Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. - Wikidata - awgldk - TriplyDB

Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals.

Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals.

http://www.wikidata.org/entity/Q37185284

about

Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria Autoacetylation of the histone acetyltransferase Rtt109 Regulation of glycolysis and gluconeogenesis by acetylation of PKM and PEPCK Mitochondrial protein acetylation is driven by acetyl-CoA from fatty acid oxidation SIRT3 substrate specificity determined by peptide arrays and machine learning.Mitochondrial DNA sequence variation associated with dementia and cognitive function in the elderly.Comparative proteomic analysis of Streptococcus suis biofilms and planktonic cells that identified biofilm infection-related immunogenic proteins.The biology of lysine acetylation integrates transcriptional programming and metabolism Mitochondrial acetylation and diseases of aging.Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction Mechanistic insights into the regulation of metabolic enzymes by acetylation Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix.Regulation of intermediary metabolism by protein acetylation.NAD and ADP-ribose metabolism in mitochondria.Protein lysine acetylation guards metabolic homeostasis to fight against cancer.Mitochondrial sirtuins as therapeutic targets for age-related disorders.Impact of acetylation on tumor metabolism.The emergence of intracellular metabolite signaling networks.Circadian and Feeding Rhythms Orchestrate the Diurnal Liver Acetylome.Enoyl-CoA hydratase-1 regulates mTOR signaling and apoptosis by sensing nutrients.Reversible lysine acetylation regulates activity of human glycine N-acyltransferase-like 2 (hGLYATL2): implications for production of glycine-conjugated signaling molecules.Urea cycle regulation by mitochondrial sirtuin, SIRT5.Systematic analysis of human lysine acetylation proteins and accurate prediction of human lysine acetylation through bi-relative adapted binomial score Bayes feature representation.Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis.Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS.

P2860

Q21129226-6C09F416-B246-489A-9AF2-5F73663E4DC7 Q24632973-B21A54BA-0386-4741-98E6-34A57C222A1F Q26825322-82E5AC7A-2D1E-482F-82D4-27461ACEBA79 Q28307555-E921F04E-2FBB-4EEB-B5BE-C81BE6A6838B Q33718384-29C23DF8-3B28-4987-9C07-0616D0CD37DF Q34140769-28A512A3-11FA-4225-881D-F0E023AE811F Q34238405-98DDC9B7-3EBC-44B3-B76C-1465B9BC811E Q34692752-4175AF34-7708-4A1D-B4FF-C765CC8F9678 Q34706402-2461C54D-E74C-4C5C-A3DF-274429718F67 Q35003686-D0BA9B5B-278A-4C7A-BA98-340FBA3F444E Q36135254-D7E02F48-5B63-4656-9B93-5405EE57DB1E Q36782178-46C2EE11-DFE7-4347-ADE3-C3079ACFD558 Q37213892-61174FED-F935-4450-98A7-4E39C2D82AAB Q37799059-1F3FCD3F-86A7-4AEB-AE88-71E6AC2C1B38 Q38101602-B98CAA54-1F52-46E5-BFC9-0736ED75ADF5 Q38105878-0103402E-13BE-4E2C-BAEB-B0E4F5C825EC Q38135826-762D3C0A-7A26-4321-88CF-BFEEF53E3409 Q38866711-FE53A148-D228-4B7F-8A8D-41E38A7EDA4C Q38987188-ED80CCB2-78E0-458E-A53A-3E013300E8C3 Q41495726-7A76ED0F-19F7-4BDD-AD29-2061E2C3C8B8 Q41636426-4EEE8AC5-98FF-413D-9F86-5BA0C665D7FB Q42111515-341AD8FF-F9EE-40EB-B249-733613E72BE9 Q42937895-4FE20F7D-BB7F-48F9-9540-7D0843FF2C9C Q43810829-DD2DC4B2-806D-421A-A4E7-CA40859B8BCC Q54613836-D18A6895-CF35-43D0-B0CE-B515DF98FD55 Q55121622-49A3A252-916A-4B15-8040-6A9812F86ADD

P2860

Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals.

http://www.wikidata.org/entity/Q37185284

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 23 March 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Lysine 88 acetylation negative ...... response to nutrient signals.

@en

Lysine 88 acetylation negative ...... response to nutrient signals.

