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1. Full Text Molecular Recognition Features in Zika Virus Proteome
by Mishra, Pushpendra Mani and Uversky, Vladimir N and Giri, Rajanish
Journal of Molecular Biology, ISSN 0022-2836, 08/2018, Volume 430, Issue 16, pp. 2372 - 2388
Viruses have compact genomes that encode limited number of proteins in comparison to other biological entities. Interestingly, viral proteins have shown... 
Circular dichroism spectroscopy | Zika virus | intrinsically disordered protein regions | intrinsically disorder protein | molecular recognition features | NS2B-NS3 PROTEASE | INTRINSIC DISORDER | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | WEST-NILE-VIRUS | BINDING REGIONS | NS3 HELICASE | DENGUE-VIRUS | STRUCTURAL BASIS | KIX DOMAIN | MEMBRANE ASSOCIATION | Viral proteins | Health aspects | Analysis | Protein binding
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2. Full Text Analysis of Molecular Recognition Features (MoRFs)
by Mohan, Amrita and Oldfield, Christopher J and Radivojac, Predrag and Vacic, Vladimir and Cortese, Marc S and Dunker, A. Keith and Uversky, Vladimir N
Journal of Molecular Biology, ISSN 0022-2836, 2006, Volume 362, Issue 5, pp. 1043 - 1059
Several proteomic studies in the last decade revealed that many proteins are either completely disordered or possess long structurally flexible regions. Many... 
protein–protein interaction | PONDR | molecular recognition | signaling | intrinsic disorder | protein-protein interaction | RAMAN OPTICAL-ACTIVITY | ACTIVATION DOMAIN | POLYPROLINE-II STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTRINSICALLY UNSTRUCTURED PROTEINS | DISORDERED PROTEINS | GLOBULAR-PROTEINS | ALDRICH-SYNDROME PROTEIN | NATIVELY UNFOLDED PROTEINS | LONG-RANGE INTERACTIONS | SECONDARY STRUCTURE | Amino Acid Sequence | Protein Structure, Secondary | Computational Biology | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Chemistry, Physical - methods | Cryoelectron Microscopy | Algorithms | Proteins - metabolism | Computer Simulation | Databases, Protein | Protein Denaturation | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Protein Conformation | Spectrum Analysis, Raman | Protein Processing, Post-Translational | Software | Kinetics | Proteins - chemistry | Binding Sites | Amino Acids, Aromatic - chemistry | Proteins - ultrastructure | Proteins | Social aspects | Monomers | Protein binding
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3. Full Text Characterization of molecular recognition features, MoRFs, and their binding partners
by Vacic, Vladimir and Oldfield, Christopher J and Mohan, Amrita and Radivojac, Predrag and Cortese, Marc S and Uversky, Vladimir N and Dunker, A. Keith
Journal of Proteome Research, ISSN 1535-3893, 06/2007, Volume 6, Issue 6, pp. 2351 - 2366
Molecular Recognition Features ( MoRFs) are short, interaction-prone segments of protein disorder that undergo disorder-to-order transitions upon specific... 
Intrinsic disorder | Molecular recognition | Signaling | MoRF | Protein-protein interaction | signaling | CRYSTAL-STRUCTURE | BIOCHEMICAL RESEARCH METHODS | DISORDERED PROTEIN | DNA-REPLICATION | SIGNAL-TRANSDUCTION | PROTEIN-PROTEIN RECOGNITION | SEQUENCE | INTERFACES | molecular recognition | protein-protein interaction | SECONDARY STRUCTURE | INTERACTION SITES | STRUCTURAL GENOMICS | intrinsic disorder | Animals | Protein Structure, Secondary | Databases, Protein | Humans | Proteins - classification | Proteins - chemistry | Protein Interaction Mapping - standards | Protein Folding
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4. Full Text Molecular recognition features (MoRFs) in three domains of life
by Yan, Jing and Dunker, A. Keith and Uversky, Vladimir N and Kurgan, Lukasz
Molecular BioSystems, ISSN 1742-206X, 03/2016, Volume 12, Issue 3, pp. 697 - 710
Intrinsically disordered proteins and protein regions offer numerous advantages in the context of protein-protein interactions when compared to the structured... 
