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1. QSAR & combinatorial science
and European Society of Combinatorial ScienceQSAR and Modelling Society
QSAR & combinatorial science, ISSN 1611-0218, 2003
QSAR (Biochemistry) | Structure-activity relationships (Biochemistry)
Journal
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2. Annual review of biophysics and biomolecular structure
Annual review of biophysics and biomolecular structure, ISSN 1056-8700, 1992
Molecular biology | Periodicals | Biophysics
Journal
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3. SAR and QSAR in environmental research
SAR and QSAR in environmental research, ISSN 1029-046X, 1993
Periodicals | QSAR (Biochemistry) | Structure-activity relationships (Biochemistry)
Journal
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4. Full Text Structure−Activity Relationships of Polymyxin Antibiotics
by Velkov, Tony and Thompson, Philip E and Nation, Roger L and Li, Jian
Journal of Medicinal Chemistry, ISSN 0022-2623, 03/2010, Volume 53, Issue 5, pp. 1898 - 1916
PERFORMANCE LIQUID-CHROMATOGRAPHY | 2-COMPONENT REGULATORY SYSTEM | OUTER-MEMBRANE | LIPOPOLYSACCHARIDE-BINDING ACTIVITY | COLISTIN NONAPEPTIDE DERIVATIVES | CHEMISTRY, MEDICINAL | GRAM-NEGATIVE BACTERIA | B NONAPEPTIDE | ANTIMICROBIAL PEPTIDE RESISTANCE | PERMEABILITY-INCREASING ACTION | SURFACE-PLASMON RESONANCE | Anti-Bacterial Agents - therapeutic use | Gram-Negative Bacteria - drug effects | Polymyxins - pharmacology | Polymyxins - therapeutic use | Anti-Bacterial Agents - chemistry | Humans | Gram-Negative Bacterial Infections - drug therapy | Anti-Bacterial Agents - pharmacology | Structure-Activity Relationship | Polymyxins - chemistry
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5. Full Text Structure–Neurotoxicity Relationships of Amyloid β-Protein Oligomers
by Kenjiro Ono and Margaret M. Condron and David B. Teplow and H. Eugene Stanley
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2009, Volume 106, Issue 35, pp. 14745 - 14750
Amyloid β-protein (Aβ) oligomers may be the proximate neurotoxins in Alzheimers disease (AD). "Oligomer" is an ill-defined term because many kinds have been... 
Oligomers | Nucleation | Fluorescence | Dimers | Trimers | Amyloids | Solar fibrils | Alzheimers disease | Dimerization | Monomers | Toxicity | Alzheimer's disease | toxicity | SCRAPIE | ASSEMBLIES | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | CROSS-LINKING | FIBRILLOGENESIS | SYNAPTIC PLASTICITY | SECRETED OLIGOMERS | PEPTIDE | AGGREGATION | Cell Survival - drug effects | Neurotoxins - chemistry | Protein Structure, Secondary | Amyloid beta-Peptides - toxicity | Protein Multimerization | Rats | Neurotoxins - toxicity | Structure-Activity Relationship | Microscopy, Electron | PC12 Cells | Animals | Amyloid beta-Peptides - ultrastructure | Amyloid beta-Peptides - metabolism | Microscopy, Atomic Force | Neurotoxins - metabolism | Hydro-Lyases - metabolism | Amyloid beta-Peptides - chemistry | Circular Dichroism | Index Medicus | Physical Sciences
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6. Full Text Li 7 Cd 4.5 Ge 4 Se 16 and Li 6.4 Cd 4.8 Sn 4 Se 16 : Strong Nonlinear Optical Response in Quaternary Diamond-Like Selenide Networks
by Guo, Yangwu and Li, Xiaoshuang and Feng, Kai and Li, Chao and Zhou, Molin and Wu, Yicheng and Yao, Jiyong
Chemistry - An Asian Journal, ISSN 1861-4728, 04/2018, Volume 13, Issue 7, pp. 871 - 876
nonlinear optics | selenides | structure–activity relationships | crystal growth | metal chalcogenides
Journal Article
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7. Full Text Structure-function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes
by Meng, Xiangfeng and Gangoiti, Joana and Bai, Yuxiang and Pijning, Tjaard and Van Leeuwen, Sander S and Dijkhuizen, Lubbert
Cellular and Molecular Life Sciences, ISSN 1420-9071, 2016, Volume 73, Issue 14, pp. 2681 - 2706
Lactic acid bacteria (LAB) are known to produce large amounts of α-glucan exopolysaccharides. Family GH70 glucansucrase (GS) enzymes catalyze the synthesis of... 
Life Sciences | Biochemistry, general | GH13 | Glucansucrase | Structure–function | Life Sciences, general | 4,6-α-Glucanotransferase | Evolution | GH70 | Biomedicine general | Cell Biology | MOLECULAR CHARACTERIZATION | ALPHA-AMYLASE FAMILY | 2 CATALYTIC DOMAINS | SEQUENCE-ANALYSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MESENTEROIDES NRRL B-1355 | SUCROSE ANALOGS | Structure-function | CELL BIOLOGY | LACTOBACILLUS-REUTERI 121 | STREPTOCOCCUS-MUTANS GLUCOSYLTRANSFERASES | LACTIC-ACID BACTERIA | LEUCONOSTOC-MESENTEROIDES | 4,6-alpha-Glucanotransferase | Glycosyltransferases - metabolism | Biocatalysis | Glycogen Debranching Enzyme System - metabolism | Glycogen Debranching Enzyme System - chemistry | Glycosyltransferases - chemistry | Bacteria - enzymology | Structure-Activity Relationship | Evolution, Molecular | Multi-Author Review
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8. Full Text QSRR:  Quantitative Structure-(Chromatographic) Retention Relationships
by Kaliszan, Roman
Chemical Reviews, ISSN 0009-2665, 07/2007, Volume 107, Issue 7, pp. 3212 - 3246
PERFORMANCE LIQUID-CHROMATOGRAPHY | WATER PARTITION-COEFFICIENTS | BIOPARTITIONING MICELLAR CHROMATOGRAPHY | CHIRAL STATIONARY-PHASE | HUMAN SERUM-ALBUMIN | SOLVATION ENERGY RELATIONSHIPS | MICROEMULSION ELECTROKINETIC CHROMATOGRAPHY | ARTIFICIAL-MEMBRANE CHROMATOGRAPHY | PARTIAL LEAST-SQUARES | MOLECULAR DESCRIPTOR SELECTION | CHEMISTRY, MULTIDISCIPLINARY | Multivariate Analysis | Animals | Chemistry, Pharmaceutical - methods | Solvents - chemistry | Chromatography - classification | Humans | Chromatography - methods | Pharmaceutical Preparations - chemistry | Pharmaceutical Preparations - analysis | Principal Component Analysis | Quantitative Structure-Activity Relationship | Hydrogen-Ion Concentration | Thermal properties | Thermodynamics | Analysis | Proteomics | Biomolecules | Research | Structure | High performance liquid chromatography
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9. Full Text Quantitative structure–(chromatographic) retention relationships
by Héberger, Károly
Journal of Chromatography A, ISSN 0021-9673, 2007, Volume 1158, Issue 1, pp. 273 - 305
Since the pioneering works of Kaliszan (R. Kaliszan, Quantitative Structure–Chromatographic Retention Relationships, Wiley, New York, 1987; and R. Kaliszan,... 
Gas chromatography | Column liquid chromatography | QSRR | QRAR | Affinity chromatography | Planar chromatography | Micellar liquid chromatography | Modeling | Chemometrics | QSERR | affinity chromatography | CHEMISTRY, ANALYTICAL | modeling | BIOPARTITIONING MICELLAR CHROMATOGRAPHY | SEMIEMPIRICAL TOPOLOGICAL INDEX | CHIRAL STATIONARY-PHASE | PRINCIPAL COMPONENT ANALYSIS | POLYCYCLIC AROMATIC-HYDROCARBONS | BIOCHEMICAL RESEARCH METHODS | ARTIFICIAL NEURAL-NETWORK | gas chromatography | column liquid chromatography | PERFORMANCE LIQUID-CHROMATOGRAPHY | chemometrics | GAS-CHROMATOGRAPHIC RETENTION | MULTIPLE LINEAR-REGRESSION | micellar liquid chromatography | planar chromatography | PARTIAL LEAST-SQUARES | Reproducibility of Results | Stereoisomerism | Quantitative Structure-Activity Relationship | Chromatography - methods | Analysis | Chromatography
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10. Quantitative structure-chromatographic retention relationships
by Kaliszan, Roman
1987, Chemical analysis, ISBN 9780471859833, Volume 93, xi, 303
Chromatographic analysis | Solution (Chemistry)
Book
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11. Full Text Structure–Activity Relationships and Quantitative Structure–Activity Relationships for Breast Cancer Resistance Protein (ABCG2)
by Gandhi, Yash A and Morris, Marilyn E
The AAPS Journal, ISSN 1550-7416, 9/2009, Volume 11, Issue 3, pp. 541 - 552
Breast cancer resistance protein (ABCG2), the newest ABC transporter, was discovered independently by three groups in the late 1990s. ABCG2 is widely... 
