8-N(3)-3'-biotinyl-ATP, a novel monofunctional reagent: differences in the F(1)- and V(1)-ATPases by means of the ATP analogue.
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Summary
UV irradiation ofTF(1) in the presence of 8-N(3)-3'-biotinyl-ATP results in a nucleotide-dependent binding of the analogue in the noncatalytic alpha and the catalytic beta subunits of TF(1), demonstrating the suitability of this analogue as a potential photoaffinity label.
- Type
- article
- Published
- 2001-09-07
- Cited by
- 18
- References
- 49
- Access
- Open access
- OpenAlex
- https://openalex.org/W11527430
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:43279155
Keywords
Artificial intelligence, Computer science, Optical flow, Pattern recognition (psychology), Region of interest
References
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- Inhibition of fructose-1,6-biphosphatase by the photoaffinity AMP analog, 8-azidoadenosine 5'-monophosphate.
- Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo.
- Protein measurement with the Folin phenol reagent.
- The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
- Localisation of adenine nucleotide-binding sites on beef-heart mitochondrial ATPase by photolabelling with 8-azido-ADP and 8-azido-ATP.
- 3′-O-(4-Benzoyl)benzoyladenosine 5′-Triphosphate Inhibits Activity of the Vacuolar (H+)-ATPase from Bovine Brain Clathrin-coated Vesicles by Modification of a Rapidly Exchangeable, Noncatalytic Nucleotide Binding Site on the B Subunit*
- Purification and Properties of a Cytosolic V1-ATPase*
- Post-translational Modifications of Endothelin Receptor B from Bovine Lungs Analyzed by Mass Spectrometry*
- An automated continuous assay of membrane-bound and solube ATPases and related enzymes.
- Inhibition and Labeling of the Coated Vesicle V-ATPase by 2-Azido-[32P]ATP (*)
- Structure of theEscherichia coli ATP synthase and role of the γ and ε subunits in coupling catalytic site and proton channeling functions
- Quaternary structure of V1 and F1 ATPase: significance of structural homologies and diversities.
- Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing.
- Aryl azide photolabels in biochemistry
- Characterization of a cysteine-containing peptide after affinity labelling of Ca2+-ATPase of sarcoplasmic reticulum with the disulfide of 3'(2')-O-biotinyl-thioinosine triphosphate.
- Selectivity of modification when latent and activated forms of the chloroplast F1-ATPase are inactivated by 7-chloro-4-nitrobenzofurazan.
- Regulation of Plasma Membrane V-ATPase Activity by Dissociation of Peripheral Subunits (*)
Cited by
- Subunit Composition, Structure, and Distribution of Bacterial V-Type ATPases
- Synthesis of γ‐Phosphate‐Labeled and Doubly Labeled Adenosine Triphosphate Analogs
- ATP/ADP Binding to a Novel Nucleotide Binding Domain of the Reticulocyte-binding Protein Py235 of Plasmodium yoelii*
- Structural Determination of Functional Units of the Nucleotide Binding Domain (NBD94) of the Reticulocyte Binding Protein Py235 of Plasmodium yoelii
- Resolution of the V1 ATPase from Manduca sexta into Subcomplexes and Visualization of an ATPase-active A3B3EG Complex by Electron Microscopy*
- Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B.
- Cloning, purification, and nucleotide-binding traits of the catalytic subunit A of the V1VO ATPase from Aedes albopictus.
- Expression, purification, and characterization of subunit E, an essential subunit of the vacuolar ATPase.
- Atrial natriuretic peptide‐dependent photolabeling of a regulatory ATP‐binding site on the natriuretic peptide receptor‐A
- Functional Role of Arginine 375 in Transmembrane Helix 6 of Multidrug Resistance Protein 4 (MRP4/ABCC4)
- Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding
- The stimulating role of subunit F in ATPase activity inside the A1-complex of the Methanosarcina mazei Gö1 A1AO ATP synthase.
- Novel insights into the biological function of the high molecular weight PY235 rhoptry protein of plasmodium Yoelii.
- ATP synthases: structure, function and evolution of unique energy converters
- Adenosine triphosphate regulates the activity of guinea pig Cav1.2 channel by direct binding to the channel in a dose-dependent manner.
- Unravelling structural and mechanistic elements of catalytic subunits A and coupling subunit F and structural and kinetic studies of the A3B3D and A3B3DF-subcomplexes of the Methanosarcina mazei Gö1 provide insights into the single molecule dynamics of this engine
- The pseudokinase domains of guanylyl cyclase–A and –B allosterically increase the affinity of their catalytic domains for substrate
- The Role of Post-Translational Modifications and Allostery in the Receptor Guanylyl Cyclases GC-A and GC-B
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