NATIVELY UNFOLDED PROTEINS | UNSTRUCTURED PROTEINS | INTRINSICALLY DISORDERED PROTEINS | FUNCTIONAL ANTHOLOGY | SEQUENCE-BASED PREDICTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTERACTION NETWORKS | SHORT LINEAR MOTIFS | SACCHAROMYCES-CEREVISIAE | POSTTRANSLATIONAL MODIFICATION | COMPUTATIONAL PREDICTION | Amino Acid Sequence | Archaea - metabolism | Bacteria - metabolism | Intrinsically Disordered Proteins - chemistry | Amino Acids - analysis | Molecular Sequence Data | Eukaryota - metabolism | Gene Ontology
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5. Full Text Mining α-helix-forming molecular recognition features with cross species sequence alignments
by Cheng, Yugong and Oldfield, Christopher J and Meng, Jingwei and Romero, Pedro and Uversky, Vladimir N and Dunker, A. Keith
Biochemistry, ISSN 0006-2960, 11/2007, Volume 46, Issue 47, pp. 13468 - 13477
Previously described algorithms for mining (x-helix-forming molecular recognition elements (MoREs), described by Oldfield et al. (Oldfield, C. J., Cheng, Y.,... 
NATIVELY UNFOLDED PROTEINS | AMINO-ACID-SEQUENCE | FUNCTIONAL ANTHOLOGY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | LONG DISORDERED REGIONS | STRUCTURAL ELEMENTS | INTRINSICALLY UNSTRUCTURED PROTEINS | INTERACTION NETWORKS | LINEAR MOTIFS | RNASE-E | Amino Acid Sequence | Sequence Alignment | Algorithms | Animals | Proteins - metabolism | Protein Structure, Secondary | Databases, Protein | Humans | Structure-Activity Relationship | Proteins - chemistry | Neural Networks (Computer) | PONDR | MoRF | protein interaction | cell signaling | protein | molecular recognition | Intrinsically disordered protein
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6. Full Text Diastereomeric Glycosyl Sulfoxides Display Different Recognition Features versus E. coli β‐Galactosidase
by Colomer, Juan P and Fernández de Toro, Beatriz and Cañada, F. Javier and Corzana, Francisco and Jiménez Barbero, Jesús and Canales, Ángeles and Varela, Oscar
European Journal of Organic Chemistry, ISSN 1434-193X, 10/2016, Volume 2016, Issue 30, pp. 5117 - 5122
The conformational analysis of the (S) and (R) diastereoisomers of benzyl 3‐deoxy‐4S‐(β‐d‐galactopyranosyl)‐4‐thio‐β‐d‐threo‐pentopyranoside S‐oxide (1S and... 
Conformation analysis | Molecular recognition | Glycomimetics | Glycosidases
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7. Full Text Diastereomeric Glycosyl Sulfoxides Display Different Recognition Features versus E-coli -Galactosidase
by Colomer, JP and de Toro, BF and Canada, FJ and Corzana, F and Barbero, JJ and Canales, A and Varela, O
EUROPEAN JOURNAL OF ORGANIC CHEMISTRY, ISSN 1434-193X, 10/2016, Volume 2016, Issue 30, pp. 5117 - 5122
The conformational analysis of the (S) and (R) diastereoisomers of benzyl 3-deoxy-4S-(-d-galactopyranosyl)-4-thio--d-threo-pentopyranoside S-oxide (1S and 1R,... 
Conformation analysis | ACID | THIO SUGARS | CHEMISTRY, ORGANIC | CONFORMATIONS | Glycomimetics | NMR | Glycosidases | Molecular recognition | BETA-GALACTOSIDASE | CHEMISTRY | INHIBITORS | BINDING | Nuclear magnetic resonance spectroscopy | Diastereomers | Analysis | Escherichia coli | Organosulfur compounds | Conformational analysis
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8. Full Text Analysis of Molecular Recognition Features (MoRFs) in membrane proteins
by Kotta-Loizou, Ioly and Tsaousis, Georgios N and Hamodrakas, Stavros J
BBA - Proteins and Proteomics, ISSN 1570-9639, 04/2013, Volume 1834, Issue 4, pp. 798 - 807
Molecular Recognition Features (MoRFs) are defined as short, intrinsically disordered regions in proteins that undergo disorder-to-order transition upon... 
