Ven et al., “-catenin prevents multinucleation through control of MKL-dependent RhoA activity during cytokinesis,” Nature Communications, vol. 7. Springer Nature, 2016.

T. M. Franks et al., “Evolution of a transcriptional regulator from a transmembrane nucleoporin,” Genes &; Development, vol. 30, no. 10. Cold Spring Harbor Laboratory, pp. 1155–1171, 2016.

A. Ibarra, C. Benner, S. Tyagi, J. Cool, and M. Hetzer, “Nucleoporin-mediated regulation of cell identity genes,” Genes &; Development, vol. 30, no. 20. Cold Spring Harbor Laboratory, pp. 2253–2258, 2016.

J. Mertens et al., “Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects,” Cell Stem Cell, vol. 17, no. 6. Elsevier, pp. 705–718, 2015.

F. V. Jacinto, C. Benner, and M. Hetzer, “The nucleoporin Nu3 regulates embryonic stem cell pluripotency through gene silencing,” Genes &; Development, vol. 29, no. 12. Cold Spring Harbor Laboratory, pp. 1224–1238, 2015.

A. Ibarra and M. Hetzer, “Nuclear pore proteins and the control of genome functions,” Genes &; Development, vol. 29, no. 4. Cold Spring Harbor Laboratory, pp. 337–349, 2015.

E. M. Hatch and M. Hetzer, “Linking micronuclei to chromosome fragmentation,” Cell, vol. 161, no. 7. Elsevier, pp. 1502–1504, 2015.

E. M. Hatch and M. Hetzer, “Chromothripsis,” Current Biology, vol. 25, no. 10. Elsevier, pp. -9, 2015.

P. Ma et al., “Observing the overall rocking motion of a protein in a crystal,” Nature Communications, vol. 6. Springer Nature, 2015.

P. M. Kraus et al., “Observation of laser-induced electronic structure in oriented polyatomic molecules,” Nature Communications, vol. 6. Springer Nature, 2015.

A. Buchwalter and M. Hetzer, “Nuclear pores set the speed limit for mitosis,” Cell, vol. 156, no. 5. Elsevier, pp. 868–869, 2014.

P. K. Kundu, G. L. Olsen, V. Kiss, and R. Klajn, “Nanoporous frameworks exhibiting multiple stimuli responsiveness,” Nature Communications, vol. 5. Springer Nature, 2014.

Y. Liang, T. M. Franks, M. C. Marchetto, F. H. Gage, and M. Hetzer, “Dynamic association of NU with the human genome,” PLoS Genetics, vol. 9, no. 2. Public Library of Science, 2013.

B. H. Toyama et al., “Identification of long-lived proteins reveals exceptional stability of essential cellular structures,” Cell, vol. 154, no. 5. Elsevier, pp. 971–982, 2013.

E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear envelope collapse in cancer cell micronuclei,” Cell, vol. 154, no. 1. Elsevier, pp. 47–60, 2013.

M. A. D’Angelo, J. S. Gomez-Cavazos, A. Mei, D. H. Lackner, and M. Hetzer, “A change in nuclear pore complex composition regulates cell differentiation,” Developmental Cell, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.

E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” Cell, vol. 149, no. 4. Elsevier, pp. 733–735, 2012.

M. Capelson, C. Doucet, and M. Hetzer, “Nuclear pore complexes: Guardians of the nuclear genome,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 75. Cold Spring Harbor Laboratory Press, pp. 585–597, 2011.

M. Hetzer, “The nuclear envelope,” Cold Spring Harbor Perspectives in Biology, vol. 2, no. 3. Cold Spring Harbor Laboratory, pp. 0539–0539, 2010.

C. M. Doucet and M. Hetzer, “Nuclear pore biogenesis into an intact nuclear envelope,” Chromosoma, vol. 119. Springer Nature, pp. 469–477, 2010.

M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes,” Cell, vol. 140, no. 3. Elsevier, pp. 372–383, 2010.

C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences in nuclear pore complex assembly in metazoa,” Cell, vol. 141, no. 6. Elsevier, pp. 1030–1041, 2010.

M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” Developmental Cell, vol. 17, no. 5. Elsevier, pp. 606–616, 2009.

M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,” Cell, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.

M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation, development and disease,” EMBO reports, vol. 10, no. 7. EMBO, pp. 697–705, 2009.

C. Franz et al., “MEL28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly,” EMBO reports, vol. 8, no. 2. EMBO, pp. 165–172, 2007.

X. Feng and H. G. Dickinson, “Packaging the male germline in plants,” Trends in Genetics, vol. 23, no. 10. Elsevier BV, pp. 503–510, 2007.

Z. Liao et al., “A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides,” DNA Sequence, vol. 15, no. 2. Informa UK Limited, pp. 153–158, 2004.

T. C. Walther et al., “The conserved Nu7-160 complex is critical for nuclear pore complex assembly,” Cell, vol. 113, no. 2. Elsevier, pp. 195–206, 2003.

D. Bilbao-Cortés, M. Hetzer, G. Längst, P. B. Becker, and I. W. Mattaj, “Ran binds to chromatin by two distinct mechanisms,” Current Biology, vol. 12, no. 13. Elsevier BV, pp. 1151–1156, 2002.