[HTML][HTML] IPM-Biological and integrated management of desert locust

LI Shuang, SQ Feng, H Ullah, XB Tu… - Journal of Integrative …, 2022 - Elsevier
Locusts have caused periodic disasters in the recorded history of humankind. Up to now,
locust disaster is still the biggest threat to the world's agricultural production. The desert …

Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies

DC De Graaf, M Aerts, M Brunain… - Insect molecular …, 2010 - Wiley Online Library
With the Nasonia vitripennis genome sequences available, we attempted to determine the
proteins present in venom by two different approaches. First, we searched for the transcripts …

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 …

Structure and stability of β‐pleated sheets

A Perczel, Z Gáspári… - Journal of computational …, 2005 - Wiley Online Library
Beside α‐helices, β‐sheets are the most common secondary structure elements of proteins.
In this article, the question of structure and stability of parallel and antiparallel sheets of …

Enzyme: substrate hydrogen bond shortening during the acylation phase of serine protease catalysis

K Fodor, V Harmat, R Neutze, L Szilágyi, L Gráf… - Biochemistry, 2006 - ACS Publications
Atomic resolution (≤ 1.2 Å) serine protease intermediate structures revealed that the
strength of the hydrogen bonds between the enzyme and the substrate changed during …

Extended intermolecular interactions in a serine protease–canonical inhibitor complex account for strong and highly specific inhibition

K Fodor, V Harmat, C Hetényi, J Kardos, J Antal… - Journal of Molecular …, 2005 - Elsevier
We have previously shown that a trypsin inhibitor from desert locust Schistocerca gregaria
(SGTI) is a taxon-specific inhibitor that inhibits arthropod trypsins, such as crayfish trypsin …

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 …

Directed evolution of canonical loops and their swapping between unrelated serine proteinase inhibitors disprove the interscaffolding additivity model

E Boros, F Sebák, D Héja, D Szakács, K Zboray… - Journal of molecular …, 2019 - Elsevier
Reversible serine proteinase inhibitors comprise 18 unrelated families. Each family has a
distinct representative structure but contains a surface loop that adopts the same, canonical …

A review of the most important classes of serine protease inhibitors in insects and leeches

E Clynen, L Schoofs, M Salzet - Medicinal Chemistry Reviews …, 2005 - ingentaconnect.com
The constant increase of life expectancy is associated with major aging of developed
populations. This indicates that the new century will have one of most epidemic …