Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Maria J. Castañón"'
Autor:
Maria J. Castañón, Gerhard Wiche
Publikováno v:
Cells, Vol 10, Iss 9, p 2453 (2021)
Plectin, a high-molecular-weight cytoskeletal linker protein, binds with high affinity to intermediate filaments of all types and connects them to junctional complexes, organelles, and inner membrane systems. In addition, it interacts with actomyosin
Externí odkaz:
https://doaj.org/article/39175185af7c4ad59215f5d642f2e9c9
Autor:
Maja Žugec, Borut Furlani, Maria J. Castañon, Boštjan Rituper, Irmgard Fischer, Giuseppe Broggi, Rosario Caltabiano, Giuseppe M. V. Barbagallo, Michelino Di Rosa, Daniele Tibullo, Rosalba Parenti, Nunzio Vicario, Saša Simčič, Victorio Martin Pozo Devoto, Gorazd B. Stokin, Gerhard Wiche, Jernej Jorgačevski, Robert Zorec, Maja Potokar
Publikováno v:
Journal of Biomedical Science, Vol 31, Iss 1, Pp 1-22 (2024)
Abstract Background The expression of aquaporin 4 (AQP4) and intermediate filament (IF) proteins is altered in malignant glioblastoma (GBM), yet the expression of the major IF-based cytolinker, plectin (PLEC), and its contribution to GBM migration an
Externí odkaz:
https://doaj.org/article/32ce5b5e6d344a77a4c23f8a8c7dcde0
Autor:
Gerhard Wiche, Maria J. Castañón
Publikováno v:
Encyclopedia of Biological Chemistry III ISBN: 9780128220405
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c7f82aa0379ba783343f43df7528212
https://doi.org/10.1016/b978-0-12-819460-7.00263-2
https://doi.org/10.1016/b978-0-12-819460-7.00263-2
Autor:
Gerhard Wiche, Christian Thiel, Nuria Muelas, Mirjam Schowalter, Matthias Türk, Herminia Argente‐Escrig, Dorothea Schultheis, Juan J. Vílchez, Christoph S. Clemen, Harald Herrmann, Lisa Kamm, Rolf Schröder, Maria J. Castañón
Publikováno v:
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY
r-IIS La Fe. Repositorio Institucional de Producción Científica del Instituto de Investigación Sanitaria La Fe
instname
r-IIS La Fe. Repositorio Institucional de Producción Científica del Instituto de Investigación Sanitaria La Fe
instname
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3aee7e20ceaf10a5be18e90ff6e6267e
https://elib.dlr.de/136064/
https://elib.dlr.de/136064/
Autor:
Kristin Kernland Lang, Miranda Nijenhuis, Katarzyna B. Gostynska, Marcel F. Jonkman, Maria J. Castañón, Hendrikus Pas, Gerhard Wiche, Henny H. Lemmink, Anna M.G. Pasmooij
Publikováno v:
Human Molecular Genetics, 24(11), 3155-3162. Oxford University Press
Gostyńska, Katarzyna B.; Nijenhuis, Miranda; Lemmink, Henny; Pas, Hendri H.; Pasmooij, Anna M.G.; Kernland Lang, Kristin; Castañón, Maria J.; Wiche, Gerhard; Jonkman, Marcel F. (2015). Mutation in exon 1a of PLEC, leading to disruption of plectin isoform 1a, causes autosomal-recessive skin-only epidermolysis bullosa simplex. Human molecular genetics, 24(11), pp. 3155-3162. Oxford University Press 10.1093/hmg/ddv066
Gostyńska, Katarzyna B.; Nijenhuis, Miranda; Lemmink, Henny; Pas, Hendri H.; Pasmooij, Anna M.G.; Kernland Lang, Kristin; Castañón, Maria J.; Wiche, Gerhard; Jonkman, Marcel F. (2015). Mutation in exon 1a of PLEC, leading to disruption of plectin isoform 1a, causes autosomal-recessive skin-only epidermolysis bullosa simplex. Human molecular genetics, 24(11), pp. 3155-3162. Oxford University Press 10.1093/hmg/ddv066
PLEC, the gene encoding the cytolinker protein plectin, has eight tissue-specific isoforms in humans, arising by alternate splicing of the first exon. To date, all PLEC mutations that cause epidermolysis bullosa simplex (EBS) were found in exons comm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bd8f6645de9a7513236b8fa45cd826c
http://doc.rero.ch/record/299576/files/ddv066.pdf
http://doc.rero.ch/record/299576/files/ddv066.pdf
Publikováno v:
Walko, G, Castañón, M J & Wiche, G 2016, ' Molecular architecture and function of the hemidesmosome ', Cell and Tissue Research, vol. 360, no. 2, pp. 363-378 . https://doi.org/10.1007/s00441-014-2061-z
Cell and Tissue Research
Cell and Tissue Research
Hemidesmosomes are multiprotein complexes that facilitate the stable adhesion of basal epithelial cells to the underlying basement membrane. The mechanical stability of hemidesmosomes relies on multiple interactions of a few protein components that f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::897f49e9b1be36ac62ba4715cb5f5823
https://kclpure.kcl.ac.uk/ws/files/56064160/Molecular_architecture_and_WALKO_Published_May2015_GOLD_VoR.pdf
https://kclpure.kcl.ac.uk/ws/files/56064160/Molecular_architecture_and_WALKO_Published_May2015_GOLD_VoR.pdf
Publikováno v:
Experimental Cell Research. 314:3570-3580
Plectin is a typical cytolinker protein that connects intermediate filaments to the other cytoskeletal filament systems and anchors them at membrane-associated junctional sites. One of the most important binding partners of plectin in fibroblasts is
Autor:
Radovan Spurny, Gottfried Koöhler, Maria J. Castañón, Kamaran Abdoulrahman, Lubomír Janda, Dominik Ruönzler, Gerhard Wiche
Publikováno v:
Journal of Biological Chemistry. 282:8175-8187
As an intermediate filament (IF)-based cytolinker protein, plectin plays a key role in the maintenance of cellular cytoarchitecture and serves at the same time as a scaffolding platform for signaling cascades. Consisting of six structural repeats (R1
Publikováno v:
Current opinion in cell biology. 32
Intermediate filaments (IFs) are involved in multiple cellular processes that are essential for the maintenance of cell and tissue integrity as well as response and adaption to stress. Mainly through pathological manifestations in patients and the an
Autor:
Maria J. Castañón, Susanne Oehler, Günther A. Rezniczek, Rudolf Hauptmann, Gerhard Wiche, Peter Fuchs, Daniel Spazierer, Michael Zörer
Publikováno v:
Human Molecular Genetics. 8:2461-2472
Plectin, the most versatile cytolinker identified to date, has essential functions in maintaining the mechanical integrity of skin, skeletal muscle and heart, as indicated by analyses of plectin-deficient mice and humans. Expression of plectin in a v