Results 61 to 70 of about 3,279,235 (401)

Crystal Structures of a Plant Trypsin Inhibitor from Enterolobium contortisiliquum (EcTI) and of Its Complex with Bovine Trypsin

PLoS ONE, 2013
A serine protease inhibitor from Enterolobium contortisiliquum (EcTI) belongs to the Kunitz family of plant inhibitors, common in plant seeds. It was shown that EcTI inhibits the invasion of gastric cancer cells through alterations in integrin-dependent ...
Dongwen Zhou, Y. A. Lobo, I. F. Batista, R. Marques-Porto, A. Gustchina, M. Oliva, A. Wlodawer   +6 more
semanticscholar   +1 more source

Genetic variability for cyanogen and trypsin inhibitor contents in sorghum (Sorghum bicolor (L.) Moench)

Electronic Journal of Plant Breeding, 2016
Sorghum is a staple food in the arid and semi-arid tropics, and is an important animal and bird feed in some developed countries. Very limited reports are available on anti-nutritional factors in sorghum. Grains of 200 sorghum genotypes including adapted
Hariprasanna K., V. Agte, M. Elangovan, S. Gite and, A. Kishore   +4 more
doaj   +1 more source

Effect of thermally untreated soybean with low levels of Kunitz trypsin inhibitors in the diet of broilers [PDF]

Agroznanje, 2011
This paper researched the effect of raw Kunitz free trypsin inhibitor soybean sort "Lana" to the production characteristics of broilers (Ross 308), compared to raw soybeans with a standard level of trypsin inhibitors. The production results indicate that
Beuković Dejan, Ljubojević D., Beuković Miloš, Đorđević Nenad, Milošević Niko, Stanaćev Vidica   +5 more
doaj  

Avaliação biológica de linhagem de soja com baixa atividade de inibidores de tripsina Biological evaluation of soybean line with low trypsin inhibitor activities

Revista Brasileira de Zootecnia, 2000
Cultivar de soja BR 36 com atividades de inibidores de tripsina convencional e linhagem de soja BRM 95-5262 geneticamente modificadas para conter baixas atividades de inibidores de tripsina foram utilizados em ensaios biológicos com aves contendo 40 e 20%
Edna Mayumi Yuahasi Miura, Marco Aurélio R. Binotti, Daliane Souza de Camargo, Ivone Yurika Mizubuti, Elza Iouko Ida   +4 more
doaj   +1 more source

Mitigation of antinutritional factors and protease inhibitors of defatted winged bean-seed proteins using thermal and hydrothermal treatments: Denaturation/unfolding coupled hydrolysis mechanism

Current Research in Food Science, 2022
The inactivation of antinutritional factors, protease inhibitors within winged bean protein was induced by two respective method treatments. The physical method based on steam vapor that was conducted using an autoclave and chemical method consisting on ...
Sami Saadi, Nazamid Saari, Hasanah Mohd Ghazali, Mohammed Sabo Abdulkarim   +3 more
doaj   +1 more source

Organization and sequence of the gene encoding the human acrosin-trypsin inhibitor (HUSI-II) [PDF]

, 1993
A complete cDNA encoding the acrosin-trypsin inhibitor, HUSI-II, was used as a probe to isolate genomic clones from a human placenta library. Three clones which cover the entire HUSI-II gene were isolated and characterized.
Abelson, Baumann, Beato, Bird, Dynan, Fink, Fink, Greene, Greene, Haendle, Hehlein-Fink, Horii, Kazal, Laskowski, Laskowski, LaThangue, Luerssen, Mead, Moritz, Policastro, Reynolds, Sambrook, Scott, Stein, Strähle, Stühmer, Tan, Tora, Weih   +28 more
core   +1 more source

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

FEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada   +8 more
wiley   +1 more source

Combinatorial optimization of cystine-knot peptides towards high-affinity inhibitors of human matriptase-1. [PDF]

PLoS ONE, 2013
Cystine-knot miniproteins define a class of bioactive molecules with several thousand natural members. Their eponymous motif comprises a rigid structured core formed by six disulfide-connected cysteine residues, which accounts for its exceptional ...
Bernhard Glotzbach, Michael Reinwarth, Niklas Weber, Sebastian Fabritz, Michael Tomaszowski, Heiko Fittler, Andreas Christmann, Olga Avrutina, Harald Kolmar   +8 more
doaj   +1 more source

Structure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1

BMC Structural Biology, 2011
BackgroundMatriptase is a type II transmembrane serine protease that is found on the surfaces of epithelial cells and certain cancer cells. Matriptase has been implicated in the degradation of certain extracellular matrix components as well as the ...
C. Yuan, Liqing Chen, E. Meehan, N. Daly, D. Craik, Mingdong Huang, J. Ngo   +6 more
semanticscholar   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

FEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang, Grace Du, Charity Yongo‐Luwawa, Angelina Lu, Brett Kinrade, Kim Munro, Karl E. Klose, William D. Lubell, Peter Davies, Shuaiqi Guo   +9 more
wiley   +1 more source