Results 1 to 10 of about 14,129 (184)

Ultra-high resolution X-ray structure of orthorhombic bovine pancreatic Ribonuclease A at 100K [PDF]

open access: yesBMC Chemistry, 2023
The crystal structure of orthorhombic Bovine Pancreatic Ribonuclease A has been determined to 0.85 Å resolution using low temperature, 100 K, synchrotron X-ray data collected at 16000 keV (λ = 0.77 Å). This is the first ultra-high-resolution structure of
David R. Lisgarten   +9 more
doaj   +2 more sources

Enhancement of the activity of the antimicrobial peptides HNP1 and LL-37 by bovine pancreatic ribonuclease A [version 3; peer review: 1 approved, 2 approved with reservations, 1 not approved] [PDF]

open access: yesF1000Research, 2023
Background: HNP1, LL-37, and HBD1 are antimicrobial against Escherichia coli ATCC 25922 at the standard inoculum but less active at higher inocula.   Methods: The virtual colony count (VCC) microbiological assay was adapted for high inocula and the ...
Bryan Ericksen
doaj   +2 more sources

Production of ovine Pancreatic Ribonuclease and investigation of enzyme characteristics [PDF]

open access: yesپژوهشهای علوم دامی ایران, 2021
Introduction Obviously, the recent decades strategy in cancer therapy, anticancer drug discovery and drug improvement is to characterize, distinguish and validate the most promising cancer-related molecular targets to which new drugs can be designed. The
mahsa Zabetian   +3 more
doaj   +1 more source

Ribonucleases as potential therapeutic agents [PDF]

open access: yesمجله بیوتکنولوژی کشاورزی, 2021
Objective Due to high cytotoxicity effect, ribonucleases (RNases) are known as pharmacological agents with therapeutic potential. The high potential of these enzymes in the destruction of RNA strand and their other substrates and subsequently, cell ...
Masoume Vakili-Azghandi   +3 more
doaj   +1 more source

Engineering and production of recombinant bovine pancreatic ribonuclease enzyme (RNase A) as a potential therapeutic [PDF]

open access: yesمجله بیوتکنولوژی کشاورزی, 2021
Objective  Immunotoxins are one of the most promising ways in therapeutic fields, specially cancer therapy which have a unique toxin-antibody structure, and kill the cancer cell by passing through the cell membrane and entering the target cell.
Masoume Vakili-Azghandi   +3 more
doaj   +1 more source

PEGylated gold nanoparticles-ribonuclease induced oxidative stress and apoptosis in colorectal cancer cells [PDF]

open access: yesBioImpacts, 2020
Introduction: Currently, drug-induced reactive oxygen species (ROS) mediating apoptosis pathway have extensively been investigated in designing effective strategies for colorectal cancer (CRC) chemotherapy.
Mostafa Akbarzadeh Khiavi   +7 more
doaj   +1 more source

Bovine Pancreatic RNase A: An Insight into the Mechanism of Antitumor Activity In Vitro and In Vivo

open access: yesPharmaceutics, 2022
In this investigation, we extensively studied the mechanism of antitumor activity of bovine pancreatic RNase A. Using confocal microscopy, we show that after RNase A penetration into HeLa and B16 cells, a part of the enzyme remains unbound with the ...
Islam Saber Ead Mohamed   +6 more
doaj   +1 more source

Revisiting the Formation of a Native Disulfide Bond: Consequences for Protein Regeneration and Beyond

open access: yesMolecules, 2020
Oxidative protein folding involves the formation of disulfide bonds and the regeneration of native structure (N) from the fully reduced and unfolded protein (R).
Mahesh Narayan
doaj   +1 more source

NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway [PDF]

open access: yes, 2014
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding).
A Jansens   +54 more
core   +3 more sources

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