Larisa E. Kapinos

ORCID: 0000-0001-6101-0876
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About
Contact & Profiles
Research Areas
  • Nuclear Structure and Function
  • RNA Research and Splicing
  • DNA and Nucleic Acid Chemistry
  • Metal complexes synthesis and properties
  • Chemical Reaction Mechanisms
  • RNA Interference and Gene Delivery
  • Genomics and Chromatin Dynamics
  • HIV/AIDS drug development and treatment
  • Advanced biosensing and bioanalysis techniques
  • Nanopore and Nanochannel Transport Studies
  • Molecular Sensors and Ion Detection
  • Viral Infections and Immunology Research
  • Alzheimer's disease research and treatments
  • Mass Spectrometry Techniques and Applications
  • Synthesis and Characterization of Heterocyclic Compounds
  • Lipid Membrane Structure and Behavior
  • Bacteriophages and microbial interactions
  • Trace Elements in Health
  • Electrochemical Analysis and Applications
  • Enzyme Structure and Function
  • Force Microscopy Techniques and Applications
  • Monoclonal and Polyclonal Antibodies Research
  • Radioactive element chemistry and processing
  • Fiber-reinforced polymer composites
  • Organic and Molecular Conductors Research

University of Basel
2016-2025

Institució Catalana de Recerca i Estudis Avançats
2018

Center for NanoScience
2015

Swiss Nanoscience Institute
2015

TU Dortmund University
2002

Leiden University
2002

Czech Academy of Sciences, Institute of Inorganic Chemistry
2001

Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry
2001

National Academy of Sciences of Ukraine
1997

B. Verkin Institute for Low Temperature Physics and Engineering of the National Academy of Sciences of Ukraine
1995-1997

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

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

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

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

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

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

Abstract Adenosine (Ado) can accept three protons, at N1, N3, and N7, to give H 3 3+ , thus has macro acidity constants. Unfortunately, these constants do not reflect the real basicity of N sites due internal repulsions, for example, between (N1)H + (N7)H . However, macroconstants are still needed evaluations first two taken from our own earlier work, that is, ${{\rm{p}}K_{{\rm{H}}_{\rm{3}} {\rm{(Ado)}}}^{\rm{H}} }$ =−4.02 ${{\rm{p}}K_{{\rm{H}}_{\rm{2}} =−1.53; third one was re‐measured as...

10.1002/chem.201003544 article EN Chemistry - A European Journal 2011-05-30

Nuclear pore complexes (NPCs) discriminate nonspecific macromolecules from importin and exportin receptors, collectively termed “karyopherins” (Kaps), that mediate nucleocytoplasmic transport. This selective barrier function is attributed to the behavior of intrinsically disordered phenylalanine-glycine nucleoporins (FG Nups) guard NPC channel. However, NPCs in vivo are typically enriched with different Kaps, how they impact remains unknown. Here, we show two major importinβ1/karyopherinβ1...

10.1083/jcb.202108107 article EN cc-by-nc-sa The Journal of Cell Biology 2022-01-28

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 acidity constants of protonated 7,9-dimethylguanine, 7-methylguanosine, 7,9-dimethylhypoxanthine, 7-methylinosine, 9-methyladenine, 1,9-dimethyladenine, 7,9-dimethyladenine and 1-methyladenosine were determined in aqueous solution at 25 °C I = 0.1 M (NaNO3). In those instances where pKa > 2 potentiometric pH titrations used for the determinations; when < 2, UV spectrophotometric 1H-NMR shift measurements employed (25 °C). these latter instances, is often larger than M, H0 scale was...

10.1039/b202023h article EN Journal of the Chemical Society Perkin Transactions 2 2002-05-28

Nucleoporins (nups) in the nuclear pore complex (NPC) form a selective barrier that suppresses diffusion of most macromolecules while enabling rapid transport receptor (NTR)–bound cargos. Recent studies have shown NPC may dilate and constrict, but how altering diameter affects its properties remains unclear. Here, we build DNA nanopores with programmable diameters nup arrangements to model constricted dilated NPCs. We find Nup62 proteins dynamic cross-channel impermeable hepatitis B virus...

10.1126/sciadv.adq8773 article EN cc-by-nc Science Advances 2024-11-13

Background In eukaryotes the genetic material is enclosed by a continuous membrane system, nuclear envelope (NE). Along NE specific proteins assemble to form meshworks and mutations in these have been described group of human diseases called laminopathies. Laminopathies include lipodystrophies, muscle cardiac as well metabolic or progeroid syndromes. Most laminopathies are caused LMNAgene encoding lamins A/C. Together with Nesprins (Nuclear Envelope Spectrin Repeat Proteins) they core...

10.1371/journal.pone.0071850 article EN cc-by PLoS ONE 2013-08-20

Protocells offer a versatile material for dissecting cellular processes and developing simplified biomimetic systems by combining biological components with synthetic ones. However, gap exists between the integrity complex functionality of native organelles such as nuclei, bottom‐up strategies reducing functions within environment. Here, this is bridged incorporating nuclei into polymeric giant unilamellar vesicles (pGUVs) using double‐emulsion microfluidics. It shown that retain their...

10.1002/smsc.202400622 article EN cc-by Small Science 2025-03-18
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