Akt/PKB: one kinase, many modifications. (Q38495836)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25997832%20AND%20SRC:MED&resulttype=core&format=json

8 March 2020

review article

1 reference

title

Akt/PKB: one kinase, many modifications (English)

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8 March 2020

2

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8 March 2020

5

Anabella Srebrow

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8 March 2020

1

Guillermo Risso

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8 March 2020

3

Berta Pozzi

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8 March 2020

4

Pablo Mammi

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8 March 2020

language of work or name

English

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publication date

1 June 2015

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8 March 2020

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8 March 2020

volume

468

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8 March 2020

issue

2

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8 March 2020

page(s)

203-214

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Signalling specificity in the Akt pathway in breast cancer

8 March 2020

cites work

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Diverse mechanisms of AKT pathway activation in human malignancy

21 January 2018

1 reference

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Perturbations of the AKT signaling pathway in human cancer

21 January 2018

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Activation of AKT kinases in cancer: implications for therapeutic targeting

21 January 2018

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Akt signalling in health and disease.

21 January 2018

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AKT/PKB signaling: navigating downstream

21 January 2018

1 reference

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The Akt isoforms are present at distinct subcellular locations

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

PI3K-independent AKT activation in cancers: a treasure trove for novel therapeutics

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Structure, regulation and function of PKB/AKT--a major therapeutic target

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The role of SHIP in growth factor induced signalling.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt activation by growth factors is a multiple-step process: the role of the PH domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Protein kinase CK2 phosphorylates and upregulates Akt/PKB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Dephosphorylation and inactivation of Akt/PKB is counteracted by protein kinase CK2 in HEK 293T cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Inactivation of the enzyme GSK3α by the kinase IKKi promotes AKT-mTOR signaling pathway that mediates interleukin-1-induced Th17 cell maintenance

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

New insights into mTOR signaling: mTORC2 and beyond

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

mTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

c-Jun N-terminal kinases mediate reactivation of Akt and cardiomyocyte survival after hypoxic injury in vitro and in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

c-Jun N-terminal kinase (JNK-1) confers protection against brief but not extended ischemia during acute myocardial infarction

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Cell-cycle-regulated activation of Akt kinase by phosphorylation at its carboxyl terminus

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Phosphorylation of Akt at the C-terminal tail triggers Akt activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt is a direct target of the phosphatidylinositol 3-kinase. Activation by growth factors, v-src and v-Ha-ras, in Sf9 and mammalian cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Regulation of Akt/PKB activation by tyrosine phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Deficiency of a beta-arrestin-2 signal complex contributes to insulin resistance.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Protein tyrosine kinase 6 directly phosphorylates AKT and promotes AKT activation in response to epidermal growth factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

IKBKE protein activates Akt independent of phosphatidylinositol 3-kinase/PDK1/mTORC2 and the pleckstrin homology domain to sustain malignant transformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt contributes to activation of the TRIF-dependent signaling pathways of TLRs by interacting with TANK-binding kinase 1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Lysine acetylation targets protein complexes and co-regulates major cellular functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Signal transduction by reactive oxygen species

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Oxidation of Akt2 kinase promotes cell migration and regulates G1-S transition in the cell cycle.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic beta cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Activation of AKT by O-linked N-acetylglucosamine induces vascular calcification in diabetes mellitus

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Recognition and processing of ubiquitin-protein conjugates by the proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Negative Regulation of AKT Activation by BRCA1

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt and CHIP coregulate tau degradation through coordinated interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt phosphorylation at Thr308 and Ser473 is required for CHIP-mediated ubiquitination of the kinase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The E3 ligase TTC3 facilitates ubiquitination and degradation of phosphorylated Akt

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt is negatively regulated by the MULAN E3 ligase

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The E3 ligase TRAF6 regulates Akt ubiquitination and activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The Skp2-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Ubiquitin-dependent regulation of phospho-AKT dynamics by the ubiquitin E3 ligase, NEDD4-1, in the insulin-like growth factor-1 response

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

CYLD negatively regulates transforming growth factor-β-signalling via deubiquitinating Akt

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Concepts in sumoylation: a decade on

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

The HECT family of E3 ubiquitin ligases: multiple players in cancer development

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

RING domain E3 ubiquitin ligases

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt SUMOylation regulates cell proliferation and tumorigenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Modification of Akt by SUMO conjugation regulates alternative splicing and cell cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Uncovering global SUMOylation signaling networks in a site-specific manner

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Nuclear PTEN controls DNA repair and sensitivity to genotoxic stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Regulation of the tumor suppressor PTEN by SUMO.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Sumoylation: a regulatory protein modification in health and disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

A two-dimensional ERK-AKT signaling code for an NGF-triggered cell-fate decision

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt up- and down-regulation in response to endoplasmic reticulum stress.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Akt determines cell fate through inhibition of the PERK-eIF2α phosphorylation pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Modulation of the Akt pathway reveals a novel link with PERK/eIF2α, which is relevant during hypoxia

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Phosphorylation of the translation initiation factor eIF2α at serine 51 determines the cell fate decisions of Akt in response to oxidative stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Patterns of basal signaling heterogeneity can distinguish cellular populations with different drug sensitivities

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

Encoding and decoding cellular information through signaling dynamics

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

SUMO modification of Akt regulates global SUMOylation and substrate SUMOylation specificity through Akt phosphorylation of Ubc9 and SUMO1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20150041

21 January 2018

Identifiers

DOI

10.1042/BJ20150041

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25997832%20AND%20SRC:MED&resulttype=core&format=json

8 March 2020

1 reference