@article{10705,
  abstract     = {Although rigidity and jamming transitions have been widely studied in physics and material science, their importance in a number of biological processes, including embryo development, tissue homeostasis, wound healing, and disease progression, has only begun to be recognized in the past few years. The hypothesis that biological systems can undergo rigidity/jamming transitions is attractive, as it would allow these systems to change their material properties rapidly and strongly. However, whether such transitions indeed occur in biological systems, how they are being regulated, and what their physiological relevance might be, is still being debated. Here, we review theoretical and experimental advances from the past few years, focusing on the regulation and role of potential tissue rigidity transitions in different biological processes.},
  author       = {Hannezo, Edouard B and Heisenberg, Carl-Philipp J},
  issn         = {1879-3088},
  journal      = {Trends in Cell Biology},
  number       = {5},
  pages        = {P433--444},
  publisher    = {Cell Press},
  title        = {{Rigidity transitions in development and disease}},
  doi          = {10.1016/j.tcb.2021.12.006},
  volume       = {32},
  year         = {2022},
}

@article{11051,
  abstract     = {Nuclear pore complexes (NPCs) bridge the nucleus and the cytoplasm and are indispensable for crucial cellular activities, such as bidirectional molecular trafficking and gene transcription regulation. The discovery of long-lived proteins (LLPs) in NPCs from postmitotic cells raises the exciting possibility that the maintenance of NPC integrity might play an inherent role in lifelong cell function. Age-dependent deterioration of NPCs and loss of nuclear integrity have been linked to age-related decline in postmitotic cell function and degenerative diseases. In this review, we discuss our current understanding of NPC maintenance in proliferating and postmitotic cells, and how malfunction of nucleoporins (Nups) might contribute to the pathogenesis of various neurodegenerative and cardiovascular diseases.},
  author       = {Liu, Jinqiang and HETZER, Martin W},
  issn         = {0962-8924},
  journal      = {Trends in Cell Biology},
  keywords     = {Cell Biology},
  number       = {3},
  pages        = {P216--227},
  publisher    = {Elsevier},
  title        = {{Nuclear pore complex maintenance and implications for age-related diseases}},
  doi          = {10.1016/j.tcb.2021.10.001},
  volume       = {32},
  year         = {2022},
}

@article{11083,
  abstract     = {Nuclear pore complex (NPC) proteins are known for their critical roles in regulating nucleocytoplasmic traffic of macromolecules across the nuclear envelope. However, recent findings suggest that some nucleoporins (Nups), including Nup98, have additional functions in developmental gene regulation. Nup98, which exhibits transcription-dependent mobility at the NPC but can also bind chromatin away from the nuclear envelope, is frequently involved in chromosomal translocations in a subset of patients suffering from acute myeloid leukemia (AML). A common paradigm suggests that Nup98 translocations cause aberrant transcription when they are recuited to aberrant genomic loci. Importantly, this model fails to account for the potential loss of wild type (WT) Nup98 function in the presence of Nup98 translocation mutants. Here we examine how the cell might regulate Nup98 nucleoplasmic protein levels to control transcription in healthy cells. In addition, we discuss the possibility that dominant negative Nup98 fusion proteins disrupt the transcriptional activity of WT Nup98 in the nucleoplasm to drive AML.},
  author       = {Franks, Tobias M. and HETZER, Martin W},
  issn         = {0962-8924},
  journal      = {Trends in Cell Biology},
  keywords     = {Cell Biology},
  number       = {3},
  pages        = {112--117},
  publisher    = {Elsevier},
  title        = {{The role of Nup98 in transcription regulation in healthy and diseased cells}},
  doi          = {10.1016/j.tcb.2012.10.013},
  volume       = {23},
  year         = {2013},
}

@article{11110,
  abstract     = {Nuclear pore complexes are large aqueous channels that penetrate the nuclear envelope, thereby connecting the nuclear interior with the cytoplasm. Until recently, these macromolecular complexes were viewed as static structures, the only function of which was to control the molecular trafficking between the two compartments. It has now become evident that this simplistic scenario is inaccurate and that nuclear pore complexes are highly dynamic multiprotein assemblies involved in diverse cellular processes ranging from the organization of the cytoskeleton to gene expression. In this review, we discuss the most recent developments in the nuclear-pore-complex field, focusing on the assembly, disassembly, maintenance and function of this macromolecular structure.},
  author       = {D’Angelo, Maximiliano A. and HETZER, Martin W},
  issn         = {0962-8924},
  journal      = {Trends in Cell Biology},
  keywords     = {Cell Biology},
  number       = {10},
  pages        = {456--466},
  publisher    = {Elsevier},
  title        = {{Structure, dynamics and function of nuclear pore complexes}},
  doi          = {10.1016/j.tcb.2008.07.009},
  volume       = {18},
  year         = {2008},
}