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Journal Article
Science, ISSN 0036-8075, 9/2011, Volume 333, Issue 6051, pp. 1891 - 1894
The unfolded protein response (UPR) detects the accumulation of unfolded proteins in the endoplasmic reticulum (ER) and adjusts the protein-folding capacity to... 
Yeasts | Messenger RNA | Ungulates | REPORTS | Amino acids | Ligands | Dimers | Coefficients | Goods and services tax | Monomers | Unfolded protein response | IRE1P | MESSENGER-RNA | SPECIFICITY | MECHANISM | PATHWAY | MULTIDISCIPLINARY SCIENCES | BIP | ENDOPLASMIC-RETICULUM | TRANSCRIPTION FACTOR | BINDING | REVEALS | Fungal Proteins - chemistry | Membrane Glycoproteins - metabolism | Membrane Glycoproteins - chemistry | Protein Multimerization | Stress, Physiological | Endoplasmic Reticulum - metabolism | Cathepsin A - chemistry | Cathepsin A - metabolism | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Glutathione Transferase - metabolism | Mutant Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Unfolded Protein Response | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Mutant Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Conformation | Protein-Serine-Threonine Kinases - chemistry | Fluorescence Polarization | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Research | Properties | Endoplasmic reticulum | Ligands (Biochemistry) | Protein binding | Signal transduction | Membranes | Cellular biology | Kinases | Protein folding
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6689 - 6695
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions... 
signaling | residual structure | electrostatics | coupled folding and binding | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein electrostatics | C-MYB | TRANSITION-STATE | INDUCED FIT | protein-protein interactions | INTRINSICALLY DISORDERED PROTEINS | LINEAGE LEUKEMIA PROTEIN | IDP | MOLECULAR RECOGNITION | KIX DOMAIN | SEQUENCE | protein folding | phi-value | TRANSACTIVATION DOMAIN | kinetics | biophysics | protein dynamic | CONFORMATIONAL SELECTION | Cyclic AMP Response Element-Binding Protein - chemistry | Humans | Myeloid Cell Leukemia Sequence 1 Protein - metabolism | CREB-Binding Protein - chemistry | Proto-Oncogene Proteins - chemistry | CREB-Binding Protein - genetics | CREB-Binding Protein - metabolism | Thermodynamics | Apoptosis Regulatory Proteins - genetics | Myeloid Cell Leukemia Sequence 1 Protein - chemistry | Protein Interaction Domains and Motifs | Proto-Oncogene Proteins - metabolism | Signal Transduction | Apoptosis Regulatory Proteins - chemistry | Proto-Oncogene Proteins - genetics | Static Electricity | Intrinsically Disordered Proteins - genetics | Molecular Dynamics Simulation | Myeloid Cell Leukemia Sequence 1 Protein - genetics | Protein Folding | Apoptosis Regulatory Proteins - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | Intrinsically Disordered Proteins - chemistry | Cyclic AMP Response Element-Binding Protein - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Kinetics | Intrinsically Disordered Proteins - metabolism | Minireviews
Journal Article
Journal Article
Science, ISSN 0036-8075, 2/2008, Volume 319, Issue 5866, pp. 1092 - 1096
Mammalian telomeres are protected by a six-protein complex: shelterin. Shelterin contains two closely related proteins (TRF1 and TRF2), which recruit various... 
Proteins | Telomeres | Colors | Atomic interactions | Amino acids | Reports | Grants | Electrostatics | Binding sites | Crystal structure | COMPLEX | DNA | INTERACTS | MULTIDISCIPLINARY SCIENCES | POLYMERASE | APOLLO | TIN2 | Humans | Molecular Sequence Data | Telomeric Repeat Binding Protein 1 - metabolism | Crystallography, X-Ray | TATA Box Binding Protein-Like Proteins - metabolism | Telomeric Repeat Binding Protein 1 - chemistry | Telomere-Binding Proteins - genetics | Inhibitor of Apoptosis Proteins - chemistry | TATA Box Binding Protein-Like Proteins - genetics | Tumor Suppressor Proteins - chemistry | TATA Box Binding Protein-Like Proteins - chemistry | Inhibitor of Apoptosis Proteins - metabolism | Nuclear Proteins - genetics | Telomere-Binding Proteins - metabolism | Dimerization | Protein Structure, Tertiary | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Protein Structure, Secondary | Telomeric Repeat Binding Protein 2 | Models, Molecular | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Amino Acid Motifs | Hydrogen Bonding | Mutant Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Conformation | Telomere-Binding Proteins - chemistry | Cellular proteins | Evaluation | Thyrotropin releasing factor | Influence | Properties | Protein binding | Protons | Biochemistry
Journal Article
Journal Article
Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6090, pp. 59 - 64
Journal Article
Cell, ISSN 0092-8674, 03/2017, Volume 168, Issue 6, pp. 1028 - 1040.e19
In eukaryotic cells, diverse stresses trigger coalescence of RNA-binding proteins into stress granules. In vitro, stress-granule-associated proteins can demix... 
