Results 131 to 140 of about 12,284 (148)

Safety evaluation of the food enzyme aspergillopepsin I from the non-genetically modified <i>Aspergillus</i> sp. strain AE-PRHF. [PDF]

EFSA J
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Van Loveren H, Vernis L, Kovalkovičová N, Cavanna D, Fernàndez-Fraguas C, Lunardi S, Peluso S, Liu Y.   +18 more
europepmc   +1 more source

Celastrol modulates IRS1 expression to alleviate ovarian aging and to enhance follicular development. [PDF]

Cell Biol Toxicol
Jiang Y, Shi Y, Lv M, Wang T, Wang P, Yuan X, Gao F, Ma B.   +7 more
europepmc   +1 more source

Small Molecule Protease Inhibitors as Model Peptidomimetics. [PDF]

Pharmaceuticals (Basel)
Gomez-Gutierrez P, Perez JJ.
europepmc   +1 more source

PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex. [PDF]

Sci Adv
Gordon J, Kaminski AM, Bommu SR, Skrajna A, Petrovich RM, Pedersen LC, McGinty RK, Warren AJ, Stanley RE.   +8 more
europepmc   +1 more source

The interaction between CfAda3 and CfGcn5 impacts growth, development and virulence of <i>Colletotrichum fructicola</i>. [PDF]

Virulence
Chen Y, Wang Y, Luo J, Li H, Zhang S.
europepmc   +1 more source

Haploid induction: an overview of parental factor manipulation during seed formation. [PDF]

Front Plant Sci
Song J, Datla R, Zou J, Xiang D.
europepmc   +1 more source

A novel milk-clotting enzyme from Aspergillus oryzae and A. luchuensis is an aspartic endopeptidase PepE presumed to be a vacuolar enzyme

A novel milk-clotting enzyme from Aspergillus oryzae and A. luchuensis is an aspartic endopeptidase PepE presumed to be a vacuolar enzyme
openaire  

Structural Analysis of a Novel Aspartic-Type Endopeptidase from Moringa oleifera Seeds and Its Milk-Clotting Properties

Journal of Agricultural and Food Chemistry, 2021
A novel aspartic-type endopeptidase was previously obtained from Moringa oleifera seeds; however, its specific milk-clotting properties have remained unclear. Here, we used various biophysical and molecular simulation approaches for characterizing the structure and function of the aspartic-type endopeptidase. The endopeptidase was preferentially active
Xuefeng Wang, Li He, Qiong Zhao, Yanan Shi, Yue Chen, Aixiang Huang   +5 more
openaire   +3 more sources

Substrate specificity of cerebral cathepsin D and high‐Mr aspartic endopeptidase

Journal of Neuroscience Research, 1988
AbstractThe specificity of action of bovine brain cortex cathepsin D (EC 3.4.23.5) and high‐Mr aspartic endopeptidase (EC 3.4.23.‐) was studied with the vasoactive peptides renin substrate tetradecapeptide (RSTP), substance P (SP), and angiotensins I and II, and with model peptides‐Lys‐Pro‐Ala‐Glu‐Phe‐Phe (NO2)‐Ala‐Leu (I), Gly‐Gly‐His‐Phe (NO2)‐Phe ...
A V, Azaryan, A A, Galoyan
openaire   +3 more sources

BYC, an atypical aspartic endopeptidase from Rhipicephalus (Boophilus) microplus eggs

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2008
An aspartic endopeptidase was purified in our laboratory from Rhipicephalus (Boophilus) microplus eggs [Logullo, C., Vaz, I.S., Sorgine, M.H., Paiva-Silva, G.O., Faria, F.S., Zingali, R.B., De Lima, M.F., Abreu, L., Oliveira, E.F., Alves, E.W., Masuda, H., Gonzales, J.C., Masuda, A., and Oliveira, P.L., 1998.
Maria Clara L, Nascimento-Silva, Alexandre T, Leal, Sirlei, Daffre, Luiz, Juliano, Itabajara, da Silva Vaz, Gabriela de O, Paiva-Silva, Pedro L, Oliveira, Marcos Henrique F, Sorgine   +7 more
openaire   +3 more sources