Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallograph-Reference-Cited by-同舟云学术

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Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallograph

Published:1998-04 Issue:4 Volume:5 Page:280-283
ISSN:1072-8368
Container-title:Nature Structural Biology
language:
Short-container-title:Nat Struct Mol Biol

Author:

Zegers Ingrid,Loris Remy,Dehollander Gillis,Haikal Abdel Fattah,Poortmans Freddy,Steyaert Jan,Wyns Lode

Publisher

Springer Science and Business Media LLC

Subject

Genetics,Biochemistry,Structural Biology

Reference30 articles.

1. 13 Ribonuclease T1

2. Base-group specificity at the primary recognition site of ribonuclease T1 for minimal RNA substrates

3. Energetics of Catalysis by Ribonucleases: Fate of the 2',3'-Cyclic Phosphodiester Intermediate

4. Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine

5. A Decade of Protein Engineering on Ribonuclease T1- Atomic Dissection of the Enzyme-Substrate Interactions

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3. RNA Cleavage Properties of Nucleobase-Specific RNase MC1 and Cusativin Are Determined by the Dinucleotide-Binding Interactions in the Enzyme-Active Site;International Journal of Molecular Sciences;2022-06-24

4. Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase–RNA complexes;Journal of Structural Biology: X;2022

5. Nucleotide binding architecture for secreted cytotoxic endoribonucleases;Biochimie;2013-06

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