Chemical Reviews, ISSN 0009-2665, 05/1998, Volume 98, Issue 3, pp. 1045 - 1066
EOSINOPHIL-DERIVED NEUROTOXIN | AMINO-ACID-SEQUENCE | TRANSITION-STATE ANALOGS | SUBSTRATE-LEASH AMPLIFICATION | CIS PROLINE MUTANTS | LEUCINE-RICH REPEATS | DIFFUSION-DRIVEN MECHANISMS | BOVINE PANCREATIC RIBONUCLEASE | SITE-DIRECTED MUTAGENESIS | CHEMISTRY, MULTIDISCIPLINARY | X-RAY REFINEMENT | Usage | Ribonuclease | Research | Recombinant DNA | Nucleic acids
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2013, Volume 110, Issue 32, pp. 13002 - 13007
Enzymes function by stabilizing reaction transition states; therefore, comparison of the transition states of enzymatic and nonenzymatic model reactions can...
Protons | Enzymes | RNA | Active sites | Isotope effects | Chemical bases | Catalysis | Modeling | Electrostatics | Phosphoranes | MOLECULAR-DYNAMICS | MECHANISM | ALKALINE-PHOSPHATASE | MULTIDISCIPLINARY SCIENCES | ISOMERIZATION | HYDROLYSIS | REACTION-PATH | MODEL | CLEAVAGE | SOLVATION | PHOSPHORYL | Protein Structure, Tertiary | Phosphorylation | Biocatalysis | Models, Chemical | Models, Molecular | RNA - chemistry | Ribonuclease, Pancreatic - chemistry | Esterification | Molecular Dynamics Simulation | Oxygen Isotopes - chemistry | Ribonuclease, Pancreatic - metabolism | Oxygen Isotopes - metabolism | Molecular Structure | Kinetics | Nucleic Acid Conformation | RNA - metabolism | RNA sequencing | Research | Molecular genetics | Quantum theory | Biological Sciences
Protons | Enzymes | RNA | Active sites | Isotope effects | Chemical bases | Catalysis | Modeling | Electrostatics | Phosphoranes | MOLECULAR-DYNAMICS | MECHANISM | ALKALINE-PHOSPHATASE | MULTIDISCIPLINARY SCIENCES | ISOMERIZATION | HYDROLYSIS | REACTION-PATH | MODEL | CLEAVAGE | SOLVATION | PHOSPHORYL | Protein Structure, Tertiary | Phosphorylation | Biocatalysis | Models, Chemical | Models, Molecular | RNA - chemistry | Ribonuclease, Pancreatic - chemistry | Esterification | Molecular Dynamics Simulation | Oxygen Isotopes - chemistry | Ribonuclease, Pancreatic - metabolism | Oxygen Isotopes - metabolism | Molecular Structure | Kinetics | Nucleic Acid Conformation | RNA - metabolism | RNA sequencing | Research | Molecular genetics | Quantum theory | Biological Sciences
Journal Article
Protein Science, ISSN 0961-8368, 09/2019, Volume 28, Issue 9, pp. 1713 - 1719
The endogenous production of enzymes as zymogens provides a means to control catalytic activities. Here, we describe the heterologous production of...
protease | HIV | circular protein | cytotoxin | zymogen | intein | ribonuclease | HIV-1 | DESIGN | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN PANCREATIC RIBONUCLEASE | CLEAVAGE | SUBSTRATE | INHIBITOR | Ribonuclease A | Occlusion | Drugs | Prodrugs | Deactivation | Splicing | Proteinase | Cytotoxicity | Catalytic activity | Inactivation | Chemical compounds | Substrates | Thermal stability | Proenzymes | Molecular modelling | Protease | Human immunodeficiency virus--HIV | Catalysis
protease | HIV | circular protein | cytotoxin | zymogen | intein | ribonuclease | HIV-1 | DESIGN | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN PANCREATIC RIBONUCLEASE | CLEAVAGE | SUBSTRATE | INHIBITOR | Ribonuclease A | Occlusion | Drugs | Prodrugs | Deactivation | Splicing | Proteinase | Cytotoxicity | Catalytic activity | Inactivation | Chemical compounds | Substrates | Thermal stability | Proenzymes | Molecular modelling | Protease | Human immunodeficiency virus--HIV | Catalysis
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2001, Volume 276, Issue 27, pp. 24978 - 24984
Mammalian ribonucleases interact very strongly with the intracellular ribonuclease inhibitor (RI), Eukaryotic cells exposed to mammalian ribonucleases are...
