Base de dados : MEDLINE
Pesquisa : D08.811.913.050.134.415 [Categoria DeCS]
Referências encontradas : 12 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 2 ir para página        

  1 / 12 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28426192
[Au] Autor:Han Z; Chou CW; Yang X; Bartlett MG; Zheng YG
[Ad] Endereço:Department of Pharmaceutical and Biomedical Sciences and Department of Chemistry, University of Georgia , Athens, Georgia 30602, United States.
[Ti] Título:Profiling Cellular Substrates of Lysine Acetyltransferases GCN5 and p300 with Orthogonal Labeling and Click Chemistry.
[So] Source:ACS Chem Biol;12(6):1547-1555, 2017 Jun 16.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:p300 and GCN5 are two representative lysine acetyltransferases (KATs) in mammalian cells. It was recently reported that they possess multiple acyltransferase activities including acetylation, propionylation, and butyrylation of the ε-amino group of lysine residues of histones and non-histone protein substrates. Although thousands of acetylated substrates and acetylation sites have been identified by mass spectrometry-based proteomic screening, our knowledge about the causative connections between individual KAT members and their corresponding sub-acylomes remain very limited. Herein, we applied 3-azidopropionyl CoA (3AZ-CoA) as a bioorthogonal surrogate of acetyl-, propionyl- and butyryl-CoA for KAT substrate identification. We successfully attached the azide as a chemical warhead to cellular substrates of wild-type p300 and engineered GCN5. The substrates were subsequently labeled with biotin tag through the copper-catalyzed azide-alkyne cycloaddition (CuAAC). Following protein enrichment on streptavidin-coated resin, we conducted LC-MS/MS studies from which more than four hundred proteins were identified as GCN5 or p300 substrate candidates. These proteins are either p300- or GCN5-unique or shared by the two KATs and are extensively involved in various biological events including gene expression, cell cycle, and cellular metabolism. We also experimentally validated two novel substrates of GCN5, that is, IQGAP1 and SMC1. These results demonstrate extensive engagement of GCN5 and p300 in cellular pathways and provide new insights into understanding their functions in specific biological processes.
[Mh] Termos MeSH primário: Proteína p300 Associada a E1A/metabolismo
Lisina Acetiltransferases/metabolismo
Fatores de Transcrição de p300-CBP/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias
Biotina/análogos & derivados
Cromatografia Líquida
Química Click
Seres Humanos
Ligantes
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Ligands); 0 (biotin-streptavidin complex); 6SO6U10H04 (Biotin); EC 2.3.1.32 (Lysine Acetyltransferases); EC 2.3.1.48 (E1A-Associated p300 Protein); EC 2.3.1.48 (EP300 protein, human); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00114


  2 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28161493
[Au] Autor:Tapias A; Wang ZQ
[Ad] Endereço:Leibniz Institute on Aging-Fritz Lipmann Institute (FLI), 07745 Jena, Germany.
[Ti] Título:Lysine Acetylation and Deacetylation in Brain Development and Neuropathies.
[So] Source:Genomics Proteomics Bioinformatics;15(1):19-36, 2017 Feb.
[Is] ISSN:2210-3244
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Embryonic development is critical for the final functionality and maintenance of the adult brain. Brain development is tightly regulated by intracellular and extracellular signaling. Lysine acetylation and deacetylation are posttranslational modifications that are able to link extracellular signals to intracellular responses. A wealth of evidence indicates that lysine acetylation and deacetylation are critical for brain development and functionality. Indeed, mutations of the enzymes and cofactors responsible for these processes are often associated with neurodevelopmental and psychiatric disorders. Lysine acetylation and deacetylation are involved in all levels of brain development, starting from neuroprogenitor survival and proliferation, cell fate decisions, neuronal maturation, migration, and synaptogenesis, as well as differentiation and maturation of astrocytes and oligodendrocytes, to the establishment of neuronal circuits. Hence, fluctuations in the balance between lysine acetylation and deacetylation contribute to the final shape and performance of the brain. In this review, we summarize the current basic knowledge on the specific roles of lysine acetyltransferase (KAT) and lysine deacetylase (KDAC) complexes in brain development and the different neurodevelopmental disorders that are associated with dysfunctional lysine (de)acetylation machineries.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Lisina/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Encéfalo/crescimento & desenvolvimento
Carboxiliases/metabolismo
Montagem e Desmontagem da Cromatina
Seres Humanos
Lisina Acetiltransferases/metabolismo
Células-Tronco Neurais/citologia
Células-Tronco Neurais/metabolismo
Transtornos do Neurodesenvolvimento/metabolismo
Transtornos do Neurodesenvolvimento/patologia
Neurogênese
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 2.3.1.32 (Lysine Acetyltransferases); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.18 (lysine decarboxylase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170206
[St] Status:MEDLINE


