Zobrazeno 1 - 10
of 267
pro vyhledávání: '"protein-protein recognition"'
Publikováno v:
Molecules, Vol 29, Iss 8, p 1875 (2024)
COVID-19 caused by SARS-CoV-2 has spread around the world. The receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 is a critical component that directly interacts with host ACE2. Here, we simulate the ACE2 recognition processes of RBD of
Externí odkaz:
https://doaj.org/article/27a229cd81654fb19b75230d5c400dda
Calmodulin variants associated with congenital arrhythmia impair selectivity for ryanodine receptors
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2023)
Among its many molecular targets, the ubiquitous calcium sensor protein calmodulin (CaM) recognizes and regulates the activity of ryanodine receptors type 1 (RyR1) and 2 (RyR2), mainly expressed in skeletal and cardiac muscle, respectively. Such regu
Externí odkaz:
https://doaj.org/article/588cee9fd4c74739bddef9e761f9be66
Akademický článek
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Autor:
Francesca Malagrinò, Giuliana Fusco, Valeria Pennacchietti, Angelo Toto, Caterina Nardella, Livia Pagano, Alfonso de Simone, Stefano Gianni
Publikováno v:
Protein science : a publication of the Protein Society. 31(9)
PDZ domains are the most diffused protein-protein interaction modules of the human proteome and are often present in tandem repeats. An example is PDZD2, a protein characterized by the presence of six PDZ domains that undergoes a proteolytic cleavage
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aafd73a79e6d6f89901a87bf72ee7bdb
https://pubmed.ncbi.nlm.nih.gov/36040267
https://pubmed.ncbi.nlm.nih.gov/36040267
Calmodulin variants associated with congenital arrhythmia impair selectivity for ryanodine receptors
Publikováno v:
Frontiers in Molecular Biosciences. 9
Among its many molecular targets, the ubiquitous calcium sensor protein calmodulin (CaM) recognizes and regulates the activity of ryanodine receptors type 1 (RyR1) and 2 (RyR2), mainly expressed in skeletal and cardiac muscle, respectively. Such regu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d134d20c5efc4b1ba6db12dbda91c1a
Autor:
Juliane E. Fiebig, Stella E. Weidauer, Li-Yan Qiu, Markus Bauer, Peter Schmieder, Monika Beerbaum, Jin-Li Zhang, Hartmut Oschkinat, Walter Sebald, Thomas D. Mueller
Publikováno v:
Molecules, Vol 18, Iss 10, Pp 11658-11682 (2013)
Bone Morphogenetic Proteins (BMPs) are secreted protein hormones that act as morphogens and exert essential roles during embryonic development of tissues and organs. Signaling by BMPs occurs via hetero-oligomerization of two types of serine/threonine
Externí odkaz:
https://doaj.org/article/f55b197c51ab4300b27ecbbccd7d73cb
Autor:
Sergey Sergeevich Khruschev, A. M. Abaturova, Aleksandra Nikitichna Diakonova, Dmitry Mikhailovitch Ustinin, D. V. Zlenko, Vladimir Andreevich Fedorov, I. B. Kovalenko, Galina Yu. Riznichenko, Andrei B. Rubin
Publikováno v:
Компьютерные исследования и моделирование, Vol 5, Iss 1, Pp 47-64 (2013)
Protein-protein interactions are of central importance for virtually every process in living matter. Modeling the dynamics of protein association is crucial for understanding their functionality. This paper proposes novel simulation software ProKSim
Externí odkaz:
https://doaj.org/article/4bf040c0670a4436a748bd5530c1d1db
Autor:
Kerry Marie Goodman, Rotem Rubinstein, Chan Aye Thu, Seetha Mannepalli, Fabiana Bahna, Göran Ahlsén, Chelsea Rittenhouse, Tom Maniatis, Barry Honig, Lawrence Shapiro
Publikováno v:
eLife, Vol 5 (2016)
Stochastic cell-surface expression of α-, β-, and γ-clustered protocadherins (Pcdhs) provides vertebrate neurons with single-cell identities that underlie neuronal self-recognition. Here we report crystal structures of ectodomain fragments compris
Externí odkaz:
https://doaj.org/article/5d4ce16104d24b35b29a6deed02c523e
Autor:
Stéphane D. Lemaire, Daniele Tedesco, Pierre Crozet, Laure Michelet, Simona Fermani, Mirko Zaffagnini, Julien Henri
Publikováno v:
Antioxidants, Vol 7, Iss 12, p 171 (2018)
Protein disulfide reduction by thioredoxins (TRXs) controls the conformation of enzyme active sites and their multimeric complex formation. TRXs are small oxidoreductases that are broadly conserved in all living organisms. In photosynthetic eukaryote
Externí odkaz:
https://doaj.org/article/040b337867e749b5892dfcfacaab4058
Akademický článek
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