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Artículo
Dimerization model of the C-terminal RNA Recognition Motif of HuR
(wiley, 2015)
Human antigen R (HuR) is a ubiquitous 32kDa protein comprising three RNA Recognition Motifs (RRMs), whose main function is to bind Adenylate and uridylate Rich Elements (AREs) in 3′ UnTranslated Regions (UTRs) of mRNAs. ...
Artículo
HuR thermal stability is dependent on domain binding and upon phosphorylation
(Springer, 2012)
Human antigen R (HuR) is a multitasking RNA binding protein involved in posttranscriptional regulation by recognizing adenine- and uracile-rich elements placed at the 3′-untranslated regions of messenger RNAs (mRNAs). The ...
Artículo
Communication between L–galactono–1,4–lactone dehydrogenase and cytochrome c
(Wiley: FEBS Journal, 2013-02-25)
l‐galactono‐1,4‐lactone dehydrogenase (GALDH) catalyzes the terminal step of vitamin C biosynthesis in plant mitochondria. Here we investigated the communication between Arabidopsis thaliana GALDH and its natural electron ...
Artículo
The dynamic complex of cytochrome c6 and cytochrome f studied with paramagnetic NMR spectroscopy
(Elsevier B.V., 2014)
The rapid transfer of electrons in the photosynthetic redox chain is achieved by the formation of short-lived complexes of cytochrome b6f with the electron transfer proteins plastocyanin and cytochrome c6. A balance must ...
Artículo
The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
(Oxford University Press, 2008)
K-homology (KH) splicing regulator protein (KSRP) is a multi-domain RNA-binding protein that regulates different steps of mRNA metabolism, from mRNA splicing to mRNA decay, interacting with a broad range of RNA sequences. ...
Artículo
Cytochrome c signalosome in mitochondria
(Springer, 2011)
Cytochrome c delicately tilts the balance between cell life (respiration) and cell death (apoptosis). Whereas cell life is governed by transient electron transfer interactions of cytochrome c inside the mitochondria, the ...
Artículo
The cytochrome f–plastocyanin complex as a model to study transient interactions between redox proteins
(Wiley, 2012)
Transient complexes, with a lifetime ranging between microseconds and seconds, are essential forbiochemical reactions requiring a fast turnover. That is the case of the interactions between proteinsengaged in electron ...
Artículo
Cytochrome c1 exhibits two binding sites for cytochrome c in plants
(Elsevier, 2014)
n plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk ...
Artículo
The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain
(Taylor & Francis, 2014)
T-cell intracellular antigen-1 (TIA-1) is a key DNA/RNA binding protein that regulates translation by sequestering target mRNAs in stress granules (SG) in response to stress conditions. TIA-1 possesses three RNA recognition ...
Artículo
Structure of the Complex between Plastocyanin and Cytochrome f from the Cyanobacterium Nostoc sp. PCC 7119 as Determined by Paramagnetic NMR
(Elsevier, 2005)
The complex between cytochrome f and plastocyanin from the cyanobacterium Nostoc has been characterized by NMR spectroscopy. The binding constant is 16 mm–1, and the lifetime of the complex is much less than 10 ms. ...