  3 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28150880
[Au] Autor:Pelletier N; Grégoire S; Yang XJ
[Ad] Endereço:Goodman Cancer Research Center and Department of Medicine, McGill University, Montreal, Quebec, Canada.
[Ti] Título:Assays for Acetylation and Other Acylations of Lysine Residues.
[So] Source:Curr Protoc Protein Sci;87:14.11.1-14.11.18, 2017 Feb 02.
[Is] ISSN:1934-3663
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysine acetylation refers to addition of an acetyl moiety to the epsilon-amino group of a lysine residue and is important for regulating protein functions in various organisms from bacteria to humans. This is a reversible and precisely controlled covalent modification that either serves as an on/off switch or participates in a codified manner with other post-translational modifications to regulate different cellular and developmental processes in normal and pathological states. This unit describes methods for in vitro and in vivo determination of lysine acetylation. Such methods can be easily extended for analysis of other acylations (such as propionylation, butyrylation, crotonylation, and succinylation) that are also present in histones and many other proteins. © 2017 by John Wiley & Sons, Inc.
[Mh] Termos MeSH primário: Lisina/química
Processamento de Proteína Pós-Traducional
Proteínas/química
[Mh] Termos MeSH secundário: Acetilação
Acilação
Animais
Anticorpos/imunologia
Eletroforese em Gel de Poliacrilamida
Células HEK293
Histona Acetiltransferases/química
Histona Acetiltransferases/metabolismo
Histonas/química
Seres Humanos
Lisina Acetiltransferases/química
Lisina Acetiltransferases/metabolismo
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Histones); 0 (Proteins); EC 2.3.1.32 (Lysine Acetyltransferases); EC 2.3.1.48 (Histone Acetyltransferases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170530
[Lr] Data última revisão:
170530
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170203
[St] Status:MEDLINE
[do] DOI:10.1002/cpps.26


  4 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28141495
[Au] Autor:Samanta S; Singh A; Biswas P; Bhatt A; Visweswariah SS
[Ad] Endereço:1​Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore, India †â€‹Present address: Indian Institute of Information Technology, Allahabad, India.
[Ti] Título:Mycobacterial phenolic glycolipid synthesis is regulated by cAMP-dependent lysine acylation of FadD22.
[So] Source:Microbiology;163(3):373-382, 2017 Mar.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mycobacterial cell envelope is unique in its chemical composition, and has an important role to play in pathogenesis. Phthiocerol dimycocerosates (PDIMs) and glycosylated phenolphthiocerol dimycocerosates, also known as phenolic glycolipids (PGLs), contribute significantly to the virulence of Mycobacterium tuberculosis. FadD22 is essential for PGL biosynthesis. We have recently shown in vitro that FadD22 is a substrate for lysine acylation by a unique cAMP-dependent, protein lysine acyltransferase found only in mycobacteria. The lysine residue that is acylated is at the active site of FadD22. Therefore, acylation is likely to inhibit FadD22 activity and reduce PGL biosynthesis. Here, we show accumulation of PGLs in a strain of M. bovis BCG deleted for the gene encoding the cAMP-dependent acyltransferase, katbcg, with no change seen in PDIM synthesis. Complementation using KATbcg mutants that are deficient in cAMP-binding or acyltransferase activity shows that PGL accumulation is regulated by cAMP-dependent protein acylation in vivo. Expression of FadD22 and KATbcg mutants in Mycobacterium smegmatis confirmed that FadD22 is a substrate for lysine acylation by KATbcg. We have therefore described a mechanism by which cAMP can regulate mycobacterial virulence as a result of the ability of this second messenger to modulate critical cell wall components that affect the host immune response.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Glicolipídeos/biossíntese
Ligases/metabolismo
Lisina Acetiltransferases/metabolismo
Mycobacterium bovis/genética
Mycobacterium smegmatis/genética
Mycobacterium tuberculosis/patogenicidade
[Mh] Termos MeSH secundário: Acilação
Antígenos de Bactérias/biossíntese
Membrana Celular/metabolismo
Parede Celular/metabolismo
AMP Cíclico/metabolismo
Lisina/metabolismo
Lisina Acetiltransferases/genética
Mycobacterium bovis/metabolismo
Mycobacterium smegmatis/metabolismo
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/metabolismo
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Glycolipids); 0 (Virulence Factors); E0399OZS9N (Cyclic AMP); EC 2.3.1.32 (Lysine Acetyltransferases); EC 6.- (Ligases); EC 6.5.- (FadD22 protein, Mycobacterium tuberculosis); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.000440


