Year |
Citation |
Score |
2015 |
Heckler EJ, Kholodovych V, Jain M, Liu T, Li H, Beuve A. Mapping Soluble Guanylyl Cyclase and Protein Disulfide Isomerase Regions of Interaction. Plos One. 10: e0143523. PMID 26618351 DOI: 10.1371/Journal.Pone.0143523 |
0.473 |
|
2014 |
Heckler E, Jain M, Kholodovych V, Li H, Beuve A. Thiol-Based Redox Regulation of the Nitric Oxide Receptor, Soluble Guanylyl Cyclase (SGC) Free Radical Biology and Medicine. 76: S15. DOI: 10.1016/J.Freeradbiomed.2014.10.492 |
0.315 |
|
2013 |
Heckler EJ, Crassous PA, Baskaran P, Beuve A. Protein disulfide-isomerase interacts with soluble guanylyl cyclase via a redox-based mechanism and modulates its activity. The Biochemical Journal. 452: 161-9. PMID 23477350 DOI: 10.1042/Bj20130298 |
0.4 |
|
2013 |
Heckler EJ, Jain M, Crassous P, Rossi AR, Li H, Beuve A. Thiol-redox proteins interact with soluble guanylyl cyclase and modulate its activity Bmc Pharmacology and Toxicology. 14. DOI: 10.1186/2050-6511-14-S1-O21 |
0.466 |
|
2011 |
Baskaran P, Heckler EJ, van den Akker F, Beuve A. Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity. Plos One. 6: e26976. PMID 22096512 DOI: 10.1371/Journal.Pone.0026976 |
0.493 |
|
2011 |
Baskaran P, Heckler EJ, van den Akker F, Beuve A. Aspartate 102 in the heme domain of soluble guanylyl cyclase has a key role in NO activation. Biochemistry. 50: 4291-7. PMID 21491881 DOI: 10.1021/Bi2004087 |
0.466 |
|
2010 |
Alon A, Heckler EJ, Thorpe C, Fass D. QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains. Febs Letters. 584: 1521-5. PMID 20211621 DOI: 10.1016/J.Febslet.2010.03.001 |
0.692 |
|
2008 |
Heckler EJ, Alon A, Fass D, Thorpe C. Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis. Biochemistry. 47: 4955-63. PMID 18393449 DOI: 10.1021/Bi702522Q |
0.596 |
|
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