Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Zsuzsanna Dosztanyi"'
Autor:
Tamás Szaniszló, Máté Fülöp, Mátyás Pajkos, Gábor Erdős, Réka Ágnes Kovács, Henrietta Vadászi, József Kardos, Zsuzsanna Dosztányi
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-15 (2022)
Abstract Dynein light chain LC8 is a small dimeric hub protein that recognizes its partners through short linear motifs and is commonly assumed to drive their dimerization. It has more than 100 known binding partners involved in a wide range of cellu
Externí odkaz:
https://doaj.org/article/49d83ae47f5e4b64ab62ad0cf6eb3be4
The Origin of Discrepancies between Predictions and Annotations in Intrinsically Disordered Proteins
Publikováno v:
Biomolecules, Vol 13, Iss 10, p 1442 (2023)
Disorder prediction methods that can discriminate between ordered and disordered regions have contributed fundamentally to our understanding of the properties and prevalence of intrinsically disordered proteins (IDPs) in proteomes as well as their fu
Externí odkaz:
https://doaj.org/article/51cbffcf289941769fb068a1cf1fc15f
Autor:
Kristina Kastano, Pablo Mier, Zsuzsanna Dosztányi, Vasilis J. Promponas, Miguel A. Andrade-Navarro
Publikováno v:
Biomolecules, Vol 12, Iss 10, p 1486 (2022)
Intrinsically disordered regions (IDRs) in protein sequences are flexible, have low structural constraints and as a result have faster rates of evolution. This lack of evolutionary conservation greatly limits the use of sequence homology for the clas
Externí odkaz:
https://doaj.org/article/cdfa6d6b59704347ab8b8411931611df
Publikováno v:
Biomolecules, Vol 11, Iss 3, p 381 (2021)
Many proteins contain intrinsically disordered regions (IDRs) which carry out important functions without relying on a single well-defined conformation. IDRs are increasingly recognized as critical elements of regulatory networks and have been also a
Externí odkaz:
https://doaj.org/article/cf6063ae62914c77a4380e75ba280477
Autor:
Kristina Kastano, Gábor Erdős, Pablo Mier, Gregorio Alanis-Lobato, Vasilis J. Promponas, Zsuzsanna Dosztányi, Miguel A. Andrade-Navarro
Publikováno v:
Biomolecules, Vol 10, Iss 10, p 1413 (2020)
Intrinsically disordered proteins (IDPs) contain regions lacking intrinsic globular structure (intrinsically disordered regions, IDRs). IDPs are present across the tree of life, with great variability of IDR type and frequency even between closely re
Externí odkaz:
https://doaj.org/article/4c1f0cc5f84f4716b084e3aad940f6e0
Autor:
Boglarka Zambo, Evelina Edelweiss, Bastien Morlet, Luc Negroni, Matyas Pajkos, Zsuzsanna Dosztanyi, Soren Ostergaard, Gilles Trave, Jocelyn Laporte, Gergo Gogl
Publikováno v:
eLife, Vol 13 (2024)
Truncation of the protein-protein interaction SH3 domain of the membrane remodeling Bridging Integrator 1 (BIN1, Amphiphysin 2) protein leads to centronuclear myopathy. Here, we assessed the impact of a set of naturally observed, previously uncharact
Externí odkaz:
https://doaj.org/article/f5c33ef1efd744989b95c329d4a4ad45
Publikováno v:
PLoS ONE, Vol 8, Iss 2, p e56465 (2013)
The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core.
Externí odkaz:
https://doaj.org/article/bd91d0b4363e4eb3bbbe429b0ccd771b
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46829 (2012)
Intrinsically disordered proteins (IDPs) exist without the presence of a stable tertiary structure in isolation. These proteins are often involved in molecular recognition processes via their disordered binding regions that can recognize partner mole
Externí odkaz:
https://doaj.org/article/876c8045480c4bb59ff80de9245bd862
Publikováno v:
PLoS Computational Biology, Vol 7, Iss 7, p e1002118 (2011)
Lengthy co-evolution of Homo sapiens and Mycobacterium tuberculosis, the main causative agent of tuberculosis, resulted in a dramatically successful pathogen species that presents considerable challenge for modern medicine. The continuous and ever in
Externí odkaz:
https://doaj.org/article/1fa61ac5b19c4e768dd54fc9b04c8cef
Publikováno v:
PLoS Computational Biology, Vol 5, Iss 5, p e1000376 (2009)
Many disordered proteins function via binding to a structured partner and undergo a disorder-to-order transition. The coupled folding and binding can confer several functional advantages such as the precise control of binding specificity without incr
Externí odkaz:
https://doaj.org/article/d6acbe0e3afb4baca57062bf2b6689bd