Intrinsic disorder | Transmembrane proteins | Protein–protein interactions | MoRFs | Peripheral membrane proteins | Protein-protein interactions | UNSTRUCTURED PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | FLEXIBLE NETS | PREDICTION | INTRINSICALLY DISORDERED PROTEINS | FUNCTIONAL ANTHOLOGY | BIOPHYSICS | DATABASE | HUB PROTEINS | SECONDARY STRUCTURE | BINDING | WEB SERVER | Analysis | Membrane proteins | Protein binding
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9. Full Text Biogenesis of yeast Mia40 – uncoupling folding from import and atypical recognition features
by Chatzi, Afroditi and Sideris, Dionisia P and Katrakili, Nitsa and Pozidis, Charalampos and Tokatlidis, Kostas
The FEBS Journal, ISSN 1742-464X, 10/2013, Volume 280, Issue 20, pp. 4960 - 4969
The discovery of the mitochondrial intermembrane space assembly (MIA) pathway was followed by studies that focused mainly on the typical small substrates of... 
Erv1 | biogenesis | import | mitochondria | Mia40 | DISULFIDE RELAY SYSTEM | RECEPTOR MIA40 | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN IMPORT | BOND FORMATION | ELECTRON-TRANSFER | MEMBRANE ORGANIZATION | SUBSTRATE | MITOCHONDRIAL INTERMEMBRANE SPACE | CYTOCHROME-C PEROXIDASE | Catalytic Domain | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Oxidation-Reduction | Glutathione - metabolism | Protein Binding | Mitochondria - metabolism | Cytochrome Reductases - metabolism | Protein Folding | Mitochondrial Membrane Transport Proteins - biosynthesis | Protein Transport | Proteins | Glucose metabolism | Cysteine | Biosynthesis | Mitochondrial DNA | Imports | Galactose | Cystine | Mitochondria | Yeast | Kinetics
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10. Full Text Modular Architecture and Unique Teichoic Acid Recognition Features of Choline-Binding Protein L (CbpL) Contributing to Pneumococcal Pathogenesis
by Gutiérrez-Fernández, Javier and Saleh, Malek and Alcorlo, Martín and Gómez-Mejóa, Alejandro and Pantoja-Uceda, David and Treviño, Miguel A and Vob, Franziska and Abdullah, Mohammed R and Galán-Bartual, Sergio and Seinen, Jolien and Sánchez-Murcia, Pedro A and Gago, Federico and Bruix, Marta and Hammerschmidt, Sven and Hermoso, Juan A
Scientific Reports, ISSN 2045-2322, 12/2016, Volume 6, Issue 1, p. 38094
The human pathogen Streptococcus pneumoniae is decorated with a special class of surface-proteins known as choline-binding proteins (CBPs) attached to... 
SYSTEM | REGULATOR | LIPOPROTEIN | STREPTOCOCCUS-PNEUMONIAE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | SUPERINFECTION EXCLUSION | SURFACE | VIRULENCE | ADHESIN | PHOSPHORYLCHOLINE ESTERASE | Cell Wall - microbiology | Choline - metabolism | Pneumococcal Infections - metabolism | Calcium - metabolism | Crystallography, X-Ray - methods | Respiratory Tract Infections - microbiology | Streptococcus pneumoniae - pathogenicity | Streptococcus pneumoniae - metabolism | Binding Sites - physiology | Teichoic Acids - metabolism | Female | Pneumococcal Infections - microbiology | Nasopharynx - microbiology | Nasopharynx - metabolism | Respiratory Tract Infections - metabolism | Models, Molecular | Phagocytes - metabolism | Phosphorylcholine - metabolism | Immune Evasion - physiology | Animals | Carrier Proteins - metabolism | Phagocytes - microbiology | Cell Wall - metabolism | Virulence - physiology | Mice | Protein L | Nuclear magnetic resonance--NMR | Calcium | Pathogenesis | Cell walls | Virulence | Long-term potentiation | Nasopharynx | Phosphorylcholine | Crystallography | Teichoic acids | Streptococcus infections | X-ray crystallography | Proteins | Choline-binding protein | Phagocytes | Choline | Binding sites | Phagocytosis | Cell migration
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