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Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond
scientific article published on 01 August 2000
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Europe PubMed Central
PubMed publication ID
11048955
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11048955%20AND%20SRC:MED&resulttype=core&format=json
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1 November 2019
title
Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond
(English)
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Europe PubMed Central
PubMed publication ID
11048955
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1 November 2019
author
Jan Steyaert
series ordinal
4
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Europe PubMed Central
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11048955
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1 November 2019
author name string
S Loverix
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1
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Europe PubMed Central
PubMed publication ID
11048955
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1 November 2019
A Winqvist
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2
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Europe PubMed Central
PubMed publication ID
11048955
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1 November 2019
R Strömberg
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3
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Europe PubMed Central
PubMed publication ID
11048955
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1 November 2019
publication date
1 August 2000
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Europe PubMed Central
PubMed publication ID
11048955
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1 November 2019
published in
Chemistry and Biology
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Europe PubMed Central
PubMed publication ID
11048955
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11048955%20AND%20SRC:MED&resulttype=core&format=json
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1 November 2019
volume
7
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Europe PubMed Central
PubMed publication ID
11048955
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11048955%20AND%20SRC:MED&resulttype=core&format=json
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1 November 2019
issue
8
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Europe PubMed Central
PubMed publication ID
11048955
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1 November 2019
page(s)
651-658
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Europe PubMed Central
PubMed publication ID
11048955
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1 November 2019
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Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine
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Dissecting histidine interactions of ribonuclease T1 with asparagine and glutamine replacements: analysis of double mutant cycles at one position
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The complex between ribonuclease T1 and 3'GMP suggests geometry of enzymic reaction path. An X-ray study
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Functional Interactions among the His40, Glu58 and His92 Catalysts of Ribonuclease T1 as Studied by Double and Triple Mutants
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Subsite interactions of ribonuclease T1: viscosity effects indicate that the rate-limiting step of GpN transesterification depends on the nature of N.
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Nucleophilic activation by positioning in phosphoryl transfer catalyzed by nucleoside diphosphate kinase
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Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases.
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Diastereomers of 5'-O-adenosyl 3'-O-uridyl phosphorothioate: chemical synthesis and enzymic properties
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Double-mutant cycles: a powerful tool for analyzing protein structure and function
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Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography
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A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1.
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Crystallographic Study of Glu58Ala RNase T1.cntdot.2'-Guanosine Monophosphate at 1.9-.ANG. Resolution
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A purification method for labile variants of ribonuclease T1
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Identifiers
DOI
10.1016/S1074-5521(00)00005-3
1 reference
stated in
Europe PubMed Central
PubMed publication ID
11048955
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11048955%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 November 2019
PubMed publication ID
11048955
1 reference
stated in
Europe PubMed Central
PubMed publication ID
11048955
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11048955%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 November 2019
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