Results 161 to 170 of about 7,348 (200)

Patient-derived xenografts from circulating cancer stem cells as a preclinical model for personalized pancreatic cancer research. [PDF]

Sci Rep
Wagner BJ, Ettner-Sitter A, Ihlo NA, Behr M, Koelbl S, Brunner SM, Weber F, Rau BM, Schlitt HJ, Brochhausen C, Schoenmehl R, Artinger A, Schott D, Pizon M, Pachmann K, Aung T, Haerteis S, Hackl C.   +17 more
europepmc   +1 more source

A keratin bundling transition uncages the nucleus in stretched epithelia

Golde T, Pensalfini M, Chahare N, Roca-Cusachs P, Wiche G, Charras GT, Arroyo M, Trepat X.   +7 more
europepmc   +1 more source

Plectin-Isoform-Specific Rescue of Hemidesmosomal Defects in Plectin (–/–) Keratinocytes [PDF]

Journal of Investigative Dermatology, 2003
The various plectin isoforms are among the major crosslinking elements of the cytoskeleton. The importance of plectin in epithelia is convincingly supported by the severe skin blistering observed in plectin-deficient humans and mice. Here, we identified plectin 1a (> 500 kDa), a full length plectin variant containing the sequence encoded by the ...
Gerhard Wiche
exaly   +4 more sources

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Plectin

Current Biology, 2023
Prechova et al. introduce the giant cytoskeletal crosslinker protein plectin.
Magdalena, Prechova, Katerina, Korelova, Martin, Gregor   +2 more
openaire   +2 more sources

The Versatility of Plectin in Cancer: A Pan-Cancer Analysis on Potential Diagnostic and Prognostic Impacts of Plectin Isoforms

OMICS: A Journal of Integrative Biology, 2023
Plectin, encoded by PLEC , is a cytoskeletal and scaffold protein with a number of unique isoforms that act on various cellular functions such as cell adhesion, signal transduction, cancer cell invasion, and migration.
Hulya Gundesli, Medi Kori, Kazim Yalcin Arga   +2 more
openaire   +3 more sources

Plectin: A Cytolinker by Design

Biological Chemistry, 1999
AbstractPlectin is a cytoskeletal protein of > 500 kDa that forms dumbbell-shaped homodimers comprising a central parallel α-helical coiled coil rod domain flanked by globular domains, thus providing a molecular backbone ideally suited to mediate the protein's interactions with an array of other cytoskeletal elements.
Steinböck, Ferdinand, Wiche, Gerhard
openaire   +3 more sources

Interaction of plectin and intermediate filaments

Journal of Dermatological Science, 2012
Plectin, a member of the plakin family proteins, is a high molecular weight protein that is ubiquitously expressed. It acts as a cytolinker for the three major components of the cyotoskeleton, namely actin microfilaments, microtubules and intermediate filaments.The aim of our experiments was to identify new binding sites for intermediate filaments on ...
Tadashi, Karashima, Daisuke, Tsuruta, Takahiro, Hamada, Norito, Ishii, Fumitake, Ono, Keiko, Hashikawa, Bungo, Ohyama, Yohei, Natsuaki, Shunpei, Fukuda, Hiroshi, Koga, Ryosuke, Sogame, Takekuni, Nakama, Teruki, Dainichi, Takashi, Hashimoto   +13 more
openaire   +2 more sources

The many faces of plectin and plectinopathies: pathology and mechanisms

Acta Neuropathologica, 2012
Plectin, a giant multifunctional cytolinker protein, plays a crucial role in stabilizing and orchestrating intermediate filament networks in cells. Mutations in the human plectin gene result in multiple diseases manifesting with muscular dystrophy, skin blistering, and signs of neuropathy.
Lilli Winter, Gerhard Wiche
exaly   +3 more sources

Proteolysis of Liver Plectin by μ-Calpain

Biochemical and Biophysical Research Communications, 1998
Rat liver plectin was found to be mainly associated with plasma membrane fractions enriched in junctional complexes. The membrane-associated plectin has been partially isolated. Plectin co-purifies with a 200 kDa polypeptide which, on the basis of sequence homology, has been identified as a myosin like-protein.
Muenchbach M, Dell'Ambrogio M, Gazzotti P   +2 more
openaire   +3 more sources

Structure and hydrodynamic properties of plectin molecules

Journal of Molecular Biology, 1987
Plectin is a cytoskeletal, high molecular weight protein of widespread and abundant occurrence in cultured cells and tissues. To study its molecular structure, the protein was purified from rat glioma C6 cells and subjected to chemical and biophysical analyses.
R, Foisner, G, Wiche
openaire   +2 more sources