Results 31 to 40 of about 14,217 (304)
Folding kinetics of mammalian ribonucleases
, 1986 The folding kinetics of seven different pancreatic ribonucleases are compared both under native conditions and within the unfolding transition. In general, the folding kinetics of these proteins are similar despite numerous amino acid substitutions ...
Jaap J. Beintema +14 more
core +1 more source
Immune Modulation by Human Secreted RNases at the Extracellular Space
Frontiers in Immunology, 2018 The ribonuclease A superfamily is a vertebrate-specific family of proteins that encompasses eight functional members in humans. The proteins are secreted by diverse innate immune cells, from blood cells to epithelial cells and their levels in our body ...
Lu Lu +3 more
doaj +1 more source
Microbial Biotechnology, 2021 Summary The development of synthetic biology has brought an unprecedented increase in the number molecular tools applicable into a microbial chassis.
Patrícia Apura +3 more
doaj +1 more source
CRYSTALLINE RIBONUCLEASE [PDF]
Journal of General Physiology, 1940 1. A crystalline enzyme capable of digesting yeast nucleic acid has been isolated from fresh beef pancreas. 2. The enzyme called "ribonuclease" is a soluble protein of albumin type. Its molecular weight is about 15,000. Its isoelectric point is in the region of pH 8.0. 3.
openaire +2 more sources
Evasion of Ribonuclease Inhibitor as a Determinant of Ribonuclease Cytotoxicity [PDF]
Current Pharmaceutical Biotechnology, 2008 Onconase (ONC) is an amphibian member of the bovine pancreatic ribonuclease (RNase A) superfamily that exhibits innate antitumoral activity. ONC has been granted both orphan-drug and fast-track status by the U.S. Food and Drug Administration for the treatment of malignant mesothelioma, and is poised to become the first chemotherapeutic agent based on a
Thomas J, Rutkoski, Ronald T, Raines
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The Synthesis of Ribonuclease A
Journal of Biological Chemistry, 1971 A protected linear polypeptide of 124 amino acid residues with the sequence of bovine pancreatic ribonuclease A was synthesized by the solid phase method. The polypeptide was removed from the solid support and purified, and the four disulfide bonds were closed by air oxidation of the reduced form. The synthetic enzyme was fractionated by gel filtration
B, Gutte, R B, Merrifield
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Molecular Oncology, EarlyView.Dimethyl fumarate (DMF) reduces growth of HPV‐positive cervical cancer spheroids and induces ferroptosis in cervical cancer cells via blocking SLC7A11/Glutathione (GSH) axis. Combination of subcytotoxic doses of DMF and cisplatin (CDDP) further suppresses spheroid growth and drives cell death in 2D culture models.
Carolina Punziano +6 more
wiley +1 more source
Decay-Initiating Endoribonucleolytic Cleavage by RNase Y Is Kept under Tight Control via Sequence Preference and Sub-cellular Localisation. [PDF]
PLoS Genetics, 2015 Bacteria depend on efficient RNA turnover, both during homeostasis and when rapidly altering gene expression in response to changes. Nevertheless, remarkably few details are known about the rate-limiting steps in targeting and decay of RNA.
Vanessa Khemici +3 more
doaj +1 more source
Molecular evolution of pancreatic-type ribonucleases.
, 1986 Amino acid sequences of 39 mammalian ribonucleases have been used to construct trees by the maximum parsimony procedure. These trees are in fairly good agreement with the biological classification of the species involved.
Beintema, J. J. +8 more
core +1 more source
COMP–PMEPA1 axis promotes epithelial‐to‐mesenchymal transition in breast cancer cells
Molecular Oncology, EarlyView.This study reveals that cartilage oligomeric matrix protein (COMP) promotes epithelial‐to‐mesenchymal transition (EMT) in breast cancer. We identify PMEPA1 (protein TMEPAI) as a novel COMP‐binding partner that mediates EMT via binding to the TSP domains of COMP, establishing the COMP–PMEPA1 axis as a key EMT driver in breast cancer.
Konstantinos S. Papadakos +6 more
wiley +1 more source