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Cells, Volume 6, Issue 2

June 2017 - 7 articles

Cover Story: Ligand binding rearranges conformation of the extracellular domains of an EGFR dimer from tethered to untethered. This rearrangement induces a rotation/twist of the transmembrane domain of the receptor parallel to the plane of the cell membrane, resulting in the reorientation of the intracellular kinase domain dimer from a symmetric inactive configuration (left) to an asymmetric active form (right). Oncogenic mutations, shown by red balls, may also induce the asymmetric active form of the kinase dimer without ligand binding. View this paper
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Articles (7)

  • Feature Paper
  • Review
  • Open Access
22 Citations
8,155 Views
17 Pages

Telomere Biology—Insights into an Intriguing Phenomenon

  • Shriram Venkatesan,
  • Aik Kia Khaw and
  • Manoor Prakash Hande

19 June 2017

Bacteria and viruses possess circular DNA, whereas eukaryotes with typically very large DNA molecules have had to evolve into linear chromosomes to circumvent the problem of supercoiling circular DNA of that size. Consequently, such organisms possess...

  • Feature Paper
  • Review
  • Open Access
159 Citations
19,946 Views
19 Pages

2 June 2017

The epidermal growth factor receptor (EGFR) plays vital roles in cellular processes including cell proliferation, survival, motility, and differentiation. The dysregulated activation of the receptor is often implicated in human cancers. EGFR is synth...

  • Review
  • Open Access
91 Citations
13,367 Views
15 Pages

9 May 2017

Lung cancer is the leading cause of cancer deaths worldwide, yet there remains a lack of specific and sensitive tools for early diagnosis and targeted therapies. High-throughput sequencing techniques revealed that non-coding RNAs (ncRNAs), e.g., micr...

  • Feature Paper
  • Review
  • Open Access
17 Citations
7,885 Views
18 Pages

4 May 2017

Genomic integrity is of outmost importance for the survival at the cellular and the organismal level and key to human health. To ensure the integrity of their DNA, cells have evolved maintenance programs collectively known as the DNA damage response....

  • Article
  • Open Access
4 Citations
7,624 Views
14 Pages

Distinct Fiber Type Signature in Mouse Muscles Expressing a Mutant Lamin A Responsible for Congenital Muscular Dystrophy in a Patient

  • Alice Barateau,
  • Nathalie Vadrot,
  • Onnik Agbulut,
  • Patrick Vicart,
  • Sabrina Batonnet-Pichon and
  • Brigitte Buendia

24 April 2017

Specific mutations in LMNA, which encodes nuclear intermediate filament proteins lamins A/C, affect skeletal muscle tissues. Early-onset LMNA myopathies reveal different alterations of muscle fibers, including fiber type disproportion or prominent dy...

  • Article
  • Open Access
9 Citations
8,375 Views
23 Pages

25 March 2017

Lamins form a scaffold lining the nucleus that binds chromatin and contributes to spatial genome organization; however, due to the many other functions of lamins, studies knocking out or altering the lamin polymer cannot clearly distinguish between d...

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Cells - ISSN 2073-4409