Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (5998) 5998
Publication (835) 835
Book Chapter (60) 60
Dissertation (37) 37
Book Review (30) 30
Conference Proceeding (15) 15
Government Document (3) 3
Web Resource (2) 2
Book / eBook (1) 1
Magazine Article (1) 1
Newspaper Article (1) 1
Streaming Video (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
humans (2900) 2900
index medicus (2347) 2347
animals (2042) 2042
14-3-3 proteins (2022) 2022
phosphorylation (1926) 1926
14-3-3 proteins - metabolism (1871) 1871
biochemistry & molecular biology (1485) 1485
14-3-3 protein (1311) 1311
proteins (1265) 1265
cell biology (1080) 1080
14-3-3 proteins - genetics (943) 943
protein binding (927) 927
mice (860) 860
female (853) 853
signal transduction (814) 814
amino acid sequence (796) 796
14-3-3 (785) 785
molecular sequence data (785) 785
male (773) 773
expression (666) 666
apoptosis (628) 628
binding (571) 571
14-3-3-proteins (517) 517
activation (509) 509
neurosciences (502) 502
cell line (462) 462
middle aged (462) 462
mutation (449) 449
gene expression (447) 447
tyrosine 3-monooxygenase (446) 446
plant sciences (435) 435
research (435) 435
binding sites (418) 418
cell line, tumor (416) 416
identification (416) 416
rats (413) 413
cancer (409) 409
oncology (406) 406
tyrosine 3-monooxygenase - metabolism (381) 381
aged (379) 379
physiological aspects (369) 369
article (355) 355
analysis (347) 347
research article (343) 343
protein (330) 330
blotting, western (318) 318
14-3-3 proteins - chemistry (316) 316
proteomics (314) 314
cell cycle (313) 313
multidisciplinary sciences (313) 313
protein-serine-threonine kinases - metabolism (312) 312
kinases (306) 306
clinical neurology (304) 304
proteins - metabolism (304) 304
cells, cultured (300) 300
adult (296) 296
cells (279) 279
biology (275) 275
in-vivo (271) 271
creutzfeldt-jakob disease (262) 262
kinase (255) 255
gene (251) 251
transfection (249) 249
biophysics (248) 248
genetic aspects (248) 248
localization (244) 244
immunohistochemistry (243) 243
genes (242) 242
mass spectrometry (240) 240
protein structure, tertiary (240) 240
gene-expression (238) 238
exoribonucleases (237) 237
base sequence (235) 235
genetics & heredity (232) 232
creutzfeldt-jakob syndrome - diagnosis (231) 231
brain (229) 229
medicine (228) 228
life sciences (222) 222
models, biological (218) 218
hela cells (214) 214
cerebrospinal-fluid (207) 207
diagnosis (207) 207
science (201) 201
protein isoforms - metabolism (197) 197
sequence homology, amino acid (197) 197
gene expression regulation (195) 195
biomarkers, tumor - metabolism (193) 193
cell nucleus - metabolism (193) 193
14-3-3 proteins - cerebrospinal fluid (191) 191
models, molecular (191) 191
hek293 cells (182) 182
enzyme activation (181) 181
family (180) 180
plants (179) 179
biochemistry (178) 178
proteins - genetics (178) 178
signal transduction - physiology (178) 178
serine - metabolism (174) 174
transcription factors - metabolism (174) 174
biochemical research methods (172) 172
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (5897) 5897
Chinese (68) 68
Japanese (32) 32
French (22) 22
Spanish (21) 21
German (12) 12
Polish (11) 11
Korean (9) 9
Russian (6) 6
Czech (3) 3
Dutch (2) 2
Portuguese (1) 1
Slovak (1) 1
Swedish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text The association of AMPK with ULK1 regulates autophagy
by Lee, Jong Woo and Park, Sungman and Takahashi, Yoshinori and Wang, Hong-Gang
PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 11, p. e15394
Autophagy is a highly orchestrated intracellular bulk degradation process that is activated by various environmental stresses. The serine/threonine kinase... 
COMPLEX | ACTIVATED PROTEIN-KINASE | METABOLISM | PHOSPHORYLATION | MACHINERY | BIOLOGY | INHIBITS CELL-GROWTH | INDUCTION | SACCHAROMYCES-CEREVISIAE | ATG13 | DEGENERATION | AMP-Activated Protein Kinases - metabolism | Phosphorylation | Immunoprecipitation | Humans | Multiprotein Complexes | Immunoblotting | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy | Protein Subunits - metabolism | Autophagy-Related Protein-1 Homolog | Mechanistic Target of Rapamycin Complex 1 | Transfection | RNA Interference | HEK293 Cells | Regulatory-Associated Protein of mTOR | Binding Sites | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | 14-3-3 Proteins - genetics | Protein Subunits - genetics | Cell Line | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Mice, Knockout | 14-3-3 Proteins - metabolism | Proteins - genetics | Animals | Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Cell Line, Tumor | Protein Binding | Mice | TOR Serine-Threonine Kinases | Mutation | Adaptor Proteins, Signal Transducing - metabolism | AMP-Activated Protein Kinases - genetics | Microscopy, Fluorescence | TOR protein | Yeast | Homology | Kinases | Inactivation | Proteins | Cell growth | Cell cycle | Binding | Biodegradation | Deactivation | Threonine | Pharmacology | Metabolism | Mammals | Environmental stress | Medicine | TSC2 protein | 14-3-3 protein | Insects | Environmental degradation | Protein-serine/threonine kinase | Regulation | Phagocytosis | Cancer | Apoptosis
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text Bioinformatic and experimental survey of 14-3-3-binding sites
by Johnson, Catherine and Crowther, Sandra and Stafford, Margaret J and Campbell, David G and Toth, Rachel and MacKintosh, Carol
Biochemical Journal, ISSN 0264-6021, 04/2010, Volume 427, Issue 1, pp. 69 - 78
More than 200 phosphorylated 14-3-3-binding sites in the literature were analysed to define 14-3-3 specificities, identify relevant protein kinases, and give... 
Evolution | 14-3-3 protein | Disrupted-in-schizophrenia 1 (DISC1) | calmodulin-dependent protein kinase | AGC protein kinase | NEURONAL MIGRATION | SIGNALING PATHWAYS | MEMBRANE H+-ATPASE | REGULATING 14-3-3 BINDING | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | EUKARYOTIC PROTEIN-KINASES | evolution | NUCLEAR-LOCALIZATION | EXOENZYME-S | STRUCTURAL BASIS | Ca2+/calmodulin-dependent protein kinase | disrupted-in-schizophrenia 1 (DISC1) | ENDOPLASMIC-RETICULUM | Protein Kinases - metabolism | Phosphorylation | Immunoprecipitation | Humans | RNA, Messenger - genetics | Cells, Cultured | Computational Biology | Kidney - cytology | RNA, Messenger - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | 14-3-3 Proteins - metabolism | Nerve Tissue Proteins - metabolism | Kidney - metabolism | Carrier Proteins - metabolism | Protein Binding | Binding Sites | Dimerization | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | 14-3-3 Proteins - genetics | Bcl-2-associated death promoter | AANAT, serotonin acetyltransferase | FOXO, Forkhead box O | KLC, kinesin light chain | CDK5, cyclin-dependent kinase 5 | HEK, human embryonic kidney | MARK, microtubule affinity-regulating kinase | AMPK, AMP-activated protein kinase | EST, expressed sequence tag | PKB, protein kinase B | RSK, ribosomal S6 kinase | CaMK, Ca2 | GLUT4, glucose transporter 4 | protein kinase G | GST, glutathione transferase | HDAC, histone deacetylase | HAP1A, Huntingtin-associated protein 1A | DIG, digoxigenin | PKC, protein kinase C | BAD, Bcl-XL | PP2A, protein phosphatase 2A | DSTT, Division of Signal Transduction Therapy | HA, haemagglutinin | AGC, protein kinase A | Ca2 | PI4K, phosphoinositide 4-kinase | DISC1, disrupted-in-schizophrenia 1 | protein kinase C family kinase | YAP1, yes-associated protein 1
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family
by Xiaowen Yang and Wen Hwa Lee and Frank Sobott and Evangelos Papagrigoriou and Carol V. Robinson and J. Günter Grossmann and Michael Sundström and Declan A. Doyle and Jonathan M. Elkins
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2006, Volume 103, Issue 46, pp. 17237 - 17242
The seven members of the human 14-3-3 protein family regulate a diverse range of cell signaling pathways by formation of proteinprotein complexes with... 
Protein isoforms | 14-3-3 proteins | Proteins | Hydrogen bonds | Atomic interactions | Crystallization | Dimers | Dimerization | Monomers | Crystal structure | Signaling | Phosphorylation | MESSENGER-RNAS | signaling | EXOENZYME-S | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | IN-VIVO | SURFACE EXPRESSION | MOLECULAR-CLONING | RAT CDNAS | CEREBROSPINAL-FLUID | phosphorylation | BINDING | Isoenzymes - genetics | Models, Molecular | Crystallography, X-Ray | Isoenzymes - chemistry | 14-3-3 Proteins - metabolism | 14-3-3 Proteins - classification | Animals | Isoenzymes - metabolism | Protein Structure, Quaternary | Protein Binding | 14-3-3 Proteins - chemistry | 14-3-3 Proteins - genetics | Protein-protein interactions | Research | Biological Sciences
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text Molecular tweezers modulate 14-3-3 protein-protein interactions
by Bier, David and Rose, Rolf and Bravo-Roiguez, Kenny and Bartel, Maria and Ramirez-Anguita, Juan Manuel and Dutt, Som and Wilch, Constanze and Klärner, Frank-Gerrit and Sanchez-Garcia, Elsa and Schrader, Thomas and Ottmann, Christian
Nature Chemistry, ISSN 1755-4330, 03/2013, Volume 5, Issue 3, pp. 234 - 239
Supramolecular chemistry has recently emerged as a promising way to modulate protein functions, but devising molecules that will interact with a protein in the... 
Phosphorylation | Proto-Oncogene Proteins c-raf/chemistry | Humans | Molecular Conformation | Models, Molecular | ADP Ribose Transferases/chemistry | Bacterial Toxins/chemistry | Journal Article | Recombinant Proteins/chemistry | Biomimetic Materials/chemistry | Research Support, Non-U.S. Gov't | Protein Binding | 14-3-3 Proteins/chemistry | ACTIVATION | COMPLEX | EXOENZYME-S | RECOGNITION | LIGANDS | DYNAMICS | IDENTIFICATION | BINDING | CHEMISTRY, MULTIDISCIPLINARY | DISCOVERY | PEPTIDE | Recombinant Proteins - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Bacterial Toxins - chemistry | Proto-Oncogene Proteins c-raf - metabolism | 14-3-3 Proteins - metabolism | Biomimetic Materials - metabolism | Bacterial Toxins - metabolism | Proto-Oncogene Proteins c-raf - chemistry | 14-3-3 Proteins - chemistry | Biomimetic Materials - chemistry | 14-3-3 Proteins - genetics | ADP Ribose Transferases - chemistry | ADP Ribose Transferases - metabolism | Binding | Salts | Computer simulation | Adapters | Crystallography | Proteins | Organic chemistry | 14-3-3 protein | Lysine | Biomolecules | Mathematical models | Protein interaction | Adapter proteins | Structural analysis
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Arabidopsis Protein Kinase PKS5 Inhibits the Plasma Membrane H⁺-ATPase by Preventing Interaction with 14-3-3 Protein
by Anja T. Fuglsang and Yan Guo and Tracey A. Cuin and Quansheng Qiu and Chunpeng Song and Kim A. Kristiansen and Katrine Bych and Alexander Schulz and Sergey Shabala and Karen S. Schumaker and Michael G. Palmgren and Jian-Kang Zhu
The Plant Cell, ISSN 1040-4651, 5/2007, Volume 19, Issue 5, pp. 1617 - 1634
Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal and environmental cues, including auxin, blue... 
Proteins | 14-3-3 proteins | Yeasts | Phosphorylation | Plant roots | Cell membranes | Plants | Seedlings | Plant cells | CELLS | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BLUE-LIGHT | PLANT SCIENCES | CELL BIOLOGY | ION FLUXES | PLANT SALT TOLERANCE | C-TERMINAL REGION | CALCIUM | STRESS SIGNAL-TRANSDUCTION | BINDING-SITE | REGULATORY DOMAIN | Protons | Gene Expression Regulation, Enzymologic - drug effects | Arabidopsis - enzymology | Adaptation, Physiological - drug effects | Molecular Sequence Data | DNA, Bacterial | Plant Roots - drug effects | Arabidopsis Proteins - metabolism | Saccharomyces cerevisiae - metabolism | RNA Interference | Protein Binding - drug effects | Ethyl Methanesulfonate | Proton-Translocating ATPases - antagonists & inhibitors | Cell Membrane - drug effects | Protein-Serine-Threonine Kinases - metabolism | Membrane Potentials - drug effects | Amino Acid Sequence | Arabidopsis Proteins - genetics | Arabidopsis - drug effects | Plant Roots - metabolism | Arabidopsis - cytology | Protein-Serine-Threonine Kinases - genetics | Down-Regulation - drug effects | Mutation - genetics | Phosphoserine - metabolism | Proton-Translocating ATPases - chemistry | 14-3-3 Proteins - metabolism | Arabidopsis - genetics | Cell Membrane - enzymology | Gene Expression Regulation, Plant - drug effects | Arabidopsis Proteins - chemistry | Calcium Signaling - drug effects | Alleles | Plant Growth Regulators - pharmacology | Arabidopsis Proteins - antagonists & inhibitors | Hydrogen-Ion Concentration
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator
by Sluchanko, Nikolai N and Beelen, Steven and Kulikova, Alexandra A and Weeks, Stephen D and Antson, Alfred A and Gusev, Nikolai B and Strelkov, Sergei V
Structure, ISSN 0969-2126, 02/2017, Volume 25, Issue 2, pp. 305 - 316
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6,... 
14-3-3 proteins | smooth muscle relaxation | small heat shock proteins | regulatory complex | crystal structure | protein-protein interaction | phosphopeptides | conformational change | small-angle X-ray scattering | intrinsically disordered regions | PHOSPHORYLATION | MOLECULE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-B-CRYSTALLIN | CELL BIOLOGY | DOMAIN DIMERS | BIOPHYSICS | PURIFICATION | AIRWAY SMOOTH-MUSCLE | BINDING | EXPRESSION | WEB SERVER | HSP20 HSPB6 | Exoribonucleases - genetics | Phosphorylation | Humans | Protein Multimerization | Exoribonucleases - chemistry | Substrate Specificity | Crystallography, X-Ray | HSP20 Heat-Shock Proteins - genetics | Phosphoproteins - metabolism | HSP20 Heat-Shock Proteins - metabolism | Phosphoproteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Protein Interaction Domains and Motifs | Binding Sites | HSP20 Heat-Shock Proteins - chemistry | 14-3-3 Proteins - genetics | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Signal Transduction | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | 14-3-3 Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | 14-3-3 Proteins - chemistry | Biomarkers, Tumor - genetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Fluorescence spectroscopy | Proteolysis | Analysis | Crystals | Fluorescence | Atoms | Heat shock proteins | Molecular biology | Structure | Protein-protein interactions | small angle X-ray scattering
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Small-molecule stabilization of the p53 - 14-3-3 protein-protein interaction
by Doveston, R.G and Kuusk, A and Anei, S.A and Leysen, S and Cao, Q and Castaldi, M.P and Henicks, A and Brunsveld, L and Chen, H and Boyd, H and Ottmann, C
FEBS Letters, ISSN 0014-5793, 08/2017, Volume 591, Issue 16, pp. 2449 - 2457
14-3-3 proteins are positive regulators of the tumor suppressor p53, the mutation of which is implicated in many human cancers. Current strategies for... 
Letter | Research Support, Non-U.S. Gov't | PPI stabilization | protein crystallography | fluorescence polarization | isothermal titration calorimetry | 14‐3‐3 proteins | p53 | 14-3-3 proteins | ACTIVATION | BIOPHYSICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | P53 PATHWAY | BINDING | CELL BIOLOGY | 14-3-3 Proteins - metabolism | Protein Structure, Secondary | Protein Binding - drug effects | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | 14-3-3 Proteins - chemistry | Tumor Suppressor Protein p53 - chemistry | Protein Stability | Glycosides - pharmacology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Moonlighting chaperone‐like activity of the universal regulatory 14‐3‐3 proteins
by Sluchanko, Nikolai N and Gusev, Nikolai B
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
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text Structural basis of 14-3-3 protein functions
by Obsil, Tomas and Obsilova, Veronika
Seminars in Cell and Developmental Biology, ISSN 1084-9521, 09/2011, Volume 22, Issue 7, pp. 663 - 672
► Structure of 14-3-3 proteins. ► Target recognition by 14-3-3 proteins. ► Common aspects of 14-3-3 protein complexes. ► Structural basis of 14-3-3 protein... 
14-3-3 | Phosphorylation | Protein–protein interactions | Structure | Protein-protein interactions | FORKHEAD TRANSCRIPTION FACTOR | DNA-BINDING | LIGAND-BINDING | MEMBRANE H+-ATPASE | PHOSPHORYLATED NITRATE REDUCTASE | TYROSINE-HYDROXYLASE | SUBCELLULAR-LOCALIZATION | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | EXOENZYME-S | ACTIVATES TRYPTOPHAN 5-MONOOXYGENASE | SEROTONIN N-ACETYLTRANSFERASE | Protein Structure, Tertiary | Humans | Models, Molecular | Eukaryota - metabolism | 14-3-3 Proteins - metabolism | Genetic Variation | Animals | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Protein Binding | 14-3-3 Proteins - chemistry | Protein Conformation | Protein Interaction Domains and Motifs | Binding Sites | 14-3-3 Proteins - genetics | DNA-Binding Proteins | Proteins | Physiological aspects | G proteins
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text 14-3-3 proteins: A historic overview
by Aitken, Alastair
Seminars in Cancer Biology, ISSN 1044-579X, 2006, Volume 16, Issue 3, pp. 162 - 172
This chapter includes a historic overview of 14-3-3 proteins with an emphasis on the differences between potentially cancer-relevant isoforms on the genomic,... 
Phospho-binding motifs | 14-3-3 Proteins | History | Protein interactions | Protein kinases | 14-3-3 proteins | LIGAND-BINDING | KINASE-C INHIBITOR | PHOSPHORYLATED NITRATE REDUCTASE | CRYSTAL-STRUCTURE | DNA-DAMAGE | protein kinases | history | BINDING-PROTEIN BELONGS | BRAIN 14-3-3 PROTEIN | FUNCTIONAL SPECIFICITY | protein interactions | ONCOLOGY | IN-VIVO | phospho-binding motifs | ZETA-ISOFORM | Protein Kinases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Phosphorylation | Signal Transduction | History, 20th Century | 14-3-3 Proteins - history | Molecular Sequence Data | Terminology as Topic | 14-3-3 Proteins - isolation & purification | 14-3-3 Proteins - metabolism | Animals | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Protein Binding | Drosophila - metabolism | Dimerization | Proteins
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights