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Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 07/2017, Volume 85, Issue 7, pp. 1336 - 1350
ABSTRACT The molecular details of the association between the human Fyn‐SH3 domain, and the fragment of 18.5‐kDa myelin basic protein (MBP) spanning residues... 
molecular recognition fragment (MoRF) | poly‐proline type II (PPII) | Fyn‐SH3 | amphipathic α‐helix | myelin basic protein (MBP) | intrinsically disordered protein (IDP) | molecular dynamics (MD) simulations | GROMACS | amphipathic α-helix | poly-proline type II (PPII) | Fyn-SH3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | IMMUNODOMINANT EPITOPE | POSTTRANSLATIONAL MODIFICATIONS | amphipathic -helix | AZE AZETIDINE-2-CARBOXYLIC ACID | INTRINSICALLY DISORDERED PROTEINS | FYN TYROSINE KINASE | BIOPHYSICS | MULTIPLE-SCLEROSIS | CRK N-SH3 DOMAIN | STATE NMR-SPECTROSCOPY | CENTRAL-NERVOUS-SYSTEM | MESSENGER-RNA TRANSPORT | Protein Structure, Tertiary | Amino Acid Sequence | Protein Conformation, alpha-Helical | Peptides - chemistry | Humans | Phosphorylcholine - analogs & derivatives | Molecular Dynamics Simulation | Proline - chemistry | src Homology Domains | Thermodynamics | Animals | Protein Conformation, beta-Strand | Myelin Basic Protein - chemistry | Water - chemistry | Phosphorylcholine - chemistry | Protein Binding | Mice | Molecular Docking Simulation | Proto-Oncogene Proteins c-fyn - chemistry | Lipid Bilayers - chemistry | Binding Sites | Dimyristoylphosphatidylcholine - chemistry | Unithiol - chemistry | Molecular dynamics | Proline | Phospholipids | Myelin proteins | Proteins | Peptides | Myelin | Docking | Fuzzy | Myelin basic protein | Sheets | Fyn protein
Journal Article
The FEBS Journal, ISSN 1742-464X, 09/2017, Volume 284, Issue 18, pp. 2981 - 2999
We determined the crystal structure of Thr1, the self‐standing adenylation domain involved in the nonribosomal‐like biosynthesis of free 4‐chlorothreonine in... 
crystallography | kinetic analysis | nonribosomal code | adenylation domain | substrate specificity | NONRIBOSOMAL PEPTIDE SYNTHETASE | FIREFLY LUCIFERASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYRINGOTOXIN | SYRB2 | PSEUDOMONAS-SYRINGAE | CONFORMATION | NRPS ADENYLATION | AMINO-ACID | SYRINGOMYCIN | Threonine - chemistry | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Threonine - metabolism | Peptide Synthases - genetics | Peptide Synthases - chemistry | Adenosine Triphosphate - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Streptomyces - chemistry | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Peptide Synthases - metabolism | Threonine - analogs & derivatives | Sequence Homology, Amino Acid | Sequence Alignment | Threonine - biosynthesis | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Bacterial Proteins - metabolism | Streptomyces - enzymology | Kinetics | Adenosine Triphosphate - chemistry | Stereoisomers | Physiological aspects | Structure | Analysis | Crystals | Surgical implants | Threonine | Cocrystallization | Biosynthesis | Crystallography | Monomers | Substrates | Biomedical materials | Substrate specificity | Adenylation | Protein structure | ATP | Crystal structure
Journal Article
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 08/2017, Volume 85, Issue 8, pp. 1480 - 1492
ABSTRACT Within the CAZy database, there are 81 carbohydrate‐binding module (CBM) families. A CBM represents a non‐catalytic domain in a modular arrangement of... 
evolutionary relatedness | family GH13 pullulanases | protein sequence‐structural comparison | starch‐binding domain | carbohydrate‐binding module family CBM41 | carbohydrate-binding module family CBM41 | starch-binding domain | protein sequence-structural comparison | Klebsiella - metabolism | Multigene Family | Substrate Specificity | Klebsiella - chemistry | Phylogeny | Streptococcus - chemistry | Streptococcus - classification | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Databases, Protein | Glycoside Hydrolases - chemistry | Receptors, Cell Surface - chemistry | Protein Interaction Domains and Motifs | Klebsiella - classification | Binding Sites | Thermotoga maritima - chemistry | Thermotoga maritima - metabolism | Streptococcus - metabolism | Protein Structure, Tertiary | Protein Conformation, alpha-Helical | Computational Biology | Models, Molecular | Receptors, Cell Surface - metabolism | alpha-Amylases - metabolism | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Thermotoga maritima - classification | Protein Conformation, beta-Strand | alpha-Amylases - chemistry | Protein Binding | Glycoside Hydrolases - metabolism | Evolution, Molecular | Proteins | Tryptophan | Amylases | Protein binding | Klebsiella | Carbohydrates | Residues | Subdivisions | Taxonomy | Starch | Aromatics | Glucan | Streptococcus | Bacteria | Catalysis | Bioinformatics | Binding sites
Journal Article
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 09/2018, Volume 46, Issue 17, pp. 9220 - 9235
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2016, Volume 64, Issue 2, pp. 236 - 250
Caspase-8 activation can be triggered by death receptor-mediated formation of the death-inducing signaling complex (DISC) and by the inflammasome adaptor ASC.... 
caspase-8 | DED | MC159 | cFLIP | DISC | Fas | death domain | FADD | vFLIP | filament | APOPTOSIS | ACTIVATION | IMMUNE-SYSTEM | INHIBITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | UNIFIED MODEL | EFFECTOR DOMAIN | CELL-DEATH | CELL BIOLOGY | Death Domain Receptor Signaling Adaptor Proteins - chemistry | Apoptosis - drug effects | Cytoskeletal Proteins - genetics | Humans | Caspase 8 - metabolism | Caspase 8 - chemistry | CASP8 and FADD-Like Apoptosis Regulating Protein - chemistry | Death Domain Receptor Signaling Adaptor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Caspase 8 - genetics | Transfection | Cytoskeletal Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | CASP8 and FADD-Like Apoptosis Regulating Protein - metabolism | Death Effector Domain | Fas-Associated Death Domain Protein - genetics | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | CASP8 and FADD-Like Apoptosis Regulating Protein - genetics | Jurkat Cells | Viral Proteins - chemistry | Fas-Associated Death Domain Protein - metabolism | Viral Proteins - genetics | fas Receptor - pharmacology | Cytoskeletal Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Plasmids - metabolism | Fas-Associated Death Domain Protein - chemistry | Cryoelectron Microscopy | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | CARD Signaling Adaptor Proteins | Plasmids - chemistry | Protein Binding | Recombinant Fusion Proteins - genetics | Death Domain Receptor Signaling Adaptor Proteins - metabolism | Autoimmunity | Medical colleges | Skin diseases | Molecular biology | Analysis | Index Medicus
Journal Article
Journal Article
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