EOSINOPHIL-DERIVED NEUROTOXIN | COMPLEX | AMINO-ACID-SEQUENCE | ANGIOGENIN | MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | CATIONIC PROTEIN | BOVINE SEMINAL RIBONUCLEASE | CATALYTIC PROPERTIES | Placental Hormones - metabolism | Protein Binding - genetics | Mutagenesis, Site-Directed | Enzyme Inhibitors - metabolism | Electrophoresis, Polyacrylamide Gel | Humans | Ribonuclease, Pancreatic - genetics | Blotting, Western | Animals | Ribonuclease, Pancreatic - metabolism | Cattle | Protein Conformation | Catalysis | Circular Dichroism | Amino Acid Substitution
EOSINOPHIL-DERIVED NEUROTOXIN | COMPLEX | AMINO-ACID-SEQUENCE | ANGIOGENIN | MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | CATIONIC PROTEIN | BOVINE SEMINAL RIBONUCLEASE | CATALYTIC PROPERTIES | Placental Hormones - metabolism | Protein Binding - genetics | Mutagenesis, Site-Directed | Enzyme Inhibitors - metabolism | Electrophoresis, Polyacrylamide Gel | Humans | Ribonuclease, Pancreatic - genetics | Blotting, Western | Animals | Ribonuclease, Pancreatic - metabolism | Cattle | Protein Conformation | Catalysis | Circular Dichroism | Amino Acid Substitution
Journal Article
Kidney International, ISSN 0085-2538, 05/2014, Volume 85, Issue 5, pp. 1179 - 1191
Recent studies stress the importance of antimicrobial peptides in protecting the urinary tract from infection. Previously, we have shown that ribonuclease 7...
pyelonephritis | ribonuclease 7 | antimicrobial peptide | intercalated cells | ribonuclease inhibitor | Ribonuclease inhibitor | Intercalated cells | Ribonuclease 7 | Pyelonephritis | Antimicrobial peptide | DEFENSE | OXIDATIVE STRESS | PROTEIN | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | PANCREATIC RIBONUCLEASE | ELASTASE | LEUCINE-RICH REPEATS | RNASE-A SUPERFAMILY | UROLOGY & NEPHROLOGY | INFECTION | Leukocyte Elastase - metabolism | Ribonucleases - urine | Ribonucleases - genetics | Carrier Proteins - urine | Humans | Kidney - enzymology | Middle Aged | Child, Preschool | Male | Cell Wall - enzymology | Pyelonephritis - microbiology | RNA, Messenger - metabolism | Case-Control Studies | Pyelonephritis - urine | Ribonucleases - metabolism | Ribonucleases - antagonists & inhibitors | Time Factors | Proteolysis | Escherichia coli - pathogenicity | Urothelium - enzymology | Adult | Female | Urinary Bladder - microbiology | Urothelium - microbiology | Urinary Bladder - enzymology | Child | Enterococcus faecalis - enzymology | Recombinant Proteins - metabolism | Pyelonephritis - enzymology | Enterococcus faecalis - pathogenicity | Escherichia coli - enzymology | Gene Expression Regulation, Enzymologic | Host-Pathogen Interactions | Carrier Proteins - genetics | Kidney - microbiology | Carrier Proteins - metabolism | Adolescent | Protein Binding | Aged | Pyelonephritis - genetics | Ribonuclease Inhibitor | Intercalated Cells | Antimicrobial Peptide | Innate Immunity | Urinary Tract Infection
pyelonephritis | ribonuclease 7 | antimicrobial peptide | intercalated cells | ribonuclease inhibitor | Ribonuclease inhibitor | Intercalated cells | Ribonuclease 7 | Pyelonephritis | Antimicrobial peptide | DEFENSE | OXIDATIVE STRESS | PROTEIN | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | PANCREATIC RIBONUCLEASE | ELASTASE | LEUCINE-RICH REPEATS | RNASE-A SUPERFAMILY | UROLOGY & NEPHROLOGY | INFECTION | Leukocyte Elastase - metabolism | Ribonucleases - urine | Ribonucleases - genetics | Carrier Proteins - urine | Humans | Kidney - enzymology | Middle Aged | Child, Preschool | Male | Cell Wall - enzymology | Pyelonephritis - microbiology | RNA, Messenger - metabolism | Case-Control Studies | Pyelonephritis - urine | Ribonucleases - metabolism | Ribonucleases - antagonists & inhibitors | Time Factors | Proteolysis | Escherichia coli - pathogenicity | Urothelium - enzymology | Adult | Female | Urinary Bladder - microbiology | Urothelium - microbiology | Urinary Bladder - enzymology | Child | Enterococcus faecalis - enzymology | Recombinant Proteins - metabolism | Pyelonephritis - enzymology | Enterococcus faecalis - pathogenicity | Escherichia coli - enzymology | Gene Expression Regulation, Enzymologic | Host-Pathogen Interactions | Carrier Proteins - genetics | Kidney - microbiology | Carrier Proteins - metabolism | Adolescent | Protein Binding | Aged | Pyelonephritis - genetics | Ribonuclease Inhibitor | Intercalated Cells | Antimicrobial Peptide | Innate Immunity | Urinary Tract Infection
Journal Article
Peptide Science, ISSN 0006-3525, 2008, Volume 90, Issue 3, pp. 259 - 277
Pancreatic ribonuclease A (EC 3.1.27.5, RNase) is, perhaps, the best‐studied enzyme of the 20th century. It was isolated by René Dubos, crystallized by Moses...
chimeric enzyme | S‐protein | S‐peptide | ribonuclease A | protein dynamics | Ribonuclease A | S-protein | Protein dynamics | Chimeric enzyme | S-peptide | RESIDUAL DIPOLAR COUPLINGS | ELECTRON-SPIN-RESONANCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN PEPTIDE INTERACTIONS | CIS AMIDE BOND | BOVINE PANCREATIC RIBONUCLEASE | DOMAIN-SWAPPED DIMER | ALPHA-AMINOISOBUTYRIC-ACID | COOH-TERMINAL TETRADECAPEPTIDE | BIOPHYSICS | RESTRICTED CONFORMATIONAL FREEDOM | HELIX-COIL TRANSITION | Amino Acid Sequence | Protein Structure, Secondary | History, 20th Century | Models, Molecular | Entropy | Ribonuclease, Pancreatic - chemistry | Ribonuclease, Pancreatic - history | Forecasting | Ribonuclease, Pancreatic - isolation & purification | Animals | Cattle | Computer Simulation | Protein Engineering | Protein Conformation
chimeric enzyme | S‐protein | S‐peptide | ribonuclease A | protein dynamics | Ribonuclease A | S-protein | Protein dynamics | Chimeric enzyme | S-peptide | RESIDUAL DIPOLAR COUPLINGS | ELECTRON-SPIN-RESONANCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN PEPTIDE INTERACTIONS | CIS AMIDE BOND | BOVINE PANCREATIC RIBONUCLEASE | DOMAIN-SWAPPED DIMER | ALPHA-AMINOISOBUTYRIC-ACID | COOH-TERMINAL TETRADECAPEPTIDE | BIOPHYSICS | RESTRICTED CONFORMATIONAL FREEDOM | HELIX-COIL TRANSITION | Amino Acid Sequence | Protein Structure, Secondary | History, 20th Century | Models, Molecular | Entropy | Ribonuclease, Pancreatic - chemistry | Ribonuclease, Pancreatic - history | Forecasting | Ribonuclease, Pancreatic - isolation & purification | Animals | Cattle | Computer Simulation | Protein Engineering | Protein Conformation
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 09/2014, Volume 289, Issue 38, pp. 25996 - 26006
Mounting evidence suggests that human pancreatic ribonuclease (RNase 1) plays important roles in vivo, ranging from regulating blood clotting and inflammation...
