Results 91 to 100 of about 7,182,421 (220)
British Journal of Pharmacology, Volume 183, Issue 22, Page 6685-6703, November 2026.Abstract Background and Purpose Site‐specific antibody modification is a useful chemical strategy to elaborate antibody therapeutic function. Conventional lysine‐ or cysteine‐based conjugation methods generate heterogeneous products, while protein engineering approaches are resource‐intensive.
Karolina Krygier +2 more
wiley +1 more source
E4 engages uPAR and enolase-1 and activates urokinase to exert antifibrotic effects
JCI Insight, 2021 Fibroproliferative disorders such as systemic sclerosis (SSc) have no effective therapies and result in significant morbidity and mortality. We recently demonstrated that the C-terminal domain of endostatin, known as E4, prevented and reversed both ...
Shailza Sharma +9 more
doaj +1 more source
Chemistry – A European Journal, Volume 32, Issue 39, 22 October 2026.Hybrid macrocyclic peptides unite genetically encoded peptide libraries with the structural complexity of synthetic small molecules. This Review critically analyzes phage‐compatible cyclization and diversification chemistries, highlights emerging opportunities beyond traditional cysteine‐based approaches, and outlines how future advances may enable the
Titia Rixt Oppewal, Clemens Mayer
wiley +1 more source
Functional Stability of Plasminogen Activator Inhibitor-1
The Scientific World Journal, 2014 Plasminogen activator inhibitor-1 (PAI-1) is the main inhibitor of plasminogen activators, such as tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA), and a major regulator of the fibrinolytic system.
Songul Yasar Yildiz +3 more
doaj +1 more source
Frontiers in Oncology, 2018 The plasminogen activator (PA) system is an extracellular proteolytic enzyme system associated with various physiological and pathophysiological processes.
Niaz Mahmood +3 more
doaj +1 more source
Structure, function and antagonists of urokinase-type plasminogen activator
Frontiers in Bioscience, 2009 Urokinase (uPA) is a serine protease which converts plasminogen to plasmin, a broad-spectrum protease active on extracellular matrix (ECM) components. Like many components of the blood coagulation, fibrinolytic and complement cascades, uPA has a modular structure, including three conserved domains: a growth factor-like domain (GFD, residues 1 - 49), a ...
Carriero MV +9 more
openaire +3 more sources
, 2009 Video from Structure-based design of an urokinase-type plasminogen activator receptor–derived peptide inhibiting cell migration and lung ...
Mario De Rosa (15040481) +12 more
core +1 more source
Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator
Scientific Reports, 2017 Although trypsin-like serine proteases have flexible surface-exposed loops and are known to adopt higher and lower activity conformations, structural determinants for the different conformations have remained largely obscure.
Tobias Kromann-Hansen +9 more
doaj +1 more source
Urokinase-type plasminogen activator receptor
, 2003 A polypeptide presenting an epitope cross-reactive with an epitope of urokinase-type plasminogen activator receptor, and/or having uPA binding activity, is described.
Pollanen,, Jari +20 more
core
Food Technology and Biotechnology, 2002 Urokinase plasminogen activator (uPA) and its inhibitors (PAI) are elements of plasminogen activation system, a proteolytic system involved in many physiological and patological processes.
Branko Brdar, Maja Matulić
doaj