Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
about
Fe2+-catalyzed site-specific cleavage of the large subunit of ribulose 1,5-bisphosphate carboxylase close to the active site.Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry.Photochemical protease: site-specific photocleavage of hen egg lysozyme and bovine serum albumin.Cleavage of recombinant proteins at poly-His sequences by Co(II) and Cu(II).Binding of the sigma 70 protein to the core subunits of Escherichia coli RNA polymerase, studied by iron-EDTA protein footprinting.Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.Chiral protein scissors: high enantiomeric selectivity for binding and its effect on protein photocleavage efficiency and specificity.Fe(2+)-tetracycline-mediated cleavage of the Tn10 tetracycline efflux protein TetA reveals a substrate binding site near glutamine 225 in transmembrane helix 7.Directed hydroxyl radical probing of 16S rRNA using Fe(II) tethered to ribosomal protein S4Metallotherapeutics: novel strategies in drug design.Modeling of the DNA-binding site of yeast Pms1 by mass spectrometry.Double-stranded cleavage of pBR322 by a diiron complex via a "hydrolytic" mechanismMapping the rRNA neighborhood of the acceptor end of tRNA in the ribosome.Orientation of Pseudomonas aeruginosa ExsA monomers bound to promoter DNA and base-specific contacts with the P(exoT) promoterThe two alpha subunits of Escherichia coli RNA polymerase are asymmetrically arranged and contact different halves of the DNA upstream elementBleomycins: towards better therapeutics.Conservation of sigma-core RNA polymerase proximity relationships between the enhancer-independent and enhancer-dependent sigma classes.Fe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domainsQuantitative studies of ribosome conformational dynamics.Conformation-dependent cleavage of staphylococcal nuclease with a disulfide-linked iron chelateMapping protein-protein interactions by localized oxidation: consequences of the reach of hydroxyl radicalDeterminants of RNA polymerase alpha subunit for interaction with beta, beta', and sigma subunits: hydroxyl-radical protein footprintingIdentification of an RNA-binding Site in the ATP binding domain of Escherichia coli Rho by H2O2/Fe-EDTA cleavage protection studies.Directed hydroxyl radical probing of 16S ribosomal RNA in ribosomes containing Fe(II) tethered to ribosomal protein S20.Phosphorylation-induced signal propagation in the response regulator ntrC.Ribosomal localization of translation initiation factor IF2Scleroderma autoantigens are uniquely fragmented by metal-catalyzed oxidation reactions: implications for pathogenesisMapping metal ions at the catalytic centres of two intron-encoded endonucleases.Core-sigma interaction: probing the interaction of the bacteriophage T4 gene 55 promoter recognition protein with E.coli RNA polymerase core.Metal-catalyzed oxidation of protein methionine residues in human parathyroid hormone (1-34): formation of homocysteine and a novel methionine-dependent hydrolysis reaction.Directed hydroxyl radical probing reveals Upf1 binding to the 80S ribosomal E site rRNA at the L1 stalk.Interaction and photo-induced cleavage studies of a copper based chemotherapeutic drug with human serum albumin: spectroscopic and molecular docking study.The Interaction of the Metallo-Glycopeptide Anti-Tumour Drug Bleomycin with DNA.Importance of Metal-Ion Exchange for the Biological Activity of Coordination Complexes of the Biomimetic Ligand N4Py.
P2860
Q30167647-84171632-6E25-4773-8EFD-4D0B85F3505BQ30329285-BB506A6D-E1AE-47BD-A8B3-159BED252DC7Q32028771-3B77ADAC-C390-43C1-8A1B-E98EA6AC30B9Q33289278-9F96645D-77CB-49AD-A5BF-F78EB20C8A9DQ33598609-C811E8E7-2895-41DD-AD6E-56EEB49584C6Q33891527-F5620730-3309-4181-B82B-5BEBA81C18EBQ34026750-D7AC4D91-9133-4DC3-B0A7-882701C5F80FQ34318526-395CAC6F-9BF5-47A8-BCEC-831C7F929C3DQ34690011-3542409F-88F4-4EAA-93A8-86C61AF04E9CQ34775956-7B58ED81-B5BC-4023-BCCD-A70D2E17C5D1Q34884364-39AE9294-E030-4BB6-8E23-BF32D2201829Q34984768-7E5504C0-A1F8-425C-BCDB-635BD9B1B926Q35853437-26C7A4C4-7A4F-46C3-A2B8-65B1D5D22FF7Q35943272-8CD21B7B-FBAA-487D-88B0-1572B3CA6FE2Q36020417-7FAF450A-7D53-4B1B-A1C2-3689700D4E30Q36026763-F4D99657-5A8B-422B-A751-00C1699609CCQ36079882-707E90AC-725C-4877-B0C4-70A35B102B82Q36569774-D60E7D01-7BC4-4E1E-820A-322DA1C213D3Q37029425-EA2C6442-50B7-429A-8216-2B924B95ABFAQ37107571-DD8E3004-9711-45A9-B0D2-17F7F08D8097Q37268676-875B0482-5152-461B-B984-B92920334BD8Q37329263-C8A7B920-32AC-4D44-9912-932B4B913266Q38300500-EDE8CE29-97E0-46C6-B1F8-085DBB4A6A7EQ38330575-0D75AA85-5AAD-4EDD-A6B4-F021B15CF5A8Q39500703-6ACE6A90-A4BE-4652-8303-9A0A2BEF0E67Q41820033-89AA0993-DE52-4C22-9E52-ACD46E10F294Q41968463-C5676302-D4CF-4F00-AC77-0AEBC2358C6AQ42620535-04B7C437-36D0-4D32-949C-12EED02C8825Q42639942-18059E5C-486F-4EE9-942C-5E585010F91DQ43116396-C57E8BBA-5308-4F23-91C4-CE3B1B2D3AF5Q47281253-01A6CBD2-BE44-4C2D-B385-FFE5D1950F39Q53157409-3C85399E-8A1B-406F-ABEF-09B929F3DC6DQ54974045-C9A5ED5C-9798-4340-8CA9-0AA0C193C01BQ55439551-A502FC90-10EA-4FC0-B6D6-4065020DE823
P2860
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
@en
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
@nl
type
label
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
@en
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
@nl
prefLabel
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
@en
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
@nl
P2860
P356
P1476
Transfer of oxygen from an artificial protease to peptide carbon during proteolysis.
@en
P2093
P2860
P304
10578-10582
P356
10.1073/PNAS.88.23.10578
P407
P577
1991-12-01T00:00:00Z