Detalhe da pesquisa
1.
Plant ecological genomics at the limits of life in the Atacama Desert.
Proc Natl Acad Sci U S A
; 118(46)2021 11 16.
Artigo
Inglês
| MEDLINE | ID: mdl-34725254
2.
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.
Artigo
Inglês
| MEDLINE | ID: mdl-35483450
3.
Substrate specificity of human chymotrypsin-like protease (CTRL) characterized by phage display-selected small-protein inhibitors.
Pancreatology
; 23(6): 742-749, 2023 Sep.
Artigo
Inglês
| MEDLINE | ID: mdl-37604733
4.
Proprotein Convertase Is the Highest-Level Activator of the Alternative Complement Pathway in the Blood.
J Immunol
; 206(9): 2198-2205, 2021 05 01.
Artigo
Inglês
| MEDLINE | ID: mdl-33858964
5.
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.
Artigo
Inglês
| MEDLINE | ID: mdl-31860690
6.
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.
Artigo
Inglês
| MEDLINE | ID: mdl-30952698
7.
Cutting Edge: A New Player in the Alternative Complement Pathway, MASP-1 Is Essential for LPS-Induced, but Not for Zymosan-Induced, Alternative Pathway Activation.
J Immunol
; 200(7): 2247-2252, 2018 04 01.
Artigo
Inglês
| MEDLINE | ID: mdl-29475986
8.
The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond.
Immunol Rev
; 274(1): 98-111, 2016 11.
Artigo
Inglês
| MEDLINE | ID: mdl-27782318
9.
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.
Artigo
Inglês
| MEDLINE | ID: mdl-36563463
10.
Overlapping Specificity of Duplicated Human Pancreatic Elastase 3 Isoforms and Archetypal Porcine Elastase 1 Provides Clues to Evolution of Digestive Enzymes.
J Biol Chem
; 292(7): 2690-2702, 2017 02 17.
Artigo
Inglês
| MEDLINE | ID: mdl-28062577
11.
Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway.
PLoS Comput Biol
; 13(12): e1005885, 2017 12.
Artigo
Inglês
| MEDLINE | ID: mdl-29240760
12.
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.
Artigo
Inglês
| MEDLINE | ID: mdl-26673137
13.
Cholesterol Crystals Activate the Lectin Complement Pathway via Ficolin-2 and Mannose-Binding Lectin: Implications for the Progression of Atherosclerosis.
J Immunol
; 196(12): 5064-74, 2016 06 15.
Artigo
Inglês
| MEDLINE | ID: mdl-27183610
14.
Comment on "Cutting Edge: Role of MASP-3 in the Physiological Activation of Factor D of the Alternative Complement Pathway".
J Immunol
; 203(12): 3091, 2019 12 15.
Artigo
Inglês
| MEDLINE | ID: mdl-31818918
15.
Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2.
Proc Natl Acad Sci U S A
; 109(26): 10498-503, 2012 Jun 26.
Artigo
Inglês
| MEDLINE | ID: mdl-22691502
16.
Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway.
J Biol Chem
; 288(13): 8922-34, 2013 Mar 29.
Artigo
Inglês
| MEDLINE | ID: mdl-23386610
17.
Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2.
J Biol Chem
; 287(24): 20290-300, 2012 Jun 08.
Artigo
Inglês
| MEDLINE | ID: mdl-22511776
18.
Inhibition of the serine proteases of the complement system.
Adv Exp Med Biol
; 735: 23-40, 2013.
Artigo
Inglês
| MEDLINE | ID: mdl-23402017
19.
Complement inhibition can decrease the haemostatic response in a microvascular bleeding model at multiple levels.
Front Immunol
; 14: 1226832, 2023.
Artigo
Inglês
| MEDLINE | ID: mdl-37771595
20.
The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action.
J Biol Chem
; 286(5): 3587-96, 2011 Feb 04.
Artigo
Inglês
| MEDLINE | ID: mdl-21097875