Biochemistry, general | Biotechnology | Biomedicine | breast cancer resistance protein | structure–activity relationships | Pharmacy | quantitative structure–activity relationships | Pharmacology/Toxicology | ABC transporter | ABCG2 | Quantitative structure-activity relationships | Structure-activity relationships | Breast cancer resistance protein | TRANSPORTER | MEDIATED DRUG-RESISTANCE | MODULATORS | FLAVONOIDS | CAMPTOTHECIN ANALOGS | STRUCTURE-PHARMACOKINETIC/PHARMACODYNAMIC RELATIONSHIPS | IN-VITRO | INHIBITION | structure-activity relationships | quantitative structure-activity relationships | PHARMACOLOGY & PHARMACY | CELL-CYCLE | MULTIDRUG-RESISTANCE | ATP Binding Cassette Transporter, Sub-Family G, Member 2 | ATP-Binding Cassette Transporters - chemistry | Drug Resistance, Multiple | Humans | Neoplasm Proteins - physiology | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - chemistry | Structure-Activity Relationship | ATP-Binding Cassette Transporters - physiology | Breast Neoplasms - physiopathology | ATP-Binding Cassette Transporters - antagonists & inhibitors | Drug resistance in microorganisms | Breast cancer | Xenobiotics | Analysis
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12. Full Text Understanding the composition–structure–bioactivity relationships in diopside (CaO·MgO·2SiO2)–tricalcium phosphate (3CaO·P2O5) glass system
by Kapoor, Saurabh and Semitela, Ângela and Goel, Ashutosh and Xiang, Ye and Du, Jincheng and Lourenço, Ana H and Sousa, Daniela M and Granja, Pedro L and Ferreira, José M.F
Acta Biomaterialia, ISSN 1742-7061, 03/2015, Volume 15, pp. 210 - 226
The present work is an amalgamation of computation and experimental approach to gain an insight into composition–structure–bioactivity relationships of... 
Tricalcium phosphate | Molecular dynamics simulation | Structure | Bioactive glasses | Diopside | MOLECULAR-DYNAMICS | MATERIALS SCIENCE, BIOMATERIALS | STRUCTURE-PROPERTY RELATIONSHIPS | ENGINEERING, BIOMEDICAL | COMPOSITION DEPENDENCE | LIME-PHOSPHOSILICATE GLASSES | STRONTIUM SUBSTITUTION | BETA-TRICALCIUM PHOSPHATE | MESENCHYMAL STEM-CELLS | IN-VITRO | SILICATE-GLASSES | MARROW STROMAL CELLS | Immunohistochemistry | Cell Survival - drug effects | Mesenchymal Stromal Cells - drug effects | Magnetic Resonance Spectroscopy | Humans | Alkaline Phosphatase - metabolism | Cells, Cultured | Silicic Acid - chemistry | Mesenchymal Stromal Cells - metabolism | Calcium Phosphates - chemistry | Structure-Activity Relationship | Glass - chemistry | Spectroscopy, Fourier Transform Infrared | Molecular Dynamics Simulation | Cell Shape - drug effects | Mesenchymal Stromal Cells - cytology | Mesenchymal Stromal Cells - ultrastructure | Cell Differentiation - drug effects | X-Ray Diffraction | Oxygen - chemistry | Calcium Phosphates - pharmacology | Silicic Acid - pharmacology | Lime | Calcium phosphate | Phosphates | TCP (protocol) | Glass | Amalgamation | Biocompatibility | Nuclear magnetic resonance | Dynamical systems | Calcium magnesium silicates
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13. Full Text Discovery, Synthesis, and Structure–Activity Relationships of Conotoxins
by Akondi, Kalyana B and Muttenthaler, Markus and Dutertre, Sébastien and Kaas, Quentin and Craik, David J and Lewis, Richard J and Alewood, Paul F
Chemical Reviews, ISSN 0009-2665, 06/2014, Volume 114, Issue 11, pp. 5815 - 5847
Peptide therapeutics are acclaimed as a promising addition to the pharmaceutical arena, and they continue to attract interest due to their high potency,... 
