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1.
Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.
J Biol Chem
; 298(6): 101985, 2022 06.
Artículo
en Inglés
| MEDLINE | ID: mdl-35483450
2.
Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum.
PLoS Pathog
; 15(12): e1008232, 2019 12.
Artículo
en Inglés
| MEDLINE | ID: mdl-31860690
3.
Novel MASP-2 inhibitors developed via directed evolution of human TFPI1 are potent lectin pathway inhibitors.
J Biol Chem
; 294(20): 8227-8237, 2019 05 17.
Artículo
en Inglés
| MEDLINE | ID: mdl-30952698
4.
Correction: Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.
J Biol Chem
; 299(1): 102807, 2023 Jan.
Artículo
en Inglés
| MEDLINE | ID: mdl-36563463
5.
MASP-1 and MASP-2 Do Not Activate Pro-Factor D in Resting Human Blood, whereas MASP-3 Is a Potential Activator: Kinetic Analysis Involving Specific MASP-1 and MASP-2 Inhibitors.
J Immunol
; 196(2): 857-65, 2016 Jan 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-26673137
6.
High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4' acidic residues.
J Biol Chem
; 286(25): 22535-45, 2011 Jun 24.
Artículo
en Inglés
| MEDLINE | ID: mdl-21515688
7.
Directed Evolution of Canonical Loops and Their Swapping between Unrelated Serine Proteinase Inhibitors Disprove the Interscaffolding Additivity Model.
J Mol Biol
; 431(3): 557-575, 2019 02 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-30543823
8.
MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked.
Sci Rep
; 6: 31877, 2016 08 18.
Artículo
en Inglés
| MEDLINE | ID: mdl-27535802
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