@nl

type

label

Lysine 88 acetylation negative ...... response to nutrient signals.

@en

Lysine 88 acetylation negative ...... response to nutrient signals.

@nl

prefLabel

Lysine 88 acetylation negative ...... response to nutrient signals.

@en

Lysine 88 acetylation negative ...... response to nutrient signals.

@nl

P1433

Q37185284-37D99E07-1733-4CA0-B396-1F763E36121C

P1476

Q37185284-92AD17F5-AB71-47C7-A776-09E55A1820C5

P2093

Q37185284-356D9183-8469-4102-9080-B4AE199CC9B9

Q37185284-3CF4E4E8-2421-47A9-8F9B-0102BAADA116

Q37185284-49B951B5-6C18-49F0-ABB2-669C91F604CF

Q37185284-574A104A-BA89-4D31-A9D9-0B00C08DD025

Q37185284-805AB031-D5EE-47AA-B20B-2861A1471AD9

Q37185284-8099309F-63D2-40B3-BEAC-4F8F560D9039

Q37185284-90EC3038-E624-4A4D-B8C1-8DFE8BC4BC3D

P2860

Q37185284-04265DB3-9EF8-4CDB-B4DB-ED49B5C5D2D2

Q37185284-15ED2DC1-DA15-4E1C-914D-56E16A0C92A9

Q37185284-2952A81A-CB7B-4809-BA96-CA58AF4C47F3

Q37185284-2EE2BB67-8E11-4CA9-B82A-2E00F82F1278

Q37185284-43AD9F0C-AB39-45A7-AEC9-5056EF3340E0

Q37185284-448B7B09-3520-4ECC-93B6-341350B678C2

Q37185284-4CBAFFF7-CB02-4A5E-86D4-2BED0C27944E

Q37185284-61EE8671-7E6E-4C1D-BDE0-57902F82F522

Q37185284-71D1ED3E-BAE0-4E33-B539-5D1782C6C6EE

Q37185284-7C11EEB4-2A69-4460-814E-695F73B3DADC

P304

Q37185284-68D196F0-B0BC-4868-A6FB-49D35B0C9D5C

P31

Q37185284-7D966921-1C19-4DA7-BCE4-6A204631EA6D

P356

Q37185284-8E349B3A-2642-4261-AF94-97BDF8EF0C61

P407

Q37185284-2C373134-4226-44D9-B183-5EF05CB92FF5

P433

Q37185284-5A54B3BC-B6FA-40D6-8DF0-4058FE3FBB25

P478

Q37185284-C526F784-33BD-4D4C-A8A8-9D1852AE4125

P50

Q37185284-B8CEC515-FCD5-42FF-A88E-B7A3A74A75E1

P577

Q37185284-076229BE-4222-4C73-8E90-F2EEB8035F48

P698

Q37185284-703ED9C0-69AE-486D-B669-EE3C55F082D6

P932

Q37185284-44C5C16A-352D-4832-82CF-C0B64461EF3F

P356

P1433

Journal of Biological Chemistry

P1476

Lysine 88 acetylation negative ...... n response to nutrient signals

@en

P2093

Jun Yao

http://www.w3.org/2001/XMLSchema#string

Kun-Liang Guan

http://www.w3.org/2001/XMLSchema#string

Shimin Zhao

http://www.w3.org/2001/XMLSchema#string

Wei Huang

http://www.w3.org/2001/XMLSchema#string

Wei Yu

http://www.w3.org/2001/XMLSchema#string

Yan Lin

http://www.w3.org/2001/XMLSchema#string

Yue Xiong

http://www.w3.org/2001/XMLSchema#string

P2860

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

Acetylation is indispensable for p53 activation

A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A

SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS

Human ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changes

Substrate-induced conformational change in a trimeric ornithine transcarbamoylase

1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiency

Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

P304

13669-13675

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M901921200

http://www.w3.org/2001/XMLSchema#string

P407

P433

20

http://www.w3.org/2001/XMLSchema#string

P478

284

http://www.w3.org/2001/XMLSchema#string

P50

P577

2009-03-23T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

19318352

http://www.w3.org/2001/XMLSchema#string

P932

2679468

http://www.w3.org/2001/XMLSchema#string