Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Adél Szabó"'
Autor:
Judit Ovádi, Marianna Csaplár, Matthias Schiedel, Attila Lehotzky, Péter Lőw, Manfred Jung, Tibor Szénási, Adél Szabó, Judit Oláh, Sándor Szunyogh
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Scientific Reports
Scientific Reports
The microtubule network exerts multifarious functions controlled by its decoration with various proteins and post-translational modifications. The disordered microtubule associated Tubulin Polymerization Promoting Protein (TPPP/p25) and the NAD+-depe
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1852:2653-2661
The pathological interaction of intrinsically disordered proteins, such as α-synuclein (SYN) and Tubulin Polymerization Promoting Protein (TPPP/p25), is often associated with neurodegenerative disorders. These hallmark proteins are co-enriched and c
Autor:
Attila Lehotzky, Tamás Szaniszló, Tibor Szénási, Adél Szabó, Timea Berki, László Nyitray, Judit Ovádi, Judit Oláh, Sándor Szunyogh
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1866:118556
Degradation of unwanted proteins is important in protein quality control cooperating with the dynein/dynactin-mediated trafficking along the acetylated microtubule (MT) network. Proteins associated directly/indirectly with tubulin/MTs play crucial ro
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1852:83-91
Tubulin Polymerization Promoting Protein/p25 (TPPP/p25), a neomorphic moonlighting protein displaying both physiological and pathological functions, plays a crucial role in the differentiation of the zinc-rich oligodendrocytes, the major constituent
Publikováno v:
Scientific Reports
Tubulin Polymerization Promoting Protein (TPPP/p25) is a brain-specific disordered protein that modulates the dynamics and stability of the microtubule network by its assembly promoting, cross-linking and acetylation enhancing activities. In normal b
Tubulin polymerization promoting proteins (TPPPs) constitute a eukaryotic protein family. There are three TPPP paralogs in the human genome, denoted as TPPP1–TPPP3. TPPP1 and TPPP3 are intrinsically unstructured proteins (IUPs) that bind and polyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76c9d62c29747e4b888766a5ca25fd9a
https://www.bib.irb.hr/1251196
https://www.bib.irb.hr/1251196
Autor:
András Láng, Judit Oláh, Sándor Szunyogh, András Perczel, Adél Szabó, Vladimir N. Uversky, Judit Ovádi, Tibor Szénási, Attila Lehotzky
Publikováno v:
Biochimica et biophysica acta. Molecular basis of disease. 1863(1)
The hallmarks of Parkinson's disease and other synucleinopathies, Tubulin Polymerization Promoting Protein (TPPP/p25) and α-synuclein (SYN) have two key features: they are disordered and co-enriched/co-localized in brain inclusions. These Neomorphic
Autor:
Fruzsina Babos, Judit Ovádi, Judit Oláh, Attila Lehotzky, Sándor Szunyogh, Adél Szabó, Elemér Vass, Anna Magyar, Natália Tőkési, Emma Hlavanda
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. (4):547-557
The disordered Tubulin Polymerization Promoting Protein (TPPP/p25), a prototype of neomorphic moonlighting proteins, displays physiological and pathological functions by interacting with distinct partners. Here the role of the disordered N- and C-ter