  5 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27983866
[Au] Autor:Oh TG; Wang SM; Muscat GE
[Ad] Endereço:Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
[Ti] Título:Therapeutic Implications of Epigenetic Signaling in Breast Cancer.
[So] Source:Endocrinology;158(3):431-447, 2017 03 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Breast cancer is a heterogeneous disease and its complexity has hindered the development of efficacious treatments targeting all breast cancer subtypes. Many studies have linked the diversity of breast carcinogenesis and metastasis to aberrant epigenetic signaling and control. Here, we focus on the current state of the discipline and review the major epigenetic enzymes controlling chromatin structure and function in the context of breast cancer, including (1) DNA methyltransferases, (2) lysine methyltransferases and demethylases, (3) protein arginine methyltransferases, and (4) histone acetyltransferases and deacetylases. Moreover, therapeutic drugs targeting these epigenetic enzymes are rapidly emerging and/or undergoing clinical trials. Therefore, we discuss the pharmacological manipulation of epigenetic enzymes for breast cancer treatment and present new clinical and survival outcome analysis on epigenetic factors that have evaded analysis to date. Understanding and pharmacologically exploiting epigenetic regulation in breast cancer promises to be an essential aspect of next-generation drug development and adjuvant therapies targeting advanced disease and treatment-resistant tumors.
[Mh] Termos MeSH primário: Neoplasias da Mama/enzimologia
Neoplasias da Mama/genética
Epigênese Genética
[Mh] Termos MeSH secundário: Animais
Carcinogênese
Metilases de Modificação do DNA/metabolismo
Feminino
Histona Desacetilases/metabolismo
Histona Desmetilases/metabolismo
Seres Humanos
Lisina Acetiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 1.14.11.- (Histone Demethylases); EC 2.1.1.- (DNA Modification Methylases); EC 2.3.1.32 (Lysine Acetyltransferases); EC 3.5.1.98 (Histone Deacetylases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170708
[Lr] Data última revisão:
170708
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE
[do] DOI:10.1210/en.2016-1716


  6 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27720985
[Au] Autor:Hirsch CL; Wrana JL; Dent SYR
[Ad] Endereço:Center for Systems Biology, Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto M5G 1X5, Canada. Electronic address: hirsch@lunenfeld.ca.
[Ti] Título:KATapulting toward Pluripotency and Cancer.
[So] Source:J Mol Biol;429(13):1958-1977, 2017 Jun 30.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Development is generally regarded as a unidirectional process that results in the acquisition of specialized cell fates. During this process, cellular identity is precisely defined by signaling cues that tailor the chromatin landscape for cell-specific gene expression programs. Once established, these pathways and cell states are typically resistant to disruption. However, loss of cell identity occurs during tumor initiation and upon injury response. Moreover, terminally differentiated cells can be experimentally provoked to become pluripotent. Chromatin reorganization is key to the establishment of new gene expression signatures and thus new cell identity. Here, we explore an emerging concept that lysine acetyltransferase (KAT) enzymes drive cellular plasticity in the context of somatic cell reprogramming and tumorigenesis.
[Mh] Termos MeSH primário: Diferenciação Celular
Cromatina/metabolismo
Regulação da Expressão Gênica
Neoplasias/fisiopatologia
[Mh] Termos MeSH secundário: Animais
Carcinogênese
Proliferação Celular
Seres Humanos
Lisina Acetiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin); EC 2.3.1.32 (Lysine Acetyltransferases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161011
[St] Status:MEDLINE


