Identification of a form of acyl-CoA:cholesterol acyltransferase specific to liver and intestine in nonhuman primates. - Wikidata - awgldk - TriplyDB

Identification of a form of acyl-CoA:cholesterol acyltransferase specific to liver and intestine in nonhuman primates.

Identification of a form of acyl-CoA:cholesterol acyltransferase specific to liver and intestine in nonhuman primates.

http://www.wikidata.org/entity/Q32012173

about

ACAT-2, a second mammalian acyl-CoA:cholesterol acyltransferase. Its cloning, expression, and characterization Localization of human acyl-coenzyme A: cholesterol acyltransferase-1 (ACAT-1) in macrophages and in various tissues Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) is induced in monocyte-derived macrophages: in vivo and in vitro studies Overexpression of human diacylglycerol acyltransferase 1, acyl-coa:cholesterol acyltransferase 1, or acyl-CoA:cholesterol acyltransferase 2 stimulates secretion of apolipoprotein B-containing lipoproteins in McA-RH7777 cells Human acyl-coenzyme A:cholesterol acyltransferase expressed in chinese hamster ovary cells: membrane topology and active site location Control of ACAT2 liver expression by HNF1 ACAT1 and ACAT2 membrane topology segregates a serine residue essential for activity to opposite sides of the endoplasmic reticulum membrane ACAT2 and human hepatic cholesterol metabolism: identification of important gender-related differences in normolipidemic, non-obese Chinese patients Contribution of Are1p and Are2p to steryl ester synthesis in the yeast Saccharomyces cerevisiae.ACAT1/SOAT1 as a therapeutic target for Alzheimer's disease Human acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) gene organization and evidence that the 4.3-kilobase ACAT-1 mRNA is produced from two different chromosomes Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains Quantitative analysis of the expression of ACAT genes in human tissues by real-time PCR Increased atherosclerosis in LDL receptor-null mice lacking ACAT1 in macrophages Monogenic dyslipidemias: window on determinants of plasma lipoprotein metabolism Upregulation of acyl-CoA: cholesterol acyltransferase in chronic renal failure Cholesterol esterification by ACAT2 is essential for efficient intestinal cholesterol absorption: evidence from thoracic lymph duct cannulation The DGA1 gene determines a second triglyceride synthetic pathway in yeast.Apolipoprotein B-containing lipoproteins in retinal aging and age-related macular degeneration.ACAT1 gene ablation increases 24(S)-hydroxycholesterol content in the brain and ameliorates amyloid pathology in mice with AD.Inhibition of acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) prevents dietary cholesterol-associated steatosis by enhancing hepatic triglyceride mobilization An approach to identify SNPs in the gene encoding acetyl-CoA acetyltransferase-2 (ACAT-2) and their proposed role in metabolic processes in pig.Impact of dietary fat type within the context of altered cholesterol homeostasis on cholesterol and lipoprotein metabolism in the F1B hamster.Transcriptional regulation of the two sterol esterification genes in the yeast Saccharomyces cerevisiae ACAT inhibition and amyloid beta reduction.Absolute stereochemistry of pentacecilides, new inhibitors of lipid droplet formation in mouse macrophages, produced by Penicillium cecidicola FKI-3765-1.Deficiency of acyl CoA:cholesterol acyltransferase 2 prevents atherosclerosis in apolipoprotein E-deficient mice.The enzymes of neutral lipid synthesis.Polymorphism of rs1044925 in the acyl-CoA:cholesterol acyltransferase-1 gene and serum lipid levels in the Guangxi Bai Ku Yao and Han populations.ACAT2 stimulates cholesteryl ester secretion in apoB-containing lipoproteins.Microsomal triglyceride transfer protein enhances cellular cholesteryl esterification by relieving product inhibition.Expression of two isozymes of acyl-coenzyme A: cholesterol acyltransferase-1 and -2 in clear cell type renal cell carcinoma.Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis.Acyl coenzyme A:cholesterol acyltransferase inhibition: potential atherosclerosis therapy or springboard for other discoveries?Sex-specific association of ACAT-1 rs1044925 SNP and serum lipid levels in the hypercholesterolemic subjects Protein mediators of sterol transport across intestinal brush border membrane.Lipid droplet formation on opposing sides of the endoplasmic reticulum Scheduled exercise phase shifts the circadian clock in skeletal muscle.Ezetimibe blocks the internalization of NPC1L1 and cholesterol in mouse small intestine.Human acyl-CoA:cholesterol acyltransferase (ACAT) and its potential as a target for pharmaceutical intervention against atherosclerosis.

P2860

Q22003885-CC5B8EF4-49C7-4409-A3F1-DB818DF4F617 Q22011023-91226183-75BF-4FE1-969D-1B7B7A1252B2 Q24299764-F8C370F1-8AD0-4FE2-B0C5-45B0BDC27004 Q24301076-08684386-C393-4FE6-85A6-5E037E32DF1E Q24305230-F6894BA6-6833-4F16-96B3-510D20F47D98 Q24305410-618C6501-00F9-42DB-8D53-40F2E8038648 Q24550974-E7C8E8D3-E646-4A2E-8DC8-9DBD5641373A Q24649651-00F3CE91-135E-499D-885C-58DAB3872B6B Q27937712-F41DCE2B-BB8B-4241-8ABA-C5C288F58ED0 Q28081654-E75ED791-2758-4D60-91EF-1452EE7189CB Q28140941-495FE81F-3FE9-4D97-BF1F-F68FB12E019A Q28141465-93F48B57-9CA1-4692-9D7E-6F9AD98EF334 Q28239400-3EC6607F-6C3C-4D64-A942-789144EC56F2 Q28346527-86FDCED2-5F65-4F26-BF18-FA691C59C2C1 Q28363810-64D64573-593B-46DB-8338-D2EB815ECA1D Q28564706-883C061A-499A-428C-97B6-35578118A0D9 Q28593758-5ACA9C17-2C53-43C1-9C39-0B70D1E8ADFD Q30667251-E3319CD5-A408-40BE-AC54-50C82274FDE4 Q33634096-47C94BA5-E701-4CF4-9A0A-9F291B3B03B3 Q33733667-1E9EE865-1374-4CA6-A857-A0F6DCE36CFB Q33824907-45AF5A90-8DAC-4FFD-8B04-A2B249298560 Q33933190-8F8432FF-057B-406C-97F5-708A634B507D Q33938794-F55EE810-A8F5-488D-97BE-6FD9A88CFA39 Q33996697-03524C21-3A75-4450-9110-C6F57BA502D9 Q34052308-275C8128-B5D2-4EE0-AB5D-70D8DB25C58C Q34111732-E9BF32B7-B751-4511-AB2F-7894E213EEF6 Q34330253-A811D601-6728-4B6F-8542-42EB7D0E68AD Q34360744-CE378604-690B-4525-9663-3B3C98CA26A9 Q34499464-4F47FC5B-385D-449F-924A-3C78B5DA1A07 Q34619768-7D2C8A4A-46B1-46CA-B3E3-66CAE5B8754C Q34656363-DD6C6DD2-5F71-4648-9C67-5CC7B280D1B4 Q34749380-FDAAC65E-8CDE-4EAE-AA96-F54AC46F5E16 Q34817393-8D663413-EBA2-488A-875E-C5FF4B83415B Q35000994-F7C5AFDA-8232-48C6-B067-195B23A8952C Q35735737-C6BC3435-F0C9-43B1-901C-5F9D1A5EF378 Q35838266-D4B01C16-CEA6-41A4-8650-11E89E150528 Q36145193-1B2C7581-56A2-4DB2-A869-79A28EB1914F Q36149868-1DD6F3BA-61FD-4CD2-9348-3F4000328EB6 Q36213859-61043BA6-881E-42DF-958C-6F380418B082 Q36414556-6418F053-0220-4817-8A99-41B936BEF65E

P2860

Identification of a form of acyl-CoA:cholesterol acyltransferase specific to liver and intestine in nonhuman primates.

http://www.wikidata.org/entity/Q32012173

description

1998 nî lūn-bûn

@nan

1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Identification of a form of ac ...... ntestine in nonhuman primates.

@ast

Identification of a form of ac ...... ntestine in nonhuman primates.

@en

type

label

Identification of a form of ac ...... ntestine in nonhuman primates.

@ast

Identification of a form of ac ...... ntestine in nonhuman primates.

@en

prefLabel

Identification of a form of ac ...... ntestine in nonhuman primates.

@ast

Identification of a form of ac ...... ntestine in nonhuman primates.

@en

P1433

Q32012173-FEC6C63E-1CB8-4811-8CCA-A7132C514F79

P1476

Q32012173-2F1EE7FB-91C2-4FC4-ADED-9EE9B0033632

P2093

Q32012173-45EFDF7D-5F86-4FAF-B3D2-FE01305C5374

Q32012173-9C13BA4E-DE72-45D3-814E-EB0777730809

Q32012173-9DAB3D70-869A-4D75-BB5F-B0415B3B78E5

Q32012173-A0FF1975-90F6-42AA-A956-5B11585B82B5

Q32012173-CAF44C7E-44F4-43FC-8924-06059F0F626C

Q32012173-CB0D4236-09E2-4A80-8A9E-226374AA156A

Q32012173-DAE0A3ED-5C09-4BA3-BA3B-AE796050C148

P2860

Q32012173-0C9572FB-8DAC-49E8-8E4C-96934235065D

Q32012173-0DEEA9A2-A0F4-4366-B1AF-48ADB424F437

Q32012173-180E0745-564D-43B6-B361-851F0783689E

Q32012173-20773501-7EF1-4022-B759-C178C3F3C6B1

Q32012173-2845157D-E1AA-40EB-827C-7D9B0D7B588E

Q32012173-61A447CB-722B-4E8B-895A-C2B7A6EA2326

Q32012173-65806215-34C2-4DF5-9DC7-588834CA2996

Q32012173-84DFDA49-1ADA-44DA-A9F1-C86A5CAB1107

Q32012173-8968F9EA-0800-4744-8C70-564E08804248

Q32012173-963AF5A3-B0C4-4366-8B5F-7AB86E3135AD

P304

Q32012173-0561EAE1-1405-4122-BA96-996D2375D722

P31

Q32012173-03A5EB3D-57AD-4DE6-9AE0-92486108578A

P356

Q32012173-B82880F1-9033-4D01-8A63-2EF5BF857FFC

P407

Q32012173-81B2DB37-6DBB-48BD-8D5D-5B16CA9273A2

P433

Q32012173-2CF5BE53-7C47-4891-8A1A-D648BE98A810

P478

Q32012173-BBA84FEB-121D-4BA2-ADF7-1BAC415F9F4D

P577

Q32012173-7BE51C8A-3433-4EA0-81A1-628EF1B161DA

P5875

Q32012173-7A8BB5BF-5C4F-43AE-ACF0-443701DEC138

P698

Q32012173-00F21526-599A-49B9-962A-2FD4E0062C0F

P356

JBC.273.41.26747

P1433

Journal of Biological Chemistry

P1476

Identification of a form of ac ...... ntestine in nonhuman primates.

@en

P2093

Anderson RA

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

Clark M

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

Davis M

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

Joyce C

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

Reagan JW

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

Rudel LL

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

Shelness GS

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

P2860

An endoplasmic reticulum-specific cyclophilin

A new method for predicting signal sequence cleavage sites

Acyl-coenzyme A:cholesterol acyltransferase

Tissue-specific expression and cholesterol regulation of acylcoenzyme A:cholesterol acyltransferase (ACAT) in mice. Molecular cloning of mouse ACAT cDNA, chromosomal localization, and regulation of ACAT in vivo and in vitro

Prediction of protein secondary structure at better than 70% accuracy

Dietary cholesterol and downregulation of cholesterol 7 alpha-hydroxylase and cholesterol absorption in African green monkeys.

Transmembrane helices predicted at 95% accuracy.

Molecular cloning and characterization of two isoforms of Saccharomyces cerevisiae acyl-CoA:sterol acyltransferase.

Disruption of the acyl-CoA:cholesterol acyltransferase gene in mice: evidence suggesting multiple cholesterol esterification enzymes in mammals.

Regulation of acylcoenzyme A. Cholesterol acyltransferase and 3-hydroxy-3-methylglutaryl coenzyme A reductase activity by lipoproteins in the intestine of parabiont rats

P304

26747-26754

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

P31

scholarly article

P356

10.1074/JBC.273.41.26747

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

P407

P433

41

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

P478

273

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

P577

1998-10-01T00:00:00Z

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

P5875

13528921

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

P698

9756918

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