Roderick Y. H. Lim

ORCID: 0000-0001-5015-6087
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About
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Research Areas
  • Nuclear Structure and Function
  • RNA Research and Splicing
  • Force Microscopy Techniques and Applications
  • Cellular Mechanics and Interactions
  • Nanopore and Nanochannel Transport Studies
  • RNA Interference and Gene Delivery
  • Genomics and Chromatin Dynamics
  • Polymer Surface Interaction Studies
  • Molecular Junctions and Nanostructures
  • RNA regulation and disease
  • Advanced Biosensing Techniques and Applications
  • Microfluidic and Bio-sensing Technologies
  • Microtubule and mitosis dynamics
  • Advanced biosensing and bioanalysis techniques
  • Microfluidic and Capillary Electrophoresis Applications
  • RNA and protein synthesis mechanisms
  • Lipid Membrane Structure and Behavior
  • Mechanical and Optical Resonators
  • thermodynamics and calorimetric analyses
  • Monoclonal and Polyclonal Antibodies Research
  • Alzheimer's disease research and treatments
  • Electrowetting and Microfluidic Technologies
  • Trace Elements in Health
  • Cell Adhesion Molecules Research
  • Cellular transport and secretion

University of Basel
2016-2025

Swiss Nanoscience Institute
2012-2023

Center for NanoScience
2015-2023

University Hospital of Basel
2018

Kantonsspital Baden
2018

Freiwillige Akademische Gesellschaft
2017

Nanyang Technological University
2011

Institute of Materials Research and Engineering
2002-2007

National University of Singapore
2001-2002

The nuclear pore complex regulates cargo transport between the cytoplasm and nucleus. We set out to correlate governing biochemical interactions nanoscopic responses of phenylalanineglycine (FG)–rich nucleoporin domains, which are involved in attenuating or promoting translocation. found that binding with receptor karyopherin-β1 caused FG domains human Nup153 collapse into compact molecular conformations. This effect was reversed by action Ran guanosine triphosphate, returned a polymer...

10.1126/science.1145980 article EN Science 2007-10-05

Abstract The human non-canonical inflammasome controls caspase-4 activation and gasdermin-D-dependent pyroptosis in response to cytosolic bacterial lipopolysaccharide (LPS). Since LPS binds oligomerizes caspase-4, the pathway is thought proceed without dedicated sensors or an platform. Here we report that interferon-induced guanylate-binding proteins (GBPs) are required for by Salmonella upon delivery of LPS. GBP1 associates with surface seconds after escape from their vacuole, initiating...

10.1038/s41467-020-16889-z article EN cc-by Nature Communications 2020-06-24

Natively unfolded phenylalanine-glycine (FG)-repeat domains are alleged to form the physical constituents of selective barrier-gate in nuclear pore complexes during nucleocytoplasmic transport. Presently, biophysical mechanism behind gate remains speculative because a lack information regarding nanomechanical properties FG domains. In this work, we have applied atomic force microscope measure mechanical response individual and clusters molecules. Single-molecule spectroscopy reveals that...

10.1073/pnas.0603521103 article EN Proceedings of the National Academy of Sciences 2006-06-13

We present a new grafting-to method for resistant "non-fouling" poly(ethylene glycol) brushes, which is based on grafting of polymers with reactive end groups in 0.9 M Na2SO4 at room temperature. The process, the resulting and resistance toward biomolecular adsorption are investigated by surface plasmon resonance, quartz crystal microbalance, atomic force microscopy. determine both density thickness independently use narrow molecular weight distributions result well-defined brushes. High...

10.1021/acsami.5b01590 article EN publisher-specific-oa ACS Applied Materials & Interfaces 2015-03-26

Nucleocytoplasmic transport is sustained by karyopherins (Kaps) and a Ran guanosine triphosphate (RanGTP) gradient that imports nuclear localization signal (NLS)–specific cargoes (NLS-cargoes) into the nucleus. However, how pore complex (NPC) barrier selectivity, Kap traffic, NLS-cargo release are systematically linked simultaneously regulated remains incoherent. In this study, we show Kapα facilitates Kapβ1 turnover occupancy at NPC in RanGTP-dependent manner directly coupled to function....

