Moonlighting Proteins: The Case of the Hexokinases [PDF]
Moonlighting proteins are defined as proteins with two or more functions that are unrelated and independent to each other, so that inactivation of one of them should not affect the second one and vice versa.
Carolina Rodríguez-Saavedra +5 more
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DnaK Functions as a Moonlighting Protein on the Surface of Mycoplasma hyorhinis Cells [PDF]
Mycoplasma hyorhinis is a common pathogen of swine and is also associated with various human tumors. It causes systemic inflammation, typically polyserositis and polyarthritis, in some infected pigs. However, the pathogenic mechanism of M.
Yao Li +25 more
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Moonlighting protein prediction using physico-chemical and evolutional properties via machine learning methods [PDF]
Background Moonlighting proteins (MPs) are a subclass of multifunctional proteins in which more than one independent or usually distinct function occurs in a single polypeptide chain.
Farshid Shirafkan +4 more
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Pathogen Moonlighting Proteins: From Ancestral Key Metabolic Enzymes to Virulence Factors
Moonlighting and multitasking proteins refer to proteins with two or more functions performed by a single polypeptide chain. An amazing example of the Gain of Function (GoF) phenomenon of these proteins is that 25% of the moonlighting functions of our ...
Luis Franco-Serrano +9 more
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The term moonlighting proteins refers to those proteins that present alternative functions performed by a single polypeptide chain acquired throughout evolution (called canonical and moonlighting, respectively).
Mario Huerta +7 more
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Moonlighting Proteins: Diverse Functions Found in Fungi
Moonlighting proteins combine multiple functions in one polypeptide chain. An increasing number of moonlighting proteins are being found in diverse fungal taxa that vary in morphology, life cycle, and ecological niche.
Nicole J. Curtis +3 more
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Dancing to Another Tune—Adhesive Moonlighting Proteins in Bacteria
Biological moonlighting refers to proteins which express more than one function. Moonlighting proteins occur in pathogenic and commensal as well as in Gram-positive and Gram-negative bacteria.
Veera Kainulainen, Timo K. Korhonen
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Structural variability of multifunctional proteins indicates frequent stochastic evolution of protein oligomers [PDF]
Recently, it has been suggested that the evolution of many protein homomer complexes follows a neutral pattern, with little effect on their biochemical function.
György Abrusán, Aleksej Zelezniak
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Beyond Bioenergetics: Moonlighting Functions of F<sub>1</sub>F<sub>O</sub>-ATPase From ATP Synthesis to an ATP-Wasting Death Switch. [PDF]
ABSTRACT Mitochondrial F1FO‐ATPase is classically viewed as the “splendid” rotary nanomachine that sustains life by converting the proton‐motive force (pmf) into ATP. Yet this same complex can adopt a second, context‐dependent function that links bioenergetics to cell fate.
Nesci S.
europepmc +2 more sources
Quantitative Phosphoproteomics Identifies Myofibrillar Protein Phosphorylation Mediated by Pyruvate Kinase M2 in Beef [PDF]
Pyruvate kinase M2 (PKM2) influences meat quality through glycolysis and also exhibits its moonlighting function as a protein kinase that catalyzes protein phosphorylation.
Ying Xu +5 more
doaj +2 more sources

