Results 11 to 20 of about 12,408 (251)

Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability.

open access: yesJournal of Inorganic Biochemistry, 2015
The reaction between cis-diamminedichloroplatinum(II) (CDDP), cisplatin, a common anticancer drug, and bovine pancreatic ribonuclease (RNase A), induces extensive protein aggregation, leading to the formation of one dimer, one trimer and higher oligomers
Fagagnini A   +13 more
core   +2 more sources

The amino acid sequence of human pancreatic ribonuclease

open access: yesAnalytical Biochemistry, 1984
The primary structure of human (Homo sapiens) pancreatic ribonuclease has been determined by automatic sequencing of the native protein and by analysis of peptides obtained by cleavage with proteolytic enzymes, cyanogen bromide, and hydroxylamine.
Weickmann, Joachim L.   +7 more
core   +2 more sources

Interaction of human pancreatic ribonuclease with human ribonuclease inhibitor [PDF]

open access: yesJournal of Biological Chemistry, 2001
Mammalian ribonucleases interact very strongly with the intracellular ribonuclease inhibitor (RI). Eukaryotic cells exposed to mammalian ribonucleases are protected from their cytotoxic action by the intracellular inhibition of ribonucleases by RI. Human
Batra, Janendra K.   +5 more
core   +2 more sources

Inclusion of Cetaceans within the order Artiodactyla based on phylogenetic analysis of pancreatic ribonuclease genes

open access: yesJournal of Molecular Evolution, 1999
Mammalian secretory ribonucleases (RNases 1) form a family of extensively studied homologous proteins that were already used for phylogenetic analyses at the protein sequence level previously. In this paper we report the determination of six ribonuclease
Beintema, JJ   +4 more
core   +3 more sources

Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis. [PDF]

open access: yesJ Pept Sci
Replacing lysine with arginine, the standard genetic approach to eliminate amine reactivity, alters physicochemical properties and leaves the N terminus unprotected. Here, reductive methylation is characterized as a conservative chemical alternative. Complete dimethylation of human ribonucleases preserves thermostability, protein–protein interaction ...
Molina OJ   +4 more
europepmc   +2 more sources

The effect of ribonuclease on phage-host interaction [PDF]

open access: yes, 1954
SUMMARY: Pancreatic ribonuclease inhibits the multiplication of a Rhizobium bacteriophage in liquid bacterial cultures by preventing permanent combination between phage and host.
Kleczkowski, A.
core   +1 more source

Angiogenin/ribonuclease 5 is an EGFR ligand and a serum biomarker for erlotinib sensitivity in pancreatic cancer

open access: yesCancer Cell, 2018
SUMMARY Pancreatic ribonuclease (RNase) is a secreted enzyme critical for host defense. We discover an intrinsic RNase function, serving as a ligand for epidermal growth factor receptor (EGFR), a member of receptor tyrosine kinase (RTK), in pancreatic ...
Ying-Nai Wang   +28 more
semanticscholar   +1 more source

Study Levels of Some Biochemical Parameters in Serum of Pancreatic Cancer Patients

open access: yesTikrit Journal of Pure Science, 2018
This study included an estimation for the levels of some biochemical parameters in the serum of those pancreatic cancer patients, by collecting (40) blood samples from patients their ages ranged (30-70) years compared with (55) blood samples of healthy ...
Layla A. Mustafa, Zena A. Mohammad
doaj   +1 more source

Rethinking Leucine Zipper : ribonuclease activity and structural dynamics of a ubiquitous oligomerization motif [PDF]

open access: yes, 2011
This dissertation focuses on structural, dynamic and catalytic properties of a Leucine Zipper (LZ) motif – a family of protein oligomerization domains which belong to the structural class of coiled coil proteins.
Nikolaev, Yaroslav
core   +1 more source

Evolutionary and Functional Novelty of Pancreatic Ribonuclease: a Study of Musteloidea (order Carnivora)

open access: yesScientific Reports, 2014
Pancreatic ribonuclease (RNASE1) is a digestive enzyme that has been one of the key models in studies of evolutionary innovation and functional diversification.
Jiang Liu   +7 more
semanticscholar   +1 more source

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