X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (2845) 2845
Publication (433) 433
Book Review (41) 41
Book Chapter (33) 33
Book / eBook (12) 12
Newsletter (11) 11
Conference Proceeding (10) 10
Data Set (2) 2
Dissertation (2) 2
Poster (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
animals (1724) 1724
phosphorylation (1476) 1476
phosphoprotein phosphatases - metabolism (1422) 1422
humans (1225) 1225
biochemistry & molecular biology (1011) 1011
index medicus (884) 884
protein phosphatase 1 (763) 763
cell biology (761) 761
phosphoprotein phosphatases - antagonists & inhibitors (697) 697
phosphatases (669) 669
phosphoprotein phosphatases - genetics (568) 568
proteins (552) 552
protein phosphatase (541) 541
rats (523) 523
okadaic acid (502) 502
mice (496) 496
molecular sequence data (478) 478
amino acid sequence (465) 465
signal transduction (447) 447
enzyme inhibitors - pharmacology (436) 436
male (416) 416
phosphatase (338) 338
kinases (321) 321
phosphoprotein phosphatases - chemistry (317) 317
catalytic subunit (314) 314
phosphoprotein phosphatase (311) 311
protein phosphatase 2 (306) 306
protein binding (299) 299
neurosciences (293) 293
okadaic acid - pharmacology (293) 293
phosphoproteins - metabolism (291) 291
activation (282) 282
cell line (252) 252
female (247) 247
biophysics (242) 242
expression (242) 242
research article (240) 240
cells, cultured (239) 239
research (239) 239
kinase (238) 238
identification (229) 229
phosphoprotein phosphatases - physiology (221) 221
article (211) 211
macromolecular substances (209) 209
dephosphorylation (203) 203
gene expression (201) 201
physiological aspects (201) 201
multidisciplinary sciences (200) 200
mutation (198) 198
apoptosis (193) 193
base sequence (180) 180
phosphorylation - drug effects (177) 177
binding sites (176) 176
mitosis (172) 172
cell cycle (168) 168
binding (167) 167
oncology (166) 166
blotting, western (165) 165
physiology (164) 164
biology (161) 161
cells (161) 161
protein-serine-threonine kinases - metabolism (161) 161
pharmacology & pharmacy (158) 158
protein phosphatase 2a (158) 158
oxazoles - pharmacology (152) 152
sequence homology, amino acid (152) 152
kinetics (150) 150
enzyme activation (147) 147
rabbits (146) 146
protein kinases (142) 142
rabbit skeletal-muscle (142) 142
enzymes (140) 140
protein phosphatase 1 - metabolism (140) 140
pp2a (139) 139
saccharomyces-cerevisiae (139) 139
inhibition (137) 137
genetics & heredity (136) 136
cell line, tumor (135) 135
time factors (135) 135
hela cells (134) 134
rats, sprague-dawley (133) 133
cancer (131) 131
substrate specificity (130) 130
cloning, molecular (129) 129
biochemistry (128) 128
pp1 (128) 128
gene (125) 125
medicine (124) 124
models, biological (123) 123
nuclear proteins - metabolism (123) 123
protein phosphatases (122) 122
life sciences (121) 121
protein kinases - metabolism (121) 121
dose-response relationship, drug (120) 120
brain (119) 119
signal transduction - physiology (119) 119
genetic aspects (118) 118
science (118) 118
signal-transduction (117) 117
cyclic amp-dependent protein kinases - metabolism (116) 116
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


Journal Article
Biochemical Journal, ISSN 0264-6021, 04/2011, Volume 435, Issue 1, pp. 73 - 83
PP1 (protein phosphatase 1) is among the most conserved enzymes known, with one or more isoforms present in all sequenced eukaryotic genomes. PP1... 
Phylogenetics | Nucleus | Signal transduction | TAP-tag | Protein phosphatase 1 (PP1) | Inhibitory protein | TRANSFORMATION | signal transduction | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | PLANT-CELLS | nucleus | protein phosphatase 1 (PP1) | SACCHAROMYCES-CEREVISIAE | FUNCTIONAL GENOMICS | INTERACTOME | INHIBITOR-2 | STRUCTURAL BASIS | PURIFICATION | phylogenetics | inhibitory protein | Protein Phosphatase 1 - chemistry | Molecular Sequence Data | Phylogeny | Phosphoproteins - metabolism | Protein Isoforms - isolation & purification | Plant Epidermis - metabolism | Recombinant Fusion Proteins - metabolism | Phosphoproteins - chemistry | Protein Subunits - metabolism | Arabidopsis Proteins - metabolism | Cell Nucleus - metabolism | Protein Isoforms - metabolism | Protein Subunits - isolation & purification | Databases, Protein | Protein Phosphatase 1 - genetics | Plant Epidermis - cytology | Protein Subunits - genetics | Amino Acid Sequence | Cell Line | Arabidopsis Proteins - genetics | Computational Biology - methods | Protein Phosphatase 1 - isolation & purification | Plant Structures - metabolism | Phosphoproteins - genetics | Plant Leaves - cytology | Arabidopsis - metabolism | Protein Transport | Arabidopsis - genetics | Arabidopsis Proteins - isolation & purification | Sequence Homology, Amino Acid | Protein Phosphatase 1 - metabolism | Sequence Alignment | Arabidopsis Proteins - chemistry | Plant Leaves - metabolism | Phosphoproteins - isolation & purification | Protein Subunits - chemistry | Protein Isoforms - genetics
Journal Article
Journal Article
Basic Research in Cardiology, ISSN 0300-8428, 9/2017, Volume 112, Issue 5, pp. 1 - 1
To access, purchase, authenticate, or subscribe to the full-text of this article, please visit this link: http://dx.doi.org/10.1007/s00395-017-0638-x 
Medicine & Public Health | Cardiology | Heart failure | Heart | Phosphatases | Atrial fibrillation | Protein phosphatase | Fibrillation | Phosphoprotein phosphatase | Heart diseases | Isoforms
Journal Article
Journal Article
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2014, Volume 289, Issue 33, pp. 23154 - 23167
Journal Article
Molecular and Cellular Neuroscience, ISSN 1044-7431, 2006, Volume 32, Issue 1, pp. 15 - 26
Mutations in (DCX) cause X-linked lissencephaly (“smooth brain”) and double cortex syndrome in humans. DCX is highly phosphorylated in migrating neurons. Here,... 
Neurabin II | Phosphorylation | Spinophilin | Lissencephaly | Protein phosphatase 1 | Doublecortin | spinophilin | NEURONAL MIGRATION | PHOSPHATASE-1 CATALYTIC SUBUNIT | DOMAIN | doublecortin | NEURABIN-II | KINASE | MICROTUBULE-ASSOCIATED PROTEIN | NEUROSCIENCES | DENDRITIC SPINES | lissencephaly | neurabin II | ACTIN CYTOSKELETON | protein phosphatase 1 | FILAMENT-BINDING PROTEIN | phosphorylation | Microtubule-Associated Proteins - chemistry | Microtubule-Associated Proteins - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | JNK Mitogen-Activated Protein Kinases - metabolism | Neurons - cytology | Cerebral Cortex - cytology | Cell Movement - physiology | Cerebral Cortex - metabolism | Nerve Tissue Proteins - chemistry | Nervous System Malformations - metabolism | Binding Sites - physiology | Nervous System Malformations - physiopathology | Microfilament Proteins - metabolism | Neurons - metabolism | Nervous System Malformations - genetics | Cell Differentiation - physiology | Protein Phosphatase 1 | Gene Expression Regulation, Developmental - physiology | Cell Line | Microfilament Proteins - chemistry | Neuropeptides - metabolism | Mice, Inbred ICR | Nerve Tissue Proteins - metabolism | Amino Acid Motifs - physiology | Animals | Cerebral Cortex - embryology | Mice | Adaptor Proteins, Signal Transducing - metabolism | Macromolecular Substances - metabolism | Neuropeptides - chemistry | Protein Structure, Tertiary - physiology | Proteins | Neurons | Phosphatases
Journal Article
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 10/2019, Volume 116, Issue 41, pp. 20472 - 20481
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 39, pp. 15152 - 15162
The protein Ser/Thr phosphatase PP1 catalyzes an important fraction of protein dephosphorylation events and forms highly specific holoenzymes through an... 
enzyme | SPLICING FACTORS | CATALYTIC SUBUNIT | REGULATORY SUBUNIT | SPECIFICITY | signal transduction | BIOCHEMISTRY & MOLECULAR BIOLOGY | MYPT1 | KINASE | IDENTIFICATION | PHOSPHORYLATION SITES | phosphoprotein phosphatase 1 (PP1) | NUCLEAR INHIBITOR | substrate specificity | phosphatase | PNUTS | NIPP1 | substrate mapping | RepoMan | REPO-MAN | Methods and Resources
Journal Article
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 09/2019, Volume 294, Issue 36, pp. 13280 - 13291
Transforming growth factor-beta membrane associated protein (TIMAP) is an endothelial cell (EC)-predominant PP1 regulatory subunit and a member of the myosin... 
SPECIFICITY | PHOSPHORYLATION | endothelial cell | angiogenesis | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | myosin phosphatase | MYPT1 | BARRIER | myosin | TARGETING SUBUNIT | DOCKING MOTIF | OKADAIC ACID | BETA | phosphoprotein phosphatase 1 (PP1) | SMOOTH-MUSCLE | inhibitor | STRUCTURAL BASIS | microcystin | Cell Biology
Journal Article