X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
biochemistry & molecular biology (1118) 1118
humans (991) 991
proteins (753) 753
intrinsically disordered proteins (694) 694
protein binding (671) 671
intrinsically disordered proteins - metabolism (609) 609
animals (576) 576
intrinsically disordered proteins - chemistry (575) 575
models, molecular (482) 482
protein conformation (478) 478
amino acid sequence (440) 440
intrinsically disordered protein (438) 438
protein folding (438) 438
biophysics (339) 339
cell biology (331) 331
binding (323) 323
protein structure, tertiary (306) 306
analysis (275) 275
molecular sequence data (263) 263
intrinsically unstructured proteins (261) 261
binding sites (260) 260
protein structure, secondary (244) 244
phosphorylation (233) 233
proteins - metabolism (202) 202
intrinsically disordered proteins - genetics (195) 195
proteins - chemistry (194) 194
multidisciplinary sciences (193) 193
unstructured proteins (191) 191
biology (172) 172
kinetics (170) 170
life sciences (168) 168
nuclear magnetic resonance, biomolecular (164) 164
research (162) 162
molecular dynamics simulation (154) 154
physiological aspects (151) 151
thermodynamics (150) 150
crystal-structure (144) 144
secondary structure (140) 140
circular dichroism (139) 139
intrinsic disorder (139) 139
mutation (136) 136
natively unfolded proteins (133) 133
mice (131) 131
molecular biology (128) 128
protein domains (127) 127
protein interaction domains and motifs (126) 126
research article (126) 126
alpha-synuclein (125) 125
nmr (125) 125
prediction (125) 125
protein (125) 125
recognition (124) 124
protein-protein interactions (122) 122
signal transduction (119) 119
structural basis (119) 119
gene expression (115) 115
recombinant proteins - chemistry (112) 112
amino acids (111) 111
chemistry, multidisciplinary (111) 111
biochemistry (110) 110
peptides (108) 108
amino acid motifs (106) 106
protein processing, post-translational (105) 105
aggregation (103) 103
protein structure (102) 102
domain (101) 101
recombinant proteins - metabolism (101) 101
spectroscopy (98) 98
protein-protein interaction (97) 97
biochemical research methods (94) 94
nuclear magnetic resonance (94) 94
mechanism (93) 93
dynamics (92) 92
escherichia coli - metabolism (91) 91
structural disorder (91) 91
structure-activity relationship (86) 86
ligands (85) 85
magnetic resonance spectroscopy (83) 83
sequence (82) 82
protein multimerization (81) 81
protein stability (81) 81
computational biology (80) 80
chemical properties (79) 79
databases, protein (79) 79
biochemistry, general (78) 78
escherichia coli - genetics (77) 77
escherichia-coli (77) 77
review (77) 77
sequence alignment (77) 77
biochemistry, molecular biology (76) 76
chemistry (76) 76
cancer (75) 75
complex (75) 75
recombinant proteins - genetics (75) 75
evolution, molecular (74) 74
in-vitro (74) 74
biomolecules (73) 73
molecular recognition (73) 73
nuclear magnetic resonance spectroscopy (73) 73
peptides - chemistry (73) 73
more...
Library Location Library Location
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Nature reviews. Molecular cell biology, ISSN 1471-0080, 2014, Volume 16, Issue 1, pp. 18 - 29
Journal Article
Journal Article
eLife, ISSN 2050-084X, 2014, Volume 3, p. e04591
.... The molecules and reactions that drive these dynamics in vivo are not well understood. In this study, we present evidence that a group of intrinsically disordered, serine-rich proteins regulate the dynamics of P granules in C. elegans embryos. The MEG... 
stem cells | C. elegans | cell biology | developmental biology | germ plasm | RNA granules | intrinsically disordered proteins | OOCYTE | CELL-FREE FORMATION | GERMLINE | CAENORHABDITIS-ELEGANS | KINASE | BIOLOGY | DYRK FAMILY | COMPONENTS | DEGRADATION | SEGREGATION | P GRANULES | Phosphorylation | Protein-Tyrosine Kinases - metabolism | Caenorhabditis elegans Proteins - chemistry | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Green Fluorescent Proteins - genetics | Cytoplasmic Granules - chemistry | Recombinant Fusion Proteins - metabolism | Protein-Tyrosine Kinases - genetics | RNA, Helminth - metabolism | Cytoplasmic Granules - metabolism | RNA, Helminth - genetics | Genes, Reporter | Amino Acid Sequence | Green Fluorescent Proteins - metabolism | Caenorhabditis elegans - metabolism | Caenorhabditis elegans - growth & development | Caenorhabditis elegans - genetics | Gene Expression Regulation | Protein Phosphatase 2 - genetics | Serine - metabolism | Protein Folding | RNA, Helminth - chemistry | Animals | Embryo, Nonmammalian | Protein Phosphatase 2 - metabolism | Recombinant Fusion Proteins - genetics | Protein Conformation | Caenorhabditis elegans Proteins - genetics | Studies | Proteins | Fertility | Serine | Dephosphorylation | Phosphatase | Ribonucleic acid--RNA | Embryos | Cytoplasm
Journal Article
Journal Article
Biochemistry (Easton), ISSN 0006-2960, 05/2017, Volume 56, Issue 18, pp. 2379 - 2384
...–target binding affinities. Increasing the level of residual structure in intrinsically disordered proteins (IDPs... 
