about
Active site opening and closure control translocation of multisubunit RNA polymeraseTwo independent evolutionary routes to Na+/H+ cotransport function in membrane pyrophosphatases.Na+-translocating membrane pyrophosphatases are widespread in the microbial world and evolutionarily precede H+-translocating pyrophosphatases.Cytochrome cbb3 of Thioalkalivibrio is a Na+-pumping cytochrome oxidase.Membrane-integral pyrophosphatase subfamily capable of translocating both Na+ and H+.Pyrophosphate-fueled Na+ and H+ transport in prokaryotes.Membrane Na+-pyrophosphatases can transport protons at low sodium concentrations.CBR antimicrobials alter coupling between the bridge helix and the β subunit in RNA polymerase.Evolutionarily divergent, Na+-regulated H+-transporting membrane-bound pyrophosphatases.Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium for activity.Mutual effects of cationic ligands and substrate on activity of the Na+-transporting pyrophosphatase of Methanosarcina mazei.Pausing controls branching between productive and non-productive pathways during initial transcription in bacteria.Monitoring translocation of multisubunit RNA polymerase along the DNA with fluorescent base analogues.Role of the potassium/lysine cationic center in catalysis and functional asymmetry in membrane-bound pyrophosphatasesThe RNA polymerase clamp interconverts dynamically among three states and is stabilized in a partly closed state by ppGpp
P50
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P50
description
investigador
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researcher
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wetenschapper
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name
Anssi Malinen
@en
Anssi Malinen
@nl
type
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Anssi Malinen
@en
Anssi Malinen
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altLabel
Anssi M Malinen
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prefLabel
Anssi Malinen
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Anssi Malinen
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P106
P21
P31
P496
0000-0003-2987-2649