DOUBLE-STRANDED-RNA | PROTEIN | SEMINAL RIBONUCLEASE | HIGH-THROUGHPUT | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOTHELIAL-CELLS | EXTRACELLULAR RNA | HUMAN PANCREATIC RIBONUCLEASE | DIFFERENTIAL SCANNING FLUOROMETRY | ANTITUMOR-ACTIVITY | EXPRESSION | Ribonuclease, Pancreatic - physiology | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Cells, Cultured | Brain - enzymology | RNA Stability | Ribonuclease, Pancreatic - chemistry | Protein Transport | Liposomes - chemistry | Animals | Cattle | Protein Binding | Kinetics | RNA, Double-Stranded - chemistry | Hydrogen-Ion Concentration | Ribonuclease | RNA | Enzymology | Double-stranded RNA (dsRNA) | Heparin-binding Protein | Enzyme Catalysis
DOUBLE-STRANDED-RNA | PROTEIN | SEMINAL RIBONUCLEASE | HIGH-THROUGHPUT | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOTHELIAL-CELLS | EXTRACELLULAR RNA | HUMAN PANCREATIC RIBONUCLEASE | DIFFERENTIAL SCANNING FLUOROMETRY | ANTITUMOR-ACTIVITY | EXPRESSION | Ribonuclease, Pancreatic - physiology | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Cells, Cultured | Brain - enzymology | RNA Stability | Ribonuclease, Pancreatic - chemistry | Protein Transport | Liposomes - chemistry | Animals | Cattle | Protein Binding | Kinetics | RNA, Double-Stranded - chemistry | Hydrogen-Ion Concentration | Ribonuclease | RNA | Enzymology | Double-stranded RNA (dsRNA) | Heparin-binding Protein | Enzyme Catalysis
Journal Article
8.
Full Text
Inhibition of Human Pancreatic Ribonuclease by the Human Ribonuclease Inhibitor Protein
Journal of Molecular Biology, ISSN 0022-2836, 2007, Volume 368, Issue 2, pp. 434 - 449
The ribonuclease inhibitor protein (RI) binds to members of the bovine pancreatic ribonuclease (RNase A) superfamily with an affinity in the femtomolar range....