10.1083/jcb.201702092 article EN cc-by-nc-sa The Journal of Cell Biology 2017-09-01

Organelle-specific nanocarriers (NCs) are highly sought after for delivering therapeutic agents into the cell nucleus. This necessitates nucleocytoplasmic transport (NCT) to bypass nuclear pore complexes (NPCs). However, little is known as how comparably large NCs infiltrate this vital intracellular barrier enter interior. Here, we developed localization signal (NLS)-conjugated polymersome (NLS-NCs) and studied NCT mechanism underlying their selective uptake. Detailed chemical, biophysical,...

10.1073/pnas.1916395117 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2020-01-27

Conformational changes at supramolecular interfaces are fundamentally coupled to binding activity, yet it remains a challenge probe this relationship directly. Within the nuclear pore complex, underlies how transport receptors known as karyopherins proceed through tethered layer of intrinsically disordered nucleoporin domains containing Phe-Gly (FG)-rich repeats (FG domains) that otherwise hinder passive transport. Here, we use nonspecific proteins (i.e., BSA) innate molecular probes explore...

10.1073/pnas.1208440109 article EN Proceedings of the National Academy of Sciences 2012-10-04

Purpose.: The purpose of this article was to create a nanometer scale topographic and biomechanical profile the human internal limiting membrane (ILM) under native conditions. Methods.: ILMs from posterior pole postmortem eyes were prepared as flat mounts investigated by atomic force microscopy (AFM) physiological Structural analysis complemented transmission electron microscopy. Results.: Average thickness fully hydrated, 3488 ± 460 nm. Thickness variations 100 nm 4326 characterized fovea,...

10.1167/iovs.11-8502 article EN Investigative Ophthalmology & Visual Science 2012-03-13

Nuclear Pore Complexes (NPCs) are key cellular transporter that control nucleocytoplasmic transport in eukaryotic cells, but its mechanism is still not understood. The centerpiece of NPC the assembly intrinsically disordered polypeptides, known as FG nucleoporins, lining passageway. Their conformations and collective dynamics during difficult to assess vivo. In vitro investigations provide partially conflicting results, lending support different models transport, which invoke various...

10.7554/elife.10785 article EN cc-by eLife 2016-05-18

The transport channel of nuclear pore complexes (NPCs) contains a high density intrinsically disordered proteins that are rich in phenylalanine-glycine (FG)-repeat motifs (FG Nups). FG Nups interact promiscuously with various receptors (NTRs), such as karyopherins (Kaps), mediate the trafficking nucleocytoplasmic cargoes while also generating selectively permeable barrier against other macromolecules. Although binding NTRs to increases molecular crowding NPC channel, it is unclear how this...

10.1016/j.bpj.2014.12.041 article EN cc-by Biophysical Journal 2015-02-01

Abstract Nuclear pore complexes (NPCs) mediate nucleocytoplasmic transport of specific macromolecules while impeding the exchange unsolicited material. However, key aspects this gating mechanism remain controversial. To address issue, we determined nanoscopic behavior permeability barrier directly within yeast S. cerevisiae NPCs at transport-relevant timescales. We show that large intrinsically disordered domains phenylalanine-glycine repeat nucleoporins (FG Nups) exhibit highly dynamic...

10.1101/2023.03.31.535055 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-04-03

The current basement membrane (BM) model proposes a single-layered extracellular matrix (ECM) sheet that is predominantly composed of laminins, collagen IVs and proteoglycans. present data show BM proteins their domains are asymmetrically organized providing human BMs with side-specific properties: A) isolated roll up in pattern, the epithelial side facing outward stromal inward. rolling independent curvature tissue from which were isolated. B) twice as stiff side, C) cells adhere to only....

10.1371/journal.pone.0067660 article EN cc-by PLoS ONE 2013-07-03

Article22 March 2018Open Access Transparent process Structural centrosome aberrations promote non-cell-autonomous invasiveness Olivier Ganier Biozentrum, University of Basel, Switzerland Search for more papers by this author Dominik Schnerch Philipp Oertle Swiss Nanoscience Institute, Roderick YH Lim Marija Plodinec Erich A Nigg Corresponding Author [email protected] orcid.org/0000-0003-4835-5719 Information Ganier1,‡, Schnerch1,3,‡, Oertle1,2, Lim1,2, Plodinec1,2 and *,1 1Biozentrum, 2Swiss...

10.15252/embj.201798576 article EN cc-by-nc-nd The EMBO Journal 2018-03-22
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