  7 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27566542
[Au] Autor:Vergnolle O; Xu H; Tufariello JM; Favrot L; Malek AA; Jacobs WR; Blanchard JS
[Ad] Endereço:From the Department of Biochemistry and.
[Ti] Título:Post-translational Acetylation of MbtA Modulates Mycobacterial Siderophore Biosynthesis.
[So] Source:J Biol Chem;291(42):22315-22326, 2016 Oct 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Iron is an essential element for life, but its soluble form is scarce in the environment and is rarer in the human body. Mtb (Mycobacterium tuberculosis) produces two aryl-capped siderophores, mycobactin (MBT) and carboxymycobactin (cMBT), to chelate intracellular iron. The adenylating enzyme MbtA catalyzes the first step of mycobactin biosynthesis in two half-reactions: activation of the salicylic acid as an acyl-adenylate and ligation onto the acyl carrier protein (ACP) domain of MbtB to form covalently salicylated MbtB-ACP. We report the first apo-MbtA structure from Mycobacterium smegmatis at 2.3 Å. We demonstrate here that MbtA activity can be reversibly, post-translationally regulated by acetylation. Indeed the mycobacterial Pat (protein lysine acetyltransferase), Rv0998, specifically acetylates MbtA on lysine 546, in a cAMP-dependent manner, leading to enzyme inhibition. MbtA acetylation can be reversed by the NAD -dependent DAc (deacetyltransferase), Rv1151c. Deletion of Pat and DAc genes in Mtb revealed distinct phenotypes for strains lacking one or the other gene at low pH and limiting iron conditions. This study establishes a direct connection between the reversible acetylation system Pat/DAc and the ability of Mtb to adapt in limited iron conditions, which is critical for mycobacterial infection.
[Mh] Termos MeSH primário: Ligases/metabolismo
Mycobacterium tuberculosis/enzimologia
Oxazóis/metabolismo
Processamento de Proteína Pós-Traducional/fisiologia
Sideróforos/biossíntese
[Mh] Termos MeSH secundário: Acetilação
Catálise
Seres Humanos
Ligases/genética
Lisina Acetiltransferases/genética
Lisina Acetiltransferases/metabolismo
Mycobacterium tuberculosis/genética
Domínios Proteicos
Sideróforos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oxazoles); 0 (Siderophores); 0 (mycobactins); EC 2.3.1.32 (Lysine Acetyltransferases); EC 6.- (Ligases); EC 6.- (salicyl-AMP ligase, Mycobacterium tuberculosis)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171014
[Lr] Data última revisão:
171014
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160828
[St] Status:MEDLINE


  8 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27423859
[Au] Autor:Montgomery DC; Meier JL
[Ad] Endereço:Chemical Biology Laboratory, National Cancer Institute, Frederick, MD, United States.
[Ti] Título:Mapping Lysine Acetyltransferase-Ligand Interactions by Activity-Based Capture.
[So] Source:Methods Enzymol;574:105-23, 2016.
[Is] ISSN:1557-7988
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Changes in reversible protein acetylation mediate many key aspects of genomic regulation and enzyme function. The catalysts for this posttranslational modification, lysine acetyltransferases (KATs), have been difficult targets for characterization due to their complex architecture and challenging reconstitution. To address this challenge, here we describe methods to profile endogenous KAT activities using activity-based probes. This method facilitates the targeted analysis of several cellular KATs and can be used to study their interactions with many different types of ligands, including acyl-CoA metabolites. This competitive activity-based capture approach provides a method to assess the selectivity of ligands for different KAT families in complex proteomic settings, and thus has the potential to offer substantial insights into the regulation of cellular KAT function.
[Mh] Termos MeSH primário: Ensaios Enzimáticos/métodos
Lisina Acetiltransferases/metabolismo
Proteômica/métodos
[Mh] Termos MeSH secundário: Acetilação
Acil Coenzima A/metabolismo
Animais
Histonas/metabolismo
Seres Humanos
Ligantes
Lisina Acetiltransferases/análise
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Histones); 0 (Ligands); EC 2.3.1.32 (Lysine Acetyltransferases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160718
[St] Status:MEDLINE