membraneless organelle | RNA-binding protein | poly(A)-binding protein | intrinsically disordered protein | quinary structure | stress granules | heat shock | low-complexity region | energy depletion | HEAT-STRESS | MESSENGER-RNAS | TEMPERATURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | LIQUID DROPLETS | DISORDERED PROTEINS | TRANSITIONS | SACCHAROMYCES-CEREVISIAE | GRANULES | BINDING | CELL BIOLOGY | Amino Acid Sequence | Saccharomyces cerevisiae - physiology | Poly(A)-Binding Proteins - genetics | Proline - metabolism | Stress, Physiological | Hot Temperature | Saccharomyces cerevisiae Proteins - genetics | Cytoplasmic Granules - chemistry | Proline - analysis | Ribonucleases - metabolism | Saccharomyces cerevisiae - cytology | Sequence Alignment | Mutagenesis | Poly(A)-Binding Proteins - chemistry | Intrinsically Disordered Proteins - chemistry | Poly(A)-Binding Proteins - metabolism | Cytoplasmic Granules - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Domains | Saccharomyces cerevisiae - growth & development | Hydrogen-Ion Concentration | Intrinsically Disordered Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA | Physiological aspects | Stress (Physiology) | Sensors | Molecular biology | Binding proteins | Protein binding | Stress (Psychology) | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES | second messenger
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2013, Volume 288, Issue 52, pp. 37204 - 37215
Journal Article
Structure, ISSN 0969-2126, 10/2015, Volume 23, Issue 10, pp. 1848 - 1857
The ULK1 complex, consisting of the ULK1 protein kinase itself, FIP200, Atg13, and Atg101, controls the initiation of autophagy in animals. We determined the... 
protein structure | hydrogen-deuterium exchange | X-ray crystallography | Atg1 | autophagy | DOMAIN | PROTEIN | MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AUTOPHAGY | IDENTIFICATION | CELL BIOLOGY | BIOPHYSICS | ROLES | ARCHITECTURE | KINASE ULK1 | BINDING | Adaptor Proteins, Signal Transducing - chemistry | Autophagy-Related Proteins | Mad2 Proteins - metabolism | Vesicular Transport Proteins - metabolism | Humans | Protein Multimerization | Molecular Sequence Data | Crystallography, X-Ray | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy-Related Protein-1 Homolog | Spodoptera | Schizosaccharomyces - genetics | Sf9 Cells | Autophagy - genetics | Binding Sites | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Protein Structure, Secondary | Vesicular Transport Proteins - genetics | Protein-Serine-Threonine Kinases - genetics | Models, Molecular | Recombinant Proteins - chemistry | Vesicular Transport Proteins - chemistry | Mad2 Proteins - chemistry | Recombinant Proteins - genetics | Benzamidines - chemistry | Schizosaccharomyces - metabolism | Sequence Alignment | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Mad2 Proteins - genetics | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein-Serine-Threonine Kinases - chemistry | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Proteins | Cells | Hydrogen | Protein kinases
Journal Article
The FEBS Journal, ISSN 1742-464X, 05/2017, Volume 284, Issue 9, pp. 1279 - 1295
The ubiquitous eukaryotic 14‐3‐3 proteins coordinate multiple cellular processes due to their well‐known regulatory function, which is based on specific... 
hydrophobicity | signal transduction | dimer interface | aggregation | oligomeric structure | neurodegenerative disorders | chaperones | phosphorylation | 14‐3‐3 proteins | dimer–monomer equilibrium | 14-3-3 proteins | TAU-PROTEIN | FUNCTIONAL INTERACTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ISOFORM-SPECIFIC MANNER | SUBCELLULAR-LOCALIZATION | ALPHA-CRYSTALLIN | RAT-LIVER CYTOSOL | PRECURSOR PROTEINS | dimer-monomer equilibrium | MOLECULAR CHAPERONE | C-TERMINAL EXTENSION | MITOCHONDRIAL IMPORT | Phosphorylation | Molecular Chaperones - metabolism | Humans | Protein Multimerization | Protein Refolding | Models, Molecular | Molecular Chaperones - chemistry | Amino Acid Motifs | 14-3-3 Proteins - metabolism | Animals | Hydrophobic and Hydrophilic Interactions | 14-3-3 Proteins - chemistry | Protein Conformation | Protein Interaction Domains and Motifs | Protein Processing, Post-Translational | Binding Sites | Dimerization | Molecular Chaperones - agonists | Heat shock proteins | Control systems | Nervous system diseases | Prions | Huntingtin | Aggresomes | Neurodegenerative diseases | Hydrophobicity | Chaperones | Small heat shock proteins | Synuclein | Proteins | 14-3-3 protein | Eukaryotes | Molecular modelling | Tau protein | Protein folding | Quality control | Proteasomes | Molecular biology | Prion protein
Journal Article