Results 21 to 30 of about 14,129 (184)

The first crystal structure of human RNase6 reveals a novel substrate binding and cleavage site arrangement [PDF]

open access: yes, 2016
Human RNase 6 is a cationic secreted protein that belongs to the RNase A superfamily. Its expression is induced in neutrophils and monocytes upon bacterial infection, suggesting a role in host defence.
Arranz Trullén, Javier   +6 more
core   +2 more sources

THE IMPORTANCE OF DYNAMIC EFFECTS ON THE ENZYME ACTIVITY: X-RAY STRUCTURE AND MOLECULAR DYNAMICS OF ONCONASE MUTANTS. [PDF]

open access: yes, 2005
Onconase (ONC), a member of the RNase A superfamily extracted from oocytes of Rana pipiens, is an effective cancer killer. It is currently used in treatment of various forms of cancer.
A. CARANNANTE   +6 more
core   +1 more source

Localization of Disulfide Bonds in Ribonuclease Using Low pH Trypsin and LC-ESI-QTOF-MS

open access: yesCHIMIA
We 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
doaj   +1 more source

Protein disulphide isomerase-assisted functionalization of proteinaceous substrates [PDF]

open access: yes, 2012
Protein disulphide isomerase (PDI) is an enzyme that catalyzes thiol-disulphide exchange reactions among a broad spectrum of substrates, including proteins and low-molecular thiols and disulphides.
Anfinsen CB   +143 more
core   +1 more source

Mitochondrial Translation Products before and after Integration into the Mitochondrial Membrane in Neurospora crassa [PDF]

open access: yes, 1972
# 1. Nascent translation products on mitochondrial ribosomes were selectively labeled in vivo in the presence of cycloheximide with radioactive leucine. They were isolated together with the ribosomes. # 2.
Michel, Rainer, Neupert, Walter
core   +1 more source

TRAIL‐PEG‐Apt‐PLGA nanosystem as an aptamer‐targeted drug delivery system potential for triple‐negative breast cancer therapy using in vivo mouse model

open access: yesMolecular Oncology, EarlyView.
Aptamers are used both therapeutically and as targeting agents in cancer treatment. We developed an aptamer‐targeted PLGA–TRAIL nanosystem that exhibited superior therapeutic efficacy in NOD/SCID breast cancer models. This nanosystem represents a novel biotechnological drug candidate for suppressing resistance development in breast cancer.
Gulen Melike Demirbolat   +8 more
wiley   +1 more source

Elucidation of the disulfide folding pathway of hirudin by a topology-based approach [PDF]

open access: yes, 2003
A theoretical model for the folding of proteins containing disulfide bonds is introduced. The model exploits the knowledge of the native state to favour the progressive establishment of native interactions.
De Filippis, V.   +3 more
core   +2 more sources

RNA‐Micelles as Self‐Assembling Structures for Efficient Co‐Delivery of Synergistic siRNA and Nucleoside Analogues to Treat CRC Lung Metastasis

open access: yesAdvanced Functional Materials, EarlyView.
Two kinds of self‐assembled RNA micelles were used to co‐deliver synergistic siRNA and nucleoside analogues for the treatment of colorectal cancer lung metastases. Near‐complete elimination of lung cancer metastases was confirmed in an orthotopic lung metastasis model constructed using human colorectal cancer lung metastases patient surgical samples to
Kai Jin   +4 more
wiley   +1 more source

Ethanol Induced Disordering of Pancreatic Acinar Cell Endoplasmic Reticulum: An ER Stress/Defective Unfolded Protein Response Model. [PDF]

open access: yes, 2018
Background & aimsHeavy alcohol drinking is associated with pancreatitis, whereas moderate intake lowers the risk. Mice fed ethanol long term show no pancreas damage unless adaptive/protective responses mediating proteostasis are disrupted. Pancreatic
Abrol, Ravinder   +13 more
core   +3 more sources

Affinity Chromatography of Bovine Pancratic Ribonuclease A [PDF]

open access: yesEuropean Journal of Biochemistry, 1969
5′‐(4‐Aminophenyl‐phosphoryl)‐uridine‐2′(3′)‐phosphate was synthesized and coupled to Sepharose by activation with cyanogen bromide. This conjugate was used as a specific adsorbent for purification of ribonuclease A by affinity chromatography. Totally reduced and oxidized RNase preparations which are enzymatically inactive were not adsorbed or retarded
M, Wilchek, M, Gorecki
openaire   +2 more sources

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