Detalhe da pesquisa
1.
An evolutionary molecular adaptation of an unusual stefin from the liver fluke Fasciola hepatica redefines the cystatin superfamily.
J Biol Chem
; 299(3): 102970, 2023 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-36736427
2.
Protease-bound structure of Ricistatin provides insights into the mechanism of action of tick salivary cystatins in the vertebrate host.
Cell Mol Life Sci
; 80(11): 339, 2023 Oct 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-37898573
3.
An Unusual Two-Domain Thyropin from Tick Saliva: NMR Solution Structure and Highly Selective Inhibition of Cysteine Cathepsins Modulated by Glycosaminoglycans.
Int J Mol Sci
; 25(4)2024 Feb 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-38396918
4.
Highly potent inhibitors of cathepsin K with a differently positioned cyanohydrazide warhead: structural analysis of binding mode to mature and zymogen-like enzymes.
J Enzyme Inhib Med Chem
; 37(1): 515-526, 2022 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-35144520
5.
Mialostatin, a Novel Midgut Cystatin from Ixodes ricinus Ticks: Crystal Structure and Regulation of Host Blood Digestion.
Int J Mol Sci
; 22(10)2021 May 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-34065290
6.
The structure and function of Iristatin, a novel immunosuppressive tick salivary cystatin.
Cell Mol Life Sci
; 76(10): 2003-2013, 2019 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-30747251
7.
An Activity-Based Probe for Cathepsin K Imaging with Excellent Potency and Selectivity.
J Med Chem
; 64(18): 13793-13806, 2021 09 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-34473502