Proteases and Delayed Wound Healing.
Advances in wound care, 2013 SIGNIFICANCE Proteases and their inhibitors contribute to the balance between extracellular matrix (ECM) degradation and deposition, creating an equilibrium that is essential for the timely and coordinated healing of cutaneous wounds.
Sara M. McCarty, S. Percival
semanticscholar +1 more source
T-SP1: a novel serine protease-like protein predominantly expressed in testis [PDF]
, 2008 Here, we describe a novel member in the group of membrane-anchored chymotrypsin (S1)-like serine proteases, namely testis serine protease 1 (T-SP1), as it is principally expressed in testis tissue.
Geissler, Claudia +6 more
core +1 more source
Molecular Oncology, EarlyView.NAD+ regeneration by mitochondrial complex I NADH dehydrogenase is important for cancer cell proliferation. Specifically, NAD+ is necessary for the activities of NAD+‐dependent deacetylases SIRT3 and SIRT7, which suppress the expression of p21Cip1 cyclin‐dependent kinase inhibitor, an antiproliferative molecule, at the translational and transcriptional
Masato Higurashi +5 more
wiley +1 more source
A folding inhibitor of the HIV-1 Protease [PDF]
arXiv, 2005 Being the HIV-1 Protease (HIV-1-PR) an essential enzyme in the viral life cycle, its inhibition can control AIDS. The folding of single domain proteins, like each of the monomers forming the HIV-1-PR homodimer, is controlled by local elementary structures (LES, folding units stabilized by strongly interacting, highly conserved, as a rule hydrophobic ...
arxiv
The in vivo transcriptome of Schistosoma mansoni in the prominent vector species Biomphalaria pfeifferi with supporting observations from Biomphalaria glabrata. [PDF]
, 2019 BackgroundThe full scope of the genes expressed by schistosomes during intramolluscan development has yet to be characterized. Understanding the gene products deployed by larval schistosomes in their snail hosts will provide insights into their ...
Bu, Lijing +6 more
core +2 more sources
Stochastic variation in the FOXM1 transcription program mediates replication stress tolerance
Molecular Oncology, EarlyView.Cellular heterogeneity is a major cause of drug resistance in cancer. Segeren et al. used single‐cell transcriptomics to investigate gene expression events that correlate with sensitivity to the DNA‐damaging drugs gemcitabine and prexasertib. They show that dampened expression of transcription factor FOXM1 and its target genes protected cells against ...
Hendrika A. Segeren +4 more
wiley +1 more source
High-Throughput Virtual Screening of 4487 flavonoids: New insights on the structural inhibition of SARS-CoV-2 Main Protease [PDF]
arXiv, 2020 COVID-19 presents a great threat to public health worldwide and the infectious agent SARS-CoV-2 is currently the target of much research aiming at inhibition. The virus' main protease is a dimeric enzyme that has only recently begun to be thoroughly described, opening the door for virtual screening more broadly. Here, a PAIN-filtered flavonoid database
arxiv
SUMO-specific proteases/isopeptidases: SENPs and beyond
Genome Biology, 2014 We summarize the evolutionary relationship, structure and subcellular distribution of SUMO proteases (or SUMO isopeptidases). We also discuss their functions and allude to their involvement in human disease.
A. Nayak, S. Müller
semanticscholar +1 more source
Influence of commercial proteases on the proteolysis of enzyme modified cheese : a thesis presented in partial fulfilment of the requirements for the degree of Master of Technology in Food Technology at Massey University, Palmerston North, New Zealand [PDF]
, 2000 The influence of four commercial proteases, Protease A, Protease B, Protease C and a two enzyme blend Protease DE, on proteolysis in an enzyme modified cheese (EMC) base has been investigated.
Chen, Emily Yi Chuan
core
In vivo imaging of protease activity by Probody therapeutic activation. [PDF]
, 2016 Probody™ therapeutics are recombinant, proteolytically-activated antibody prodrugs, engineered to remain inert until activated locally by tumor-associated proteases.
Craik, Charles S +4 more
core +1 more source