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Showing 1–26 of 26 results
Advanced filters: Author: Edward A. Lemke Clear advanced filters
  • Some transcription factors can organize into different structural states, from small nanoscale clusters to macrophases. Here authors show that NHA9 undergoes differential conformational expansion across these states and exhibits micelle-like organization with non-fixed stoichiometry.

    • Hao Ruan
    • Rodrigo F. Dillenburg
    • Edward A. Lemke
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-18
  • Synthetic organelles enable the selective manipulation of cellular biochemistry. Here the authors focus on RNA modifications and use designer organelles in mammalian cells to selectively incorporate pseudouridine into mRNA using circular guide RNAs.

    • Lukas Schartel
    • Cosimo Jann
    • Edward A. Lemke
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-10
  • Site-specific labeling of proteins with small fluorophores is advantageous for imaging. Lemke et al. describe how to site-specifically label membrane proteins with organic fluorophores by incorporating non-canonical amino acids via Amber suppression technology.

    • Ivana Nikić
    • Jun Hee Kang
    • Edward A Lemke
    Protocols
    Nature Protocols
    Volume: 10, P: 780-791
  • Genetic code expansion (GCE) is a protein engineering tool that enables programmed and site-specific installation of noncanonical amino acids into proteins. Here, authors show that cellular stress remodelling boosts GCE in mammalian cells including GCE realized by orthogonally translating organelles.

    • Mikhail E. Sushkin
    • Christine Koehler
    • Edward A. Lemke
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14
  • A laminar flow mixing microfluidic device enables single-molecule fluorescence resonance energy transfer (FRET) kinetic measurements with a time resolution of 0.2 ms, enabling the study of early binding-coupled folding and unfolding events of an intrinsically disordered protein, α-synuclein. Also in this issue, Kim et al. describe another microfluidic mixing device for single-molecule experiments.

    • Yann Gambin
    • Virginia VanDelinder
    • Ashok A Deniz
    Research
    Nature Methods
    Volume: 8, P: 239-241
  • The TAM receptor kinases Axl and Mer are critical for microglial recognition and clearance of accumulating amyloid in transgenic models of Alzheimer’s disease.

    • Edward N. Wilson
    • Katrin I. Andreasson
    News & Views
    Nature Immunology
    Volume: 22, P: 543-544
  • Fluorescent probes for bioimaging need to exhibit bright fluorescence, be biocompatible and offer several alternatives for attachment to biomolecules of interest. Here, a near-infrared silicon–rhodamine fluorophore is introduced that can be coupled to intracellular proteins in live cells and tissues and can be exploited for super-resolution microscopy.

    • Gražvydas Lukinavičius
    • Keitaro Umezawa
    • Kai Johnsson
    Research
    Nature Chemistry
    Volume: 5, P: 132-139
  • Sensors and reporters are among the most exciting tools used in cell biology. Now, they are increasingly used in developmental biology and medicine because they allow us to spy on events in living cells and organisms, including humans, in real time and with high spatial resolution. Herein, we discuss multiple design options for fluorescent sensors and reporters as well as strategies to improve their properties and increase development.

    • Edward A Lemke
    • Carsten Schultz
    Comments & Opinion
    Nature Chemical Biology
    Volume: 7, P: 480-483
  • A method for producing multiprotein complexes engineered with site–specifically introduced noncanonical amino acids is described, enabling applications in biochemical and biophysical analysis, as well as in biotechnology.

    • Christine Koehler
    • Paul F Sauter
    • Edward A Lemke
    Research
    Nature Methods
    Volume: 13, P: 997-1000
  • Biological clocks can be used to evaluate the age of a cell or organisms. This Perspective proposes the concept of an intrinsically disordered protein (IDP) clock, whereby the aggregation state of an IDP encodes for a biological ageing signature.

    • Dorothee Dormann
    • Edward Anton Lemke
    Reviews
    Nature Cell Biology
    Volume: 26, P: 851-858
  • The realization that the cell is abundantly compartmentalized into biomolecular condensates has opened new opportunities for understanding the physics and chemistry underlying many cellular processes1, fundamentally changing the study of biology2. The term biomolecular condensate refers to non-stoichiometric assemblies that are composed of multiple types of macromolecules in cells, occur through phase transitions, and can be investigated by using concepts from soft matter physics3. As such, they are intimately related to aqueous two-phase systems4 and water-in-water emulsions5. Condensates possess tunable emergent properties such as interfaces, interfacial tension, viscoelasticity, network structure, dielectric permittivity, and sometimes interphase pH gradients and electric potentials614. They can form spontaneously in response to specific cellular conditions or to active processes, and cells appear to have mechanisms to control their size and location1517. Importantly, in contrast to membrane-enclosed organelles such as mitochondria or peroxisomes, condensates do not require the presence of a surrounding membrane.

    • Simon Alberti
    • Paolo Arosio
    • Tanja Mittag
    Comments & OpinionOpen Access
    Nature Communications
    Volume: 16, P: 1-14
  • Three versatile and mutually orthogonal tRNA/aminoacyl-tRNA synthetase pairs have been developed. Collectively, these pairs enable the site-specific incorporation of three different non-canonical amino acids into a protein that can still be terminated faithfully by a natural stop codon.

    • Christopher D. Reinkemeier
    • Edward A. Lemke
    News & Views
    Nature Chemistry
    Volume: 12, P: 503-504
  • Femtosecond resolution X-ray fluorescence spectroscopy is shown to track the charge and spin dynamics triggered when an iron coordination complex is excited by light, and establishes the critical role of intermediate spin states in the de-excitation process.

    • Wenkai Zhang
    • Roberto Alonso-Mori
    • Kelly J. Gaffney
    Research
    Nature
    Volume: 509, P: 345-348
  • The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization.

    • Alexander von Appen
    • Jan Kosinski
    • Martin Beck
    Research
    Nature
    Volume: 526, P: 140-143