The chromatin remodeler SPLAYED negatively regulates SN-mediated immunity
K.C.M. Johnson, S. Xia, X. Feng, X. Li, Plant and Cell Physiology 56 (2015) 1616–1623.
LibreCat: https://research-explorer.ista.ac.at/record/12196
DOI: 10.1093/pcp/pcv087
PMID: 26063389

Cancer/Testis antigen PAS silences the circadian clock
A.K. Michael, S.L. Harvey, P.J. Sammons, A.P. Anderson, H.M. Kopalle, A.H. Banham, C.L. Partch, Molecular Cell 58 (2015) 743–754.
LibreCat: https://research-explorer.ista.ac.at/record/15160
DOI: 10.1016/j.molcel.2015.03.031

Nu is required for cell differentiation and exhibits transcription-dependent dynamics
A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014) 2472–2484.
LibreCat: https://research-explorer.ista.ac.at/record/11082
DOI: 10.1091/mbc.e14-04-0865

Breaching the nuclear envelope in development and disease
E. Hatch, M. Hetzer, Journal of Cell Biology 205 (2014) 133–141.
LibreCat: https://research-explorer.ista.ac.at/record/11081
DOI: 10.1083/jcb.201402003
PMID: 24751535

The role of Nu in transcription regulation in healthy and diseased cells
T.M. Franks, M. Hetzer, Trends in Cell Biology 23 (2013) 112–117.
LibreCat: https://research-explorer.ista.ac.at/record/11083
DOI: 10.1016/j.tcb.2012.10.013
PMID: 23246429

Protein homeostasis: Live long, won't prosper
B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.
LibreCat: https://research-explorer.ista.ac.at/record/11084
DOI: 10.1038/nrm3496
PMID: 23258296

Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins
J.S. Gomez-Cavazos, M. Hetzer, Current Opinion in Cell Biology 24 (2012) 775–783.
LibreCat: https://research-explorer.ista.ac.at/record/11089
DOI: 10.1016/j.ceb.2012.08.008
PMID: 22995343

Transient nuclear envelope rupturing during interphase in human cancer cells
J.D. Vargas, E.M. Hatch, D.J. Anderson, M. Hetzer, Nucleus 3 (2012) 88–100.
LibreCat: https://research-explorer.ista.ac.at/record/11091
DOI: 10.4161/nucl.18954
PMID: 22567193

A change in nuclear pore complex composition regulates cell differentiation
M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458.
LibreCat: https://research-explorer.ista.ac.at/record/11093
DOI: 10.1016/j.devcel.2011.11.021
PMID: 22264802

POM121 and Sun1 play a role in early steps of interphase NPC assembly
J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.
LibreCat: https://research-explorer.ista.ac.at/record/11094
DOI: 10.1083/jcb.201012154
PMID: 21727197

Functional interactions between nucleoporins and chromatin
Y. Liang, M. Hetzer, Current Opinion in Cell Biology 23 (2011) 65–70.
LibreCat: https://research-explorer.ista.ac.at/record/11096
DOI: 10.1016/j.ceb.2010.09.008
PMID: 21030234

Editorial overview
M. Hetzer, G. Cavalli, Current Opinion in Cell Biology 23 (2011) 255–257.
LibreCat: https://research-explorer.ista.ac.at/record/11095
DOI: 10.1016/j.ceb.2011.04.013
PMID: 21592757

The role of the nuclear pore complex in aging of post-mitotic cells
M. Hetzer, Aging 2 (2010) 74–75.
LibreCat: https://research-explorer.ista.ac.at/record/11098
DOI: 10.18632/aging.100125
PMID: 20354266

Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein ;22-Microglobulin revealed by real-time two-dimensional NMR
A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.
LibreCat: https://research-explorer.ista.ac.at/record/8473
DOI: 10.1074/jbc.m109.061168

Tapetal cell fate, lineage and proliferation in the Arabidopsis anther
X. Feng, H.G. Dickinson, Development 137 (2010) 2409–2416.
LibreCat: https://research-explorer.ista.ac.at/record/12199
DOI: 10.1242/dev.049320
PMID: 20570940

Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther
X. Feng, H.G. Dickinson, Biochemical Society Transactions 38 (2010) 571–576.
LibreCat: https://research-explorer.ista.ac.at/record/12200
DOI: 10.1042/bst0380571
PMID: 20298223

Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes
M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.
LibreCat: https://research-explorer.ista.ac.at/record/11103
DOI: 10.1016/j.devcel.2009.10.007
PMID: 19922866

Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo
D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology 186 (2009) 183–191.
LibreCat: https://research-explorer.ista.ac.at/record/11106
DOI: 10.1083/jcb.200901106
PMID: 19620630

ER membrane–bending proteins are necessary for de novo nuclear pore formation
T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology 184 (2009) 659–675.
LibreCat: https://research-explorer.ista.ac.at/record/11107
DOI: 10.1083/jcb.200806174
PMID: 19273614

Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation
D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 911–924.
LibreCat: https://research-explorer.ista.ac.at/record/11111
DOI: 10.1083/jcb.200805140
PMID: 18779370