Results 41 to 50 of about 6,887,148 (264)
The likelihood that two proteins interact might depend on the proteins' age [PDF]
It has been previously shown [1] that _S. cerevisiae_ proteins preferentially interact with proteins of the same estimated likely time of origin. To study this observation further, the protein interaction networks of _S. cerevisiae_ and _H.
Pedro Beltrao
core +2 more sources
Diphthamide synthesis is linked to the eEF2‐client chaperone machinery
The diphthamide modification of eukaryotic translation elongation factor 2 (eEF2) is important for accurate protein synthesis. We addressed the potential coordination of de novo eEF2 synthesis with simultaneous or subsequent diphthamide modification. Our work reveals that the co‐chaperones Hgh1 and Cpr7, which are known to support folding of nascent ...
Lars Kaduhr+4 more
wiley +1 more source
Stochastic Ratchet Mechanisms for Replacement of Proteins Bound to DNA [PDF]
Experiments indicate that unbinding rates of proteins from DNA can depend on the concentration of proteins in nearby solution. Here we present a theory of multi-step replacement of DNA-bound proteins by solution-phase proteins. For four different kinetic
Cocco, Simona+2 more
core +3 more sources
The mitochondrial outer membrane iron–sulphur ([Fe‐S]) protein mitoNEET is a target of the type‐2 diabetes drug pioglitazone. Its unknown molecular function is linked to respiratory complex activity and mitochondrial function. We discovered that O2 protects the mitoNEET [2Fe‐2S] cluster against NO oxidation and desensitization towards reduction by H2S.
Thao Nghi Hoang+9 more
wiley +1 more source
Characterization of fungal carbonyl sulfide hydrolase belonging to clade D β‐carbonic anhydrase
Here, we performed a functional analysis of the fungal enzymes belonging to clade D of the β‐class carbonic anhydrase family (β‐D‐CA). The β‐D‐CAs in the basidiomycete Gloeophyllum trabeum and the ascomycete Trichoderma harzianum showed very low activity in the hydration of CO2 but exhibited high activity in the hydrolysis of carbonyl sulfide (COS ...
Ryuka Iizuka+6 more
wiley +1 more source
Alterations of the mitochondrial proteome caused by the absence of mitochondrial DNA: A proteomic view [PDF]
The proper functioning of mitochondria requires that both the mitochondrial and the nuclear genome are functional. To investigate the importance of the mitochondrial genome, which encodes only 13 subunits of the respiratory complexes, the mitochondrial ...
Abdul+39 more
core +4 more sources
The glacier ice worm Mesenchytraeus solifugus survives year‐round at 0 °C. Its ATP6 subunit, which forms a regulatory component of the proton pore in mitochondrial ATP synthase, has a carboxy‐terminal extension not found in any other organism examined to date. Here, we show that fusion of this extension to the homologous AtpB protein in E. coli results
Truman Dunkley+2 more
wiley +1 more source
In modular polyketide synthases, the dehydratase (DH) domain catalyzes the dehydration reaction of the β‐hydroxyacyl unit attached to the cognate acyl carrier protein (ACP) domain. However, it is unclear how DH interacts with ACP during the reaction. In this study, we identified DH–ACP interface residues, providing the first detailed insights into DH ...
Kaede Kotagiri+8 more
wiley +1 more source
Proteomic Analysis of a Noninvasive Human Model of Acute Inflammation and Its Resolution: The Twenty-one Day Gingivitis Model [PDF]
The 21-day experimental gingivitis model, an established noninvasive model of inflammation in response to increasing bacterial accumulation in humans, is designed to enable the study of both the induction and resolution of inflammation.
Barr, Gordon+8 more
core +3 more sources
Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions
This study addresses the inhibition of lytic polysaccharide monooxygenases (LPMOs) by cyanide and explains how and why the magnitude of observed inhibitory effects depends on the way LPMO reactions are setup and on the type of LPMO. Enzymes known as lytic polysaccharide monooxygenases (LPMOs) are mono‐copper polysaccharide‐degrading peroxygenases that ...
Ole Golten+10 more
wiley +1 more source