UNSTRUCTURED PROTEINS | IMPROVED SENSITIVITY | SPECTROSCOPY | BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | KIX DOMAIN | Myeloid-Lymphoid Leukemia Protein - metabolism | Proline - metabolism | Humans | Myeloid-Lymphoid Leukemia Protein - chemistry | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Tumor Suppressor Protein p53 - genetics | Cloning, Molecular | Escherichia coli - metabolism | Conserved Sequence | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Histone-Lysine N-Methyltransferase - genetics | Membrane Proteins - genetics | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Intrinsically Disordered Proteins - genetics | Protein Folding | Proline - chemistry | Histone-Lysine N-Methyltransferase - chemistry | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Histone-Lysine N-Methyltransferase - metabolism | Membrane Proteins - chemistry | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Myeloid-Lymphoid Leukemia Protein - genetics | Protein Binding | Mice | Tumor Suppressor Protein p53 - chemistry | Mutation | Intrinsically Disordered Proteins - metabolism | Helix-loop-helix motif | Protein deficiency | Research
Journal Article
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2017, Volume 292, Issue 50, pp. 20509 - 20527
.... FtsZ comprises a polymerizing GTPase domain, an intrinsically disordered C-terminal linker (CTL... 
Caulobacter crescentus | GTP | intrinsically disordered protein | bacteria | cytoskeleton | CAULOBACTER | cytokinesis | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | bundling | BACTERIAL | SUGGESTS | IDENTIFICATION | electron microscopy (EM) | TUBULIN-LIKE PROTEIN | FtsZ | CELL-DIVISION PROTEIN | Z-RING | PROMOTES | Cytoskeletal Proteins - genetics | Protein Multimerization | Bacterial Proteins - chemistry | Guanosine Triphosphate - metabolism | Recombinant Fusion Proteins - metabolism | Caulobacter crescentus - metabolism | Gene Deletion | Cytoskeletal Proteins - metabolism | Membrane Proteins - metabolism | Protein Stability | Peptide Fragments - genetics | Cytoskeleton - chemistry | Recombinant Proteins - metabolism | Microscopy, Electron, Transmission | Peptide Fragments - metabolism | Membrane Proteins - genetics | Bacterial Proteins - genetics | Caulobacter crescentus - ultrastructure | Recombinant Proteins - chemistry | Cytoskeletal Proteins - chemistry | Cytoskeleton - ultrastructure | Recombinant Fusion Proteins - chemistry | Intrinsically Disordered Proteins - genetics | Hydrolysis | Peptide Fragments - chemistry | Membrane Proteins - chemistry | Intrinsically Disordered Proteins - chemistry | Cytoskeleton - metabolism | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Protein Conformation | Kinetics | Mutation | Amino Acid Substitution | Intrinsically Disordered Proteins - metabolism | Luminescent Proteins - metabolism | Microbiology
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2016, Volume 291, Issue 13, pp. 6714 - 6722
The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a particularly rich set of interactions with disordered and partly ordered partners, as a part of their ubiquitous role in facilitating transcription of genes... 
ACTIVATION DOMAIN | UNSTRUCTURED PROTEINS | viral oncoprotein | intrinsically disordered protein | coupled folding and binding | intrinsically disordered region | BIOCHEMISTRY & MOLECULAR BIOLOGY | structure-function | STAT transcription factor | C-MYB | transcriptional coactivator | VIRAL-PROTEINS | transcriptional activation | P53 TRANSACTIVATION DOMAIN | COMPLEX-FORMATION | cAMP response element-binding protein (CREB) | hypoxia-inducible factor (HIF) | IDP | STRUCTURAL BASIS | IDR | KIX DOMAIN | TAZ2 DOMAIN | PEPTIDE MOTIFS | protein-protein interaction | Humans | E1A-Associated p300 Protein - genetics | STAT Transcription Factors - metabolism | CREB-Binding Protein - chemistry | NF-kappa B - metabolism | E1A-Associated p300 Protein - metabolism | NF-kappa B - chemistry | Viral Proteins - metabolism | Tumor Suppressor Protein p53 - genetics | CREB-Binding Protein - genetics | CREB-Binding Protein - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - chemistry | Transcription, Genetic | Protein Interaction Domains and Motifs | Protein Structure, Secondary | Hypoxia-Inducible Factor 1, alpha Subunit - genetics | Viral Proteins - chemistry | E1A-Associated p300 Protein - chemistry | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Viral Proteins - genetics | Intrinsically Disordered Proteins - genetics | Protein Folding | STAT Transcription Factors - genetics | NF-kappa B - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | STAT Transcription Factors - chemistry | Tumor Suppressor Protein p53 - chemistry | Intrinsically Disordered Proteins - metabolism | Minireviews
Journal Article
Protein Science, ISSN 0961-8368, 04/2017, Volume 26, Issue 4, pp. 700 - 717
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 37, pp. 14942 - 14947
Journal Article