Results 171 to 180 of about 177,764 (316)

Expression of neutral endopeptidase (enkephalinase) in heterologous COS-1 cells. Characterization of the recombinant enzyme and evidence for a glutamic acid residue at the active site.

, 1988
Alain Devault, Christiane Nault, M Zollinger, M.-C. Fournié-Zaluski, B.P. Roques, Philippe Crine, Guy Boileau   +6 more
openalex   +1 more source

AEP promotes aberrant RNA splicing through DDX3X cleavage in solid tumors

The Journal of Clinical Investigation
Aberrant alternative splicing (AS) events have been identified in a variety of cancers. Although somatic mutations of splicing factors and dysregulation of RNA-binding proteins (RBPs) have been linked to AS and tumor malignancy, it remains unclear how ...
Yadong Xie, Haohao Zhang, Xinyang Song
doaj   +1 more source

Cyclical variation of serum neutral endopeptidase lost in asthmatics: A pilot study

, 2006
R. Matai, Michael D. Barker
openalex   +1 more source

Proteins of the kidney microvillar membrane. Reconstitution of endopeptidase in liposomes shows that it is a short-stalked protein [PDF]

, 1983
A J Kenny, I S Fulcher, K A McGill, D Kershaw   +3 more
openalex   +1 more source

Streptococcus pneumoniae Endopeptidase O Promotes the Clearance of Staphylococcus aureus and Streptococcus pneumoniae via SH2 Domain-Containing Inositol Phosphatase 1-Mediated Complement Receptor 3 Upregulation [PDF]

, 2020
Sijie Li, Hong Zhang, Jiangming Xiao, Taixian Yuan, Zhaoche Shu, Yajun Min, Wenchun Xu, Yibing Yin, Xuemei Zhang   +8 more
openalex   +1 more source

Affinity‐Based Protein Profiling Revealed that HIGD1A is a Direct Target Protein of Aristolochic Acids

Advanced Science, Volume 13, Issue 5, 27 January 2026.
Using an affinity‐based probe, this study reveals that aristolochic acid directly binds to HIGD1A with high affinity in the kidney. This binding disrupts the HIGD1A‐TFAM interaction, which in turn triggers TFAM degradation, cytosolic mitochondrial DNA release, and the activation of inflammatory pathways. Abstract Exposure to aristolochic acids (AA) via
Yin Gong, Shanshan Zhang, Anying Wei, Xiang Ji, Xiaodan Chong, Jinfeng Cen, Xuan Zhao, Zimeng Luo, Zhipeng Pei, Guanchao Mao, Xinkang Zhang, Mingxue Sun, Zhiguo Sun, Zifei Yin, Zhengrong Zou, Wen‐Qi Meng   +15 more
wiley   +1 more source

Safety evaluation of the food enzyme papain from the latex of <i>Carica papaya</i> L. [PDF]

EFSA J
Abstract The food enzyme papain (EC 3.4.22.2) is extracted from the latex of unripe Carica papaya L. by Nagase (Europe) GmbH. It is intended to be used in six food manufacturing processes. The dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 1.112 mg TOS/kg body weight per day. This exposure is up to one order of
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 M, Van Loveren H, Vernis L, Criado A, Fraguas Cristina CF, Cavanna D, Liu Y.   +16 more
europepmc   +2 more sources

Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins

, 2021
Hans C. van Leeuwen, Dick Roelofs, Jeroen Corver, Paul J. Hensbergen   +3 more
openalex   +1 more source

Nanoscopic Mapping of the Extracellular Space in Amyloid Plaque‐rich Cortex

Advanced Science, Volume 13, Issue 1, 5 January 2026.
The extracellular space and diffusion around amyloid plaques are examined using shadow imaging and single‐particle tracking. Increased diffusivity is found near plaques, extracellular matrix alterations, and plaque core penetrability that varies with amyloid phenotype.
Juan Estaún‐Panzano, Yulia Dembitskaya, Ivo Calaresu, Somen Nandi, Quentin Gresil, Evelyne Doudnikoff, Thierry Leste‐Lasserre, Thierry Amédée, Laurent Cognet, Laurent Groc, Urs Valentin Nägerl, Erwan Bezard   +11 more
wiley   +1 more source

Endopeptidase Inhibitors

Drugs in R & D, 1999
S G, Coleman, R, Duff
openaire   +2 more sources