Phagemid vectors for phage display: properties, characteristics and construction

H Qi, H Lu, HJ Qiu, V Petrenko, A Liu - Journal of molecular biology, 2012 - Elsevier
Phagemids are filamentous-phage-derived vectors containing the replication origin of a
plasmid. Phagemids usually encode no or only one kind of coat proteins. Other structural …

MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked

J Dobó, D Szakács, G Oroszlán, E Kortvely, B Kiss… - Scientific reports, 2016 - nature.com
MASP-3 was discovered 15 years ago as the third mannan-binding lectin (MBL)-associated
serine protease of the complement lectin pathway. Lacking any verified substrate its role …

Pacifastin-related peptides: structural and functional characteristics of a family of serine peptidase inhibitors

B Breugelmans, G Simonet, V van Hoef, S Van Soest… - Peptides, 2009 - Elsevier
Members of the pacifastin family are serine peptidase inhibitors, found in arthropods and
have many members within different insect orders. Based on their structural characteristics …

Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and-2 are essential for lectin pathway activation and reveal …

D Héja, V Harmat, K Fodor, M Wilmanns, J Dobó… - Journal of Biological …, 2012 - ASBMB
The lectin pathway is an antibody-independent activation route of the complement system. It
provides immediate defense against pathogens and altered self-cells, but it also causes …

Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 …

A Kocsis, KA Kékesi, R Szász, BM Végh… - The Journal of …, 2010 - journals.aai.org
The complement system, an essential part of the innate immune system, can be activated
through three distinct routes: the classical, the alternative, and the lectin pathways. The …

Directed evolution reveals the binding motif preference of the LC8/DYNLL hub protein and predicts large numbers of novel binders in the human proteome

P Rapali, L Radnai, D Süveges, V Harmat, F Tölgyesi… - PloS one, 2011 - journals.plos.org
LC8 dynein light chain (DYNLL) is a eukaryotic hub protein that is thought to function as a
dimerization engine. Its interacting partners are involved in a wide range of cellular …

Arg236 in human chymotrypsin B2 (CTRB2) is a key determinant of high enzyme activity, trypsinogen degradation capacity, and protection against pancreatitis

BZ Németh, A Demcsák, A Micsonai, B Kiss… - … et Biophysica Acta (BBA …, 2022 - Elsevier
Pancreatic chymotrypsins (CTRs) are digestive proteases that in humans include CTRB1,
CTRB2, CTRC, and CTRL. The highly similar CTRB1 and CTRB2 are the products of gene …

Phage display as a powerful tool to engineer protease inhibitors

ML Zani, T Moreau - Biochimie, 2010 - Elsevier
Since its introduction by Georges Smith some 25 years ago, phage display has proved to be
a powerful molecular technique for selecting proteins with desired biological properties from …

Substrate specificity of human chymotrypsin-like protease (CTRL) characterized by phage display-selected small-protein inhibitors

BZ Németh, ZA Nagy, B Kiss, G Gellén, G Schlosser… - Pancreatology, 2023 - Elsevier
Chymotrypsin-like protease (CTRL) is one of the four chymotrypsin isoforms expressed in
the human exocrine pancreas. Human genetic and experimental evidence indicate that …

High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4′ acidic residues

A Szabó, D Héja, D Szakács, K Zboray… - Journal of Biological …, 2011 - ASBMB
Human chymotrypsin C (CTRC) is a pancreatic protease that participates in the regulation of
intestinal digestive enzyme activity. Other chymotrypsins and elastases are inactive on the …