Results 181 to 190 of about 118,840 (299)

Cathepsin C inhibition reduces neutrophil serine protease activity and improves activated neutrophil-mediated disorders. [PDF]

Nat Commun
Nishibata Y, Arai S, Taniguchi M, Nakade I, Ogawa H, Kitano S, Hosoi Y, Shindo A, Nishiyama R, Masuda S, Nakazawa D, Tomaru U, Shimizu T, Sinko W, Nagakura T, Terada Y, Ishizu A.   +16 more
europepmc   +1 more source

Proteolysis of defensive proteins in peritonitis exudate [PDF]

, 1991
Assfalg-Machleidt, Irmgard, Billing, A., Fröhlich, D., Jochum, Marianne, Machleidt, W.   +4 more
core   +1 more source

Extracellular matrix and proteolysis: mechanisms driving irreversible changes and shaping cell behavior

The FEBS Journal, EarlyView.
Irreversible ECM proteolysis by remodeling enzymes shapes development, homeostasis, and disease. ECM‐degrading proteases display cell specificity and are governed by shared mechanisms, exhibiting functional redundancy in generating matrikines, growth factors, and cytokines.
Inna Solomonov, Orit Kollet, Irit Sagi
wiley   +1 more source

The preclinical and phase 1 development of the novel oral cathepsin C inhibitor BI 1291583. [PDF]

ERJ Open Res
Chalmers JD, Badorrek P, Diefenbach C, Kögler H, Sauter W, Kreideweiss S, Hohlfeld JM.   +6 more
europepmc   +1 more source

A Mutation in Cathepsin C Gene Causing Papillon-Lefèvre Syndrome in a Saudi Patient: A Case Report. [PDF]

Cureus, 2020
Shawli A, Almaghrabi Y, AlQuhaibi AS, Alghamdi Y, Aboud AM.   +4 more
europepmc   +1 more source

A guide to the types, structures, and multifaceted functions of matrix metalloproteinases in cancer

The FEBS Journal, EarlyView.
Matrix metalloproteinases (MMPs) orchestrate cancer progression and metastasis through proteolytic and non‐proteolytic actions. By remodeling the tumor microenvironment, enhancing growth factor availability, and modulating cell behavior, MMPs promote proliferation, migration or invasion, and epithelial‐to‐mesenchymal transition. Alongside extracellular
Zoi Piperigkou, Sylvia Mangani, Spyros Kremmydas, Nikolaos E. Koletsis, Nikos K. Karamanos   +4 more
wiley   +1 more source

Novel cathepsin C inhibitor, BI 1291583, intended for treatment of bronchiectasis: Phase I characterization in healthy volunteers. [PDF]

Clin Transl Sci
Badorrek P, Diefenbach C, Kögler H, Eleftheraki A, Seitz F, Hohlfeld JM.   +5 more
europepmc   +1 more source

Various roles of heme oxygenase-1 in response of bone marrow macrophages to RANKL and in the early stage of osteoclastogenesis [PDF]

, 2018
Bukowska-Straková, Karolina, Dulak, Józef, Florczyk-Soluch, Urszula, Józefczuk, Ewelina, Józkowicz, Alicja, Mendel, Mateusz, Nowak, Witold, Stępniewski, Jacek, Viscardi, Monika   +8 more
core   +1 more source

Interactions between small leucine‐rich proteoglycans and proteases: implications for tissue homeostasis and pathology

The FEBS Journal, EarlyView.
Small leucine‐rich proteoglycans (SLRPs) are key modulators of extracellular matrix structure and signaling. Their proteolytic processing by MMPs (Matrix Metalloproteinases), ADAMTS (disintegrin and metalloprotease with thrombospondin motifs), and serine proteases generates bioactive fragments that regulate collagen remodeling, inflammation, and ...
Maria Konstantaraki, Lydia‐Nefeli Thrapsanioti, Aikaterini Berdiaki, Ioanna Spyridaki, Dragana Nikitovic   +4 more
wiley   +1 more source

Degradomics for large‐scale mechanistic insights on proteases and proteolysis in human health

The FEBS Journal, EarlyView.
Proteolysis has an important role in human disease but remains relatively unexplored. Degradomics, the uncovering of proteolysis in tissues, cells, and proteins, uses mass spectrometry‐based terminomics to identify protein termini occurring therein (forward degradomics) and to define the actions of proteases (reverse degradomics).
Daniel R. Martin, Sumit Bhutada, Suneel S. Apte   +2 more
wiley   +1 more source