Results 31 to 40 of about 12,408 (251)
F1000Research, 2018 Deoxyoligonucleotide binding to bovine pancreatic ribonuclease A (RNase A) was investigated using electrospray ionization ion-trap mass spectrometry (ESI-IT-MS). Deoxyoligonucleotides included CCCCC (dC5) and CCACC (dC2AC2).
Daniel D. Clark
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Ligand-Induced Variations in Structural and Dynamical Properties Within an Enzyme Superfamily
Frontiers in Molecular Biosciences, 2018 Enzyme catalysis is a complex process involving several steps along the reaction coordinates, including substrate recognition and binding, chemical transformation, and product release.
Chitra Narayanan +7 more
doaj +1 more source
Construction of Highly Stable Cytotoxic Nuclear-Directed Ribonucleases
Molecules, 2018 Ribonucleases are proteins whose use is promising in anticancer therapy. We have previously constructed different human pancreatic ribonuclease variants that are selectively cytotoxic for tumor cells by introducing a nuclear localization signal into ...
David Roura Padrosa +5 more
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Elevated serum ribonuclease in patients with pancreatic cancer.
Proceedings of the National Academy of Sciences of the United States of America, 1976 Serum RNase (ribonuclease) of normal persons and of patients with pancreatitis, carcinoma of pancreas, or other neoplasms was determined with poly(C) as substrate. Strikingly abnormal elevations occur in the serum RNase of patients with pancreatic cancer.
K. Reddi, J. Holland
semanticscholar +1 more source
NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping. [PDF]
PLoS ONE, 2012 Three-dimensional domain swapping is a common phenomenon in pancreatic-like ribonucleases. In the aggregated state, these proteins acquire new biological functions, including selective cytotoxicity against tumour cells.
Roberta Spadaccini +9 more
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Endowing Human Pancreatic Ribonuclease with Toxicity for Cancer Cells*
Journal of Biological Chemistry, 2001 Onconase® is an amphibian protein that is now in Phase III clinical trials as a cancer chemotherapeutic. Human pancreatic ribonuclease (RNase 1) is homologous to Onconase® but is not cytotoxic. Here, ERDD RNase 1, which is the L86E/N88R/G89D/R91D variant
P. Leland +3 more
semanticscholar +1 more source
Localization of Disulfide Bonds in Ribonuclease Using Low pH Trypsin and LC-ESI-QTOF-MS
CHIMIAWe evaluated a method to localize disulfide bonds in bovine pancreatic ribonuclease (RNase) by applying low pH trypsin protein digestion with a bottom-up LC-ESI-QTOF-MS approach.
Amélie Bornex, Saša M. Miladinović
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Journal of Biological Chemistry, 1975 With the glutathione system that leads to rapid regeneration of reduced lysozyme (Saxena, V. P., and Wetlaufer, D. B. (1971) Biochemistry 9, 5015), reduced pancreatic ribonuclease (RNase) regenerated activity in high yield (greater than 90%) but at a ...
A. Karim +3 more
semanticscholar +1 more source
Molecular Oncology, EarlyView.Pancreatic sensory neurons innervating healthy and PDAC tissue were retrogradely labeled and profiled by single‐cell RNA sequencing. Tumor‐associated innervation showed a dominant neurofilament‐positive subtype, altered mitochondrial gene signatures, and reduced non‐peptidergic neurons.
Elena Genova +14 more
wiley +1 more source
Conserved amino acid networks modulate discrete functional properties in an enzyme superfamily
Scientific Reports, 2017 In this work, we applied the sequence-based statistical coupling analysis approach to characterize conserved amino acid networks important for biochemical function in the pancreatic-type ribonuclease (ptRNase) superfamily.
Chitra Narayanan +3 more
doaj +1 more source