Identification of lipid-accessible sites on the nephrops 16-kDa proteolipid incorporated into a hybrid vacuolar H(+)-ATPase: site-directed labeling with N-(1-Pyrenyl)cyclohexylcarbodiimide and fluorescence quenching analysis.

Identification of lipid-accessible sites on the nephrops 16-kDa proteolipid incorporated into a hybrid vacuolar H(+)-ATPase: site-directed labeling with N-(1-Pyrenyl)cyclohexylcarbodiimide and fluorescence quenching analysis.

Item
http://www.wikidata.org/entity/Q52864017
Flexibility within the rotor and stators of the vacuolar H+-ATPaseTopological characterization of the c, c', and c" subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae.Proton translocation driven by ATP hydrolysis in V-ATPasesA single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzymeIdentification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat liver carnitine palmitoyltransferase I that are important for catalytic activity and malonyl-CoA sensitivityMembrane embedded location of Na+ or H+ binding sites on the rotor ring of F1F0 ATP synthases.Neurotransmitter release through the V0 sector of V-ATPase.Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.EPR Studies of V-ATPase with Spin-Labeled Inhibitors DCC and Archazolid: Interaction Dynamics with Proton Translocating Subunit c.Evidence that there are two copies of subunit c" in V0 complexes in the vacuolar H+-ATPase.The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae.TM2 but not TM4 of subunit c'' interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking.A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator.A model for the proteolipid ring and bafilomycin/concanamycin-binding site in the vacuolar ATPase of Neurospora crassa.New biophysical probes for structure-activity analyses of vacuolar-H+ -ATPase enzymes.
P2860

Identification of lipid-accessible sites on the nephrops 16-kDa proteolipid incorporated into a hybrid vacuolar H(+)-ATPase: site-directed labeling with N-(1-Pyrenyl)cyclohexylcarbodiimide and fluorescence quenching analysis.

Item
http://www.wikidata.org/entity/Q52864017
description
2000 nî lūn-bûn
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2000年の論文
@ja
2000年学术文章
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2000年学术文章
@zh
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
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2000年學術文章
@zh-hant
name
Identification of lipid-access ...... rated into a hybrid vacuolar H
@nl
Identification of lipid-access ...... uorescence quenching analysis.
@en
Identification of lipid-access ...... uorescence quenching analysis.
@en-gb
type
label
Identification of lipid-access ...... rated into a hybrid vacuolar H
@nl
Identification of lipid-access ...... uorescence quenching analysis.
@en
Identification of lipid-access ...... uorescence quenching analysis.
@en-gb
prefLabel
Identification of lipid-access ...... rated into a hybrid vacuolar H
@nl
Identification of lipid-access ...... uorescence quenching analysis.
@en
Identification of lipid-access ...... uorescence quenching analysis.
@en-gb
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Identification of lipid-access ...... uorescence quenching analysis.
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698