(Q37537953)

20 August 2017

Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme (English)

1 reference

20 August 2017

W W Bachovchin

1

1 reference

PMCID

390887

20 August 2017

language of work or name

English

0 references

publication date

1 December 1985

1 reference

Proceedings of the National Academy of Sciences of the United States of America

20 August 2017

1 reference

20 August 2017

82

1 reference

20 August 2017

7948-7951

1 reference

20 August 2017

23

1 reference

Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin A.alpha

20 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=390887

Re-examination of the charge relay system in subtilisin comparison with other serine proteases

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=390887

The charge-relay system of serine proteinases: Proton magnetic resonance titration studies of the four histidines of porcine trypsin

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=390887

High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors.

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=390887

Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=390887

Hydrogen bonds in serine proteinases and their complexes with protein proteinase inhibitors. Proton nuclear magnetic resonance studies

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=390887

High resolution nuclear magnetic resonance study of the histidine—Aspartate hydrogen bond in chymotrypsin and chymotrypsinogen

25 June 2018

1 reference

12 December 2020

High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. I. The hydrogen bonded protons of the "charge relay" system

1 reference

12 December 2020

Nitrogen-15-labeled yeast tRNAPhe: double and two-dimensional heteronuclear NMR of guanosine and uracil ring NH groups

1 reference

12 December 2020

Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer

1 reference

12 December 2020

Proton nuclear magnetic resonance evidence for the absence of a stable hydrogen bond between the active site aspartate and histidine residues of native subtilisins and for its presence in thiolsubtilisins

1 reference

12 December 2020

A detailed structural comparison between the charge relay system in chymotrypsinogen and in alpha-chymotrypsin

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.82.23.7948

1 reference

20 August 2017

0 references

1 reference

20 August 2017

1 reference

PMCID

390887