GAMMA-CARBOXYGLUTAMIC ACID | TOTAL CHEMICAL-SYNTHESIS | NUCLEAR-MAGNETIC-RESONANCE | X-RAY-STRUCTURE | NICOTINIC ACETYLCHOLINE-RECEPTOR | DISULFIDE BOND ISOMERS | PHASE PEPTIDE-SYNTHESIS | VITRO BIOLOGICAL-ACTIVITY | RESISTANT SODIUM-CHANNELS | CHEMISTRY, MULTIDISCIPLINARY | CYSTEINE-RICH PEPTIDES | Conotoxins - pharmacology | Amino Acid Sequence | Animals | Humans | Molecular Sequence Data | Terminology as Topic | Drug Discovery - methods | Structure-Activity Relationship | Conotoxins - chemical synthesis | Snails - chemistry | Conotoxins - chemistry | Organic chemistry | Chemical Sciences
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14. Full Text Structure-function relationships in calpains
by Campbell, Robert L and Davies, Peter L
Biochemical Journal, ISSN 0264-6021, 11/2012, Volume 447, Issue 3, pp. 335 - 351
Calpains are a family of complex multi-domain intracellular enzymes that share a calcium-dependent cysteine protease core. These are not degradative enzymes,... 
X-ray crystallography | Domain structure | Proteolysis | Calcium-binding | Proteinase | Inhibitor complex | Enzyme activation | enzyme activation | inhibitor complex | calcium-binding | CRYSTAL-STRUCTURE | EF-HAND | BIOCHEMISTRY & MOLECULAR BIOLOGY | domain structure | GIRDLE MUSCULAR-DYSTROPHY | ACTIVATED NEUTRAL PROTEASE | SKELETAL-MUSCLE | proteinase | MUSCLE-SPECIFIC CALPAIN | CA-2&-ACTIVATED PROTEASE | MU-CALPAIN | CA2+ REQUIREMENT | proteolysis | CALCIUM-DEPENDENT PROTEASE | Calcium-Binding Proteins - chemistry | Humans | Recombinant Proteins - chemistry | Terminology as Topic | Recombinant Proteins - genetics | Structure-Activity Relationship | Calpain - genetics | Calpain - chemistry | Protein Isoforms - physiology | Calpain - physiology | Animals | Protein Isoforms - chemistry | Calcium-Binding Proteins - physiology | Protein Conformation | Protein Subunits - chemistry | Enzyme Activation | Protein Subunits - physiology | Calcium Signaling | Calpain - antagonists & inhibitors | Protein Isoforms - genetics | Protein Subunits - genetics
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15. Full Text Structure–function relationships of human JmjC oxygenases—demethylases versus hydroxylases
by Markolovic, Suzana and Leissing, Thomas M and Chowdhury, Rasheduzzaman and Wilkins, Sarah E and Lu, Xin and Schofield, Christopher J
Current Opinion in Structural Biology, ISSN 0959-440X, 12/2016, Volume 41, pp. 62 - 72
The Jumonji-C (JmjC) subfamily of 2-oxoglutarate (2OG)-dependent oxygenases are of biomedical interest because of their roles in the regulation of gene... 
HYPOXIA-INDUCIBLE FACTOR | HISTONE DEMETHYLASE | SUBSTRATE-SPECIFICITY | INHIBITING-HIF FIH | 2-OXOGLUTARATE-DEPENDENT OXYGENASES | JUMONJI FAMILY | DOMAIN-CONTAINING PROTEIN | LYSYL-HYDROXYLATION | ASPARAGINYL HYDROXYLASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | Animals | Biocatalysis | Humans | Protein Multimerization | Jumonji Domain-Containing Histone Demethylases - chemistry | Mixed Function Oxygenases - metabolism | Structure-Activity Relationship | Jumonji Domain-Containing Histone Demethylases - metabolism | Oxidases | Oligomers | Catalysis | Hydroxylases
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