X-ray crystallography | protein–protein interaction | cytotoxin | cancer | tight-binding inhibitor | protein-protein interaction | ELECTROSTATIC INTERACTIONS | MAXIMUM-LIKELIHOOD | MEDIATED CYTOTOXICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 3-DIMENSIONAL STRUCTURE | ANGSTROM RESOLUTION | CYTOTOXIC RIBONUCLEASES | MOLECULAR RECOGNITION | CONFORMATIONAL STABILITY | BOVINE SEMINAL RIBONUCLEASE | CATALYTIC-ACTIVITY | Amino Acid Sequence | Placental Hormones - metabolism | Placental Hormones - chemistry | Protein Structure, Secondary | Humans | Enzyme Stability | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Mutant Proteins - metabolism | Ribonuclease, Pancreatic - chemistry | Static Electricity | Animals | Hydrogen Bonding | Ribonuclease, Pancreatic - metabolism | Cattle | Swine | Cell Death | K562 Cells | Protein Binding | Kinetics | Ribonuclease, Pancreatic - antagonists & inhibitors | Proteins
X-ray crystallography | protein–protein interaction | cytotoxin | cancer | tight-binding inhibitor | protein-protein interaction | ELECTROSTATIC INTERACTIONS | MAXIMUM-LIKELIHOOD | MEDIATED CYTOTOXICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 3-DIMENSIONAL STRUCTURE | ANGSTROM RESOLUTION | CYTOTOXIC RIBONUCLEASES | MOLECULAR RECOGNITION | CONFORMATIONAL STABILITY | BOVINE SEMINAL RIBONUCLEASE | CATALYTIC-ACTIVITY | Amino Acid Sequence | Placental Hormones - metabolism | Placental Hormones - chemistry | Protein Structure, Secondary | Humans | Enzyme Stability | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Mutant Proteins - metabolism | Ribonuclease, Pancreatic - chemistry | Static Electricity | Animals | Hydrogen Bonding | Ribonuclease, Pancreatic - metabolism | Cattle | Swine | Cell Death | K562 Cells | Protein Binding | Kinetics | Ribonuclease, Pancreatic - antagonists & inhibitors | Proteins
Journal Article
9.
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Protein–Surfactant Interaction: Sodium Dodecyl Sulfate-Induced Unfolding of Ribonuclease A
The Journal of Physical Chemistry B, ISSN 1520-6106, 12/2011, Volume 115, Issue 49, pp. 14760 - 14767
Protein–surfactant interaction is widely studied to understand stability and structural changes in proteins. In this Article, we have investigated SDS-induced...
B: Biophysical Chemistry | POLYACRYLAMIDE GEL-ELECTROPHORESIS | CONFORMATIONAL-CHANGES | MOLTEN GLOBULE | SDS | FLUORESCENCE | N-ALKYL SULFATES | COMPLEXES | GUANIDINE-HYDROCHLORIDE | CHEMISTRY, PHYSICAL | BETA-LACTOGLOBULIN | PROBE | Animals | Protein Structure, Secondary | Cattle | Protein Unfolding | Sodium Dodecyl Sulfate - chemistry | Hydrophobic and Hydrophilic Interactions | Spectrometry, Fluorescence | Surface-Active Agents - chemistry | Ribonuclease, Pancreatic - chemistry | Circular Dichroism | Micelles | Fluorescence | Hydrophobic effect | Research | Chemical properties | Ribonuclease | Binding proteins | Structure | Proteins | Absorbance | Sodium | Anisotropy | Agglomeration | Beads | Surfactants
B: Biophysical Chemistry | POLYACRYLAMIDE GEL-ELECTROPHORESIS | CONFORMATIONAL-CHANGES | MOLTEN GLOBULE | SDS | FLUORESCENCE | N-ALKYL SULFATES | COMPLEXES | GUANIDINE-HYDROCHLORIDE | CHEMISTRY, PHYSICAL | BETA-LACTOGLOBULIN | PROBE | Animals | Protein Structure, Secondary | Cattle | Protein Unfolding | Sodium Dodecyl Sulfate - chemistry | Hydrophobic and Hydrophilic Interactions | Spectrometry, Fluorescence | Surface-Active Agents - chemistry | Ribonuclease, Pancreatic - chemistry | Circular Dichroism | Micelles | Fluorescence | Hydrophobic effect | Research | Chemical properties | Ribonuclease | Binding proteins | Structure | Proteins | Absorbance | Sodium | Anisotropy | Agglomeration | Beads | Surfactants
Journal Article
Nano Letters, ISSN 1530-6984, 07/2007, Volume 7, Issue 7, pp. 1991 - 1995
This paper reports on the unfolding behavior of ribonuclease A (RNase A) on silica nanoparticle surfaces and quantitively demonstrates that nanoscale size and...
P61A MUTATION | PROTEIN ADSORPTION | PARTICLES | SOLID-SURFACES | STABILITY | MATERIALS SCIENCE, MULTIDISCIPLINARY | DENATURATION | NANOSCIENCE & NANOTECHNOLOGY | CHEMISTRY, MULTIDISCIPLINARY | Nanoparticles | Animals | Adsorption | Cattle | Silicon Dioxide | Enzyme Stability | Ribonuclease, Pancreatic - pharmacokinetics | Ribonuclease, Pancreatic - chemistry | Protein Folding
P61A MUTATION | PROTEIN ADSORPTION | PARTICLES | SOLID-SURFACES | STABILITY | MATERIALS SCIENCE, MULTIDISCIPLINARY | DENATURATION | NANOSCIENCE & NANOTECHNOLOGY | CHEMISTRY, MULTIDISCIPLINARY | Nanoparticles | Animals | Adsorption | Cattle | Silicon Dioxide | Enzyme Stability | Ribonuclease, Pancreatic - pharmacokinetics | Ribonuclease, Pancreatic - chemistry | Protein Folding
Journal Article
11.
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Ribonuclease A Inhibition by Carboxymethylsulfonyl‐Modified Xylo‐ and Arabinopyrimidines
ChemMedChem, ISSN 1860-7179, 09/2014, Volume 9, Issue 9, pp. 2138 - 2149
A group of acidic nucleosides were synthesized to develop a new class of ribonuclease A (RNase A) inhibitors. Our recent study on...
docking | inhibitors | modified nucleosides | RNase A | pyrimidines | carboxymethylsulfonyls | Carboxymethylsulfonyls | Docking | Pyrimidines | Inhibitors | Modified nucleosides | RNaseA | COMPLEX | DESIGN | CHEMISTRY, MEDICINAL | MECHANISM | CRYSTAL-STRUCTURE | BOVINE PANCREATIC RIBONUCLEASE | HUMAN ANGIOGENIN | CLEAVAGE | EOSINOPHIL-DERIVED NEUROTOXIN | PYRIMIDINE NUCLEOSIDES | BINDING SITES | PHARMACOLOGY & PHARMACY | RNase A | Catalytic Domain - drug effects | Cytidine - chemistry | Arabinonucleotides - pharmacology | Computational Biology | Enzyme Inhibitors - pharmacology | Models, Molecular | Kinetics | Enzyme Inhibitors - chemical synthesis | Ribonuclease, Pancreatic - antagonists & inhibitors | Arabinonucleotides - chemical synthesis | Uridine - chemistry
docking | inhibitors | modified nucleosides | RNase A | pyrimidines | carboxymethylsulfonyls | Carboxymethylsulfonyls | Docking | Pyrimidines | Inhibitors | Modified nucleosides | RNaseA | COMPLEX | DESIGN | CHEMISTRY, MEDICINAL | MECHANISM | CRYSTAL-STRUCTURE | BOVINE PANCREATIC RIBONUCLEASE | HUMAN ANGIOGENIN | CLEAVAGE | EOSINOPHIL-DERIVED NEUROTOXIN | PYRIMIDINE NUCLEOSIDES | BINDING SITES | PHARMACOLOGY & PHARMACY | RNase A | Catalytic Domain - drug effects | Cytidine - chemistry | Arabinonucleotides - pharmacology | Computational Biology | Enzyme Inhibitors - pharmacology | Models, Molecular | Kinetics | Enzyme Inhibitors - chemical synthesis | Ribonuclease, Pancreatic - antagonists & inhibitors | Arabinonucleotides - chemical synthesis | Uridine - chemistry
Journal Article
Current Pharmaceutical Biotechnology, ISSN 1389-2010, 06/2008, Volume 9, Issue 3, pp. 185 - 199
Onconase (R) (ONC) is an amphibian member of the bovine pancreatic ribonuclease ( RNase A) superfamily that exhibits innate antitumoral activity. ONC has been...
Ribonuclease A | Ribonuclease inhibitor | Cytotoxin | Pancreatic ribonuclease | Cancer | RANA-CATESBEIANA BULLFROG | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN PANCREATIC RIBONUCLEASE | cytotoxin | FIBROBLAST-GROWTH-FACTOR | pancreatic ribonuclease | ribonuclease inhibitor | EOSINOPHIL-DERIVED NEUROTOXIN | PROTEIN-PROTEIN RECOGNITION | INSERTIONAL FUSION PROTEIN | AMINO-ACID-SEQUENCE | LEUCINE-RICH REPEATS | PHARMACOLOGY & PHARMACY | cancer | BOVINE SEMINAL RIBONUCLEASE | TUMOR VASCULAR-PERMEABILITY | ribonuclease A | Amino Acid Sequence | Cytosol - classification | Ribonucleases - genetics | Mutagenesis, Site-Directed | Ribonucleases - chemistry | Humans | Cytosol - drug effects | Enzyme Stability | Models, Molecular | Molecular Sequence Data | Antineoplastic Agents - chemistry | Ribonucleases - antagonists & inhibitors | Cytosol - enzymology | Sequence Alignment | Animals | Antineoplastic Agents - isolation & purification | Protein Binding | Cytosol - metabolism | Antineoplastic Agents - pharmacology | Ribonucleases - pharmacology | Ribonucleases - isolation & purification
Ribonuclease A | Ribonuclease inhibitor | Cytotoxin | Pancreatic ribonuclease | Cancer | RANA-CATESBEIANA BULLFROG | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN PANCREATIC RIBONUCLEASE | cytotoxin | FIBROBLAST-GROWTH-FACTOR | pancreatic ribonuclease | ribonuclease inhibitor | EOSINOPHIL-DERIVED NEUROTOXIN | PROTEIN-PROTEIN RECOGNITION | INSERTIONAL FUSION PROTEIN | AMINO-ACID-SEQUENCE | LEUCINE-RICH REPEATS | PHARMACOLOGY & PHARMACY | cancer | BOVINE SEMINAL RIBONUCLEASE | TUMOR VASCULAR-PERMEABILITY | ribonuclease A | Amino Acid Sequence | Cytosol - classification | Ribonucleases - genetics | Mutagenesis, Site-Directed | Ribonucleases - chemistry | Humans | Cytosol - drug effects | Enzyme Stability | Models, Molecular | Molecular Sequence Data | Antineoplastic Agents - chemistry | Ribonucleases - antagonists & inhibitors | Cytosol - enzymology | Sequence Alignment | Animals | Antineoplastic Agents - isolation & purification | Protein Binding | Cytosol - metabolism | Antineoplastic Agents - pharmacology | Ribonucleases - pharmacology | Ribonucleases - isolation & purification
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 11/2007, Volume 46, Issue 46, pp. 8887 - 8889
The rating game: The effect of cations and anions of ionic liquids (ILs) on the stability of ribonuclease A in aqueous solutions was studied by differential...
ionic liquids | differential scanning calorimetry | Hofmeister series | proteins | ribonuclease A | Proteins | Ribonuclease A | Ionic liquids | Differential scanning calorimetry | STABILITY | LIPASE-B | CYTOTOXICITY | CHEMISTRY, MULTIDISCIPLINARY | ribonuclease A | Ionic Liquids | Ribonuclease, Pancreatic - chemistry | Protein Denaturation | Water - chemistry
ionic liquids | differential scanning calorimetry | Hofmeister series | proteins | ribonuclease A | Proteins | Ribonuclease A | Ionic liquids | Differential scanning calorimetry | STABILITY | LIPASE-B | CYTOTOXICITY | CHEMISTRY, MULTIDISCIPLINARY | ribonuclease A | Ionic Liquids | Ribonuclease, Pancreatic - chemistry | Protein Denaturation | Water - chemistry
Journal Article