  9 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27143356
[Au] Autor:Shi S; Liu K; Chen Y; Zhang S; Lin J; Gong C; Jin Q; Yang XJ; Chen R; Ji Z; Han A
[Ad] Endereço:From the State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiang'an, Xiamen 361102, China and.
[Ti] Título:Competitive Inhibition of Lysine Acetyltransferase 2B by a Small Motif of the Adenoviral Oncoprotein E1A.
[So] Source:J Biol Chem;291(27):14363-72, 2016 Jul 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The adenovirus early region 1A (E1A) oncoprotein hijacks host cells via direct interactions with many key cellular proteins, such as KAT2B, also known as PCAF (p300/CBP associated factor). E1A binds the histone acetyltransferase (HAT) domain of KAT2B to repress its transcriptional activation. However, the molecular mechanism by which E1A inhibits the HAT activity is not known. Here we demonstrate that a short and relatively conserved N-terminal motif (cNM) in the intrinsically disordered E1A protein is crucial for KAT2B interaction, and inhibits its HAT activity through a direct competition with acetyl-CoA, but not its substrate histone H3. Molecular modeling together with a series of mutagenesis experiments suggests that the major helix of E1A cNM binds to a surface of the acetyl-CoA pocket of the KAT2B HAT domain. Moreover, transient expression of the cNM peptide is sufficient to inhibit KAT2B-specific H3 acetylation H3K14ac in vivo Together, our data define an essential motif cNM in N-terminal E1A as an acetyl-CoA entry blocker that directly associates with the entrance of acetyl-CoA binding pocket to block the HAT domain access to its cofactor.
[Mh] Termos MeSH primário: Proteínas E1A de Adenovirus/fisiologia
Lisina Acetiltransferases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Acetilação
Proteínas E1A de Adenovirus/química
Motivos de Aminoácidos
Sequência de Aminoácidos
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Cinética
Modelos Moleculares
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenovirus E1A Proteins); EC 2.3.1.32 (Lysine Acetyltransferases)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160505
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.697300


  10 / 12 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26808162
[Au] Autor:Kaypee S; Sudarshan D; Shanmugam MK; Mukherjee D; Sethi G; Kundu TK
[Ad] Endereço:Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore, Karnataka, India.
[Ti] Título:Aberrant lysine acetylation in tumorigenesis: Implications in the development of therapeutics.
[So] Source:Pharmacol Ther;162:98-119, 2016 06.
[Is] ISSN:1879-016X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The 'language' of covalent histone modifications translates environmental and cellular cues into gene expression. This vast array of post-translational modifications on histones are more than just covalent moieties added onto a protein, as they also form a platform on which crucial cellular signals are relayed. The reversible lysine acetylation has emerged as an important post-translational modification of both histone and non-histone proteins, dictating numerous epigenetic programs within a cell. Thus, understanding the complex biology of lysine acetylation and its regulators is essential for the development of epigenetic therapeutics. In this review, we will attempt to address the complexities of lysine acetylation in the context of tumorigenesis, their role in cancer progression and emphasize on the modalities developed to target lysine acetyltransferases towards cancer treatment.
[Mh] Termos MeSH primário: Lisina Acetiltransferases/metabolismo
Lisina/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Antineoplásicos/farmacologia
Carcinogênese/metabolismo
Seres Humanos
Neoplasias/tratamento farmacológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); EC 2.3.1.32 (Lysine Acetyltransferases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170317
[Lr] Data última revisão:
170317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160126
[St] Status:MEDLINE



página 1 de 2 ir para página        
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde