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insulin (127) 127
phosphorylation (121) 121
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mice (99) 99
glucose - metabolism (95) 95
gtpase-activating proteins - metabolism (92) 92
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glucose metabolism (64) 64
rats (64) 64
glut4 (62) 62
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akt substrate (61) 61
biochemistry & molecular biology (59) 59
cell biology (58) 58
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muscles (53) 53
ampk (49) 49
physiological aspects (49) 49
proto-oncogene proteins c-akt - metabolism (49) 49
signal transduction (48) 48
dextrose (47) 47
activated protein-kinase (46) 46
glucose-transport (44) 44
muscle, skeletal - drug effects (44) 44
skeletal-muscle (44) 44
glucose transport (43) 43
amp-activated protein kinases - metabolism (41) 41
gtpase-activating-protein (41) 41
akt (40) 40
metabolism (39) 39
3t3-l1 adipocytes (37) 37
hormones, hormone substitutes, and hormone antagonists (37) 37
plasma-membrane (37) 37
tbc1d1 (37) 37
female (36) 36
insulin sensitivity (36) 36
research (36) 36
proteins (34) 34
transport (34) 34
adipocytes - metabolism (33) 33
article (33) 33
cell line (32) 32
3t3-l1 cells (31) 31
human skeletal-muscle (31) 31
phosphorylation - drug effects (31) 31
gtpase-activating proteins - genetics (30) 30
trafficking (30) 30
exercise - physiology (28) 28
obesity (28) 28
glucose uptake (27) 27
muscle, skeletal - physiology (27) 27
protein transport (27) 27
resistance (27) 27
sensitivity (27) 27
insulin-resistance (26) 26
musculoskeletal system (26) 26
translocation (26) 26
health aspects (25) 25
activation (24) 24
muscle contraction - physiology (24) 24
glucose-uptake (23) 23
protein kinases (23) 23
rab gtp-binding proteins - metabolism (23) 23
tbc1d4 (23) 23
akt substrate of 160 kda (22) 22
diabetes (22) 22
signal transduction - drug effects (22) 22
type 2 diabetes (22) 22
amp-activated protein kinase (21) 21
expression (21) 21
glucose transporter type 4 - genetics (21) 21
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160 kda as160 (20) 20
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stimulated glucose-transport (19) 19
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Biochemical Journal, ISSN 0264-6021, 01/2013, Volume 449, Issue 2, pp. 479 - 489
AS160 (Akt substrate of 160 kDa) is a Rab GTPase-activating protein implicated in insulin control of GLUT4 (glucose transporter 4) trafficking. In humans, a... 
Insulin resistance | Muscle | Akt substrate of 160 kDa (AS160) | Glucose transport | Liver | glucose transport | FUSION | liver | STIMULATED GLUT4 TRANSLOCATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | GTPASE-ACTIVATING-PROTEIN | TRAFFICKING | RABGAP AS160 | PLASMA-MEMBRANE | GLUCOSE-TRANSPORTER | muscle | MUTATION | insulin resistance | CONSCIOUS MICE | GTPase-Activating Proteins - deficiency | Glucose Transporter Type 4 - metabolism | Humans | Phosphoenolpyruvate Carboxykinase (GTP) - metabolism | Male | Muscle, Skeletal - metabolism | Adipocytes - drug effects | Insulin - blood | Adipose Tissue - metabolism | Hypoglycemic Agents - blood | Liver - drug effects | Muscle, Skeletal - drug effects | Female | Phosphorylation - drug effects | Insulin - pharmacology | Glucose Tolerance Test | Liver - metabolism | Cells, Cultured | Glycogen Synthase Kinase 3 - metabolism | Blotting, Western | Hypoglycemic Agents - pharmacology | Mice, Knockout | Animals | Adipocytes - metabolism | Glucose - pharmacokinetics | Insulin Resistance - genetics | Glucose - metabolism | Mice | GTPase-Activating Proteins - genetics | Blood Glucose - metabolism | In Vitro Techniques | Adipose Tissue - drug effects | PM, plasma membrane | FBP-1, fructose-1,6-bisphosphatase 1 | GLUT, glucose transporter | RER, respiratory exchange ratio | GSK3, glycogen synthase kinase 3 | PEPCK, phosphoenolpyruvate carboxykinase | EDL, extensor digitorum longus | TA, tibialis anterior | PKB, protein kinase B | MBP, myelin basic protein | Akt substrate of 160 kDa (AS160) | GIR, glucose infusion rate | PCK | GAP, GTPase-activating protein | AS160, Akt substrate of 160 kDa | GAPDH, glyceraldehyde-3-phosphate dehydrogenase
Journal Article
Biochemical Journal, ISSN 0264-6021, 10/2007, Volume 407, Issue 2, pp. 231 - 241
AS 160 (Akt substrate of 160 kDa) mediates insulin-stimulated GLUT4 (glucose transporter 4) translocation, but is widely expressed in insulin-insensitive... 
14-3-3 | Akt/protein kinase B (PKB) | GTPase-activating protein (GAP) | p90 ribosomal S6 kinase (RSK) | Akt substrate of 160 kDa (AS160) | Serum- and glucocorticoid-induced protein kinase (SGK) | MOUSE SKELETAL-MUSCLE | MAMMALIAN TARGET | BIOCHEMISTRY & MOLECULAR BIOLOGY | Akt substrate of 160kDa (AS160) | AKT SUBSTRATE | CELL-GROWTH | GTPASE-ACTIVATING PROTEIN | INSULIN-STIMULATED PHOSPHORYLATION | GLUT4 TRANSLOCATION | S6 KINASE | PROTEOMIC ANALYSIS | RAB-GAP | serum- and glucocorticoid-induced protein kinase (SGK) | Cell Line | Insulin-Like Growth Factor I - pharmacology | Phosphorylation | Humans | GTPase-Activating Proteins - metabolism | Insulin | Amino Acids | Aminoimidazole Carboxamide - pharmacology | Hypoglycemic Agents - pharmacology | 14-3-3 Proteins - metabolism | Ribonucleotides - pharmacology | Aminoimidazole Carboxamide - analogs & derivatives | Protein Binding | Epidermal Growth Factor - pharmacology | Binding Sites | ACC, acetyl-CoA carboxylase | AGC kinase, protein kinase A | AICAR, 5-amino-4-imidazolecarboxamide1-β-D-ribofuranoside | PI3K, phosphoinositide 3-kinase | EGF, epidermal growth factor | TOS motif, mTOR signalling motif | PAS, phospho-Akt substrate | pSer, phosphorylated serine | TSC, tuberous sclerosis complex | AS160, Akt substrate of 160 kDa | PKB, protein kinase B (also known as Akt) | AMPK, AMP-activated protein kinase | RSK, p90 ribosomal S6 kinase | DSP, dithiobis(succinimidyl propionate) | protein kinase C-family | ERK, extracellular-signal-regulated kinase | PDK1, phosphoinositide-dependent kinase 1 | protein kinase B (PKB) | IGF-1, insulin-like growth factor-1 | Akt substrate of 160 kDa (AS160) | GLUT4, glucose transporter 4 | protein kinase G | mTOR, mammalian target of rapamycin | TORC1, mTOR–raptor (regulatory associated protien of mTOR) complex | 4E-BP1, eukaryotic initiation factor 4E-binding protein 1 | GST, glutathione S-transferase | PKC, protein kinase C | PP2A, protein phosphatase 2A | Akt | SGK, serum- and glucocorticoid-induced protein kinase | HA, haemagglutinin | GSV, GLUT4 storage vesicle | p70S6K, p70 S6 kinase | PTB, phosphotyrosine binding domain | pThr, phosphorylated threonine | GAP, GTPase-activating protein | HEK-293, human embryonic kidney-293 | IRAP, insulin-responsive aminopeptidase | Rheb, Ras enriched in brain | MAPK, mitogen-activated protein kinase
Journal Article
Journal Article
FRONTIERS IN MICROBIOLOGY, ISSN 1664-302X, 04/2019, Volume 10, p. 666
Chlamydia trachomatis, an obligate intracellular bacterium, intercepts different trafficking pathways of the host cell to acquire essential lipids for its... 
GAMMA | Rab proteins | AS160 | Rab14 | KINASE | ENDOCYTIC MULTIVESICULAR BODIES | MICROBIOLOGY | Chlamydia trachomatis | AKT SUBSTRATE | Golgi-derived sphingolipids | GTPASE-ACTIVATING PROTEIN | MEDIATED PHAGOCYTOSIS | TRACHOMATIS INCLUSION | GTPase activating proteins | Akt/AS160 signaling pathway | GLUT4 | vesicular transport | Lipids | Health aspects
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2011, Volume 108, Issue 38, pp. 16092 - 16097
AMP-activated protein kinase (AMPK) β1 or β2 subunits are required for assembling of AMPK heterotrimers and are important for regulating enzyme activity and... 
Proteins | Phosphorylation | Mitochondria | Protein synthesis | Treadmills | Muscles | Insulin resistance | Muscle contraction | Insulin | Skeletal muscle | Type 2 diabetes | Obesity | TBC1D1 | PGC1-α | AS160 | Biological Sciences | type 2 diabetes | obesity
Journal Article
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 09/2011, Volume 108, Issue 38, pp. 16092 - 16097
AMP-activated protein kinase (AMPK) beta 1 or beta 2 subunits are required for assembling of AMPK heterotrimers and are important for regulating enzyme... 
MOUSE SKELETAL-MUSCLE | AS160 | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | SENSITIVITY | TBC1D1 | TRANSPORT | type 2 diabetes | CONTRACTION | METABOLISM | INSULIN-RESISTANCE | PGC1-alpha | NITRIC-OXIDE | obesity | SUBUNIT
Journal Article
by Li, Z and Yue, YY and Hu, F and Zhang, C and Ma, XF and Li, N and Qiu, LH and Fu, ML and Chen, LM and Yao, Z and Bilan, PJ and Klip, A and Niu, WY
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM, ISSN 0193-1849, 05/2018, Volume 314, Issue 5, pp. E478 - E493
Electrical pulse stimulation induces GLUT4 glucose transporter translocation in C2C12 myotubes that depends on Rab8A, Rabl3. and Rabl4. Am J Physiol Endocrinol... 
MOUSE SKELETAL-MUSCLE | PHYSIOLOGY | AS160 | ACTIVATED PROTEIN-KINASE | insulin | CA2+ RELEASE | SOLEUS MUSCLE | LIVING MICE | INSULIN SENSITIVITY | AS160 PHOSPHORYLATION | TBC1D1 | TRANSVERSE TUBULES | Rab | CaMKII | ENDOCRINOLOGY & METABOLISM | AMPK | contraction | GLUT4 | skeletal muscle | GLUCOSE-UPTAKE
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 04/2008, Volume 283, Issue 15, pp. 9787 - 9796
The Akt substrate of 160 kDa (AS160) is phosphorylated on Akt substrate (PAS) motifs in response to insulin and contraction in skeletal muscle, regulating... 
AS160 PHOSPHORYLATION | PHOSPHORYLATION ANALYSIS | DOMAIN | GLUT4 TRANSLOCATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | GTPASE-ACTIVATING-PROTEIN | GLUCOSE-TRANSPORT | RABGAP AS160 | AKT SUBSTRATE | BINDING | Glucose Transporter Type 4 - metabolism | Male | Muscle, Skeletal - metabolism | Protein Transport - physiology | Protein Transport - drug effects | GTPase-Activating Proteins - metabolism | Proto-Oncogene Proteins c-akt - genetics | Aminoimidazole Carboxamide - pharmacology | Ribonucleotides - pharmacology | Cyclic AMP-Dependent Protein Kinases - genetics | Muscle Proteins - metabolism | Phosphorylation - drug effects | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-akt - metabolism | Organ Specificity - physiology | Cyclic AMP-Dependent Protein Kinases - metabolism | Insulin - pharmacology | Glucose Transporter Type 4 - genetics | Gene Expression Regulation - physiology | Nuclear Proteins - metabolism | Enzyme Activation - drug effects | Mice, Inbred ICR | Hypoglycemic Agents - pharmacology | Gene Expression Regulation - drug effects | Muscle Proteins - genetics | Animals | Aminoimidazole Carboxamide - analogs & derivatives | Muscle Contraction - drug effects | Adipocytes - metabolism | Muscle Contraction - physiology | Glucose - metabolism | Mice | GTPase-Activating Proteins - genetics | Amino Acid Motifs - genetics | Metabolism and Bioenergetics
Journal Article
Trends in Endocrinology & Metabolism, ISSN 1043-2760, 2015, Volume 26, Issue 8, pp. 422 - 429
Journal Article