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acetylleucyl-leucyl-norleucinal and Cancer of Liver

acetylleucyl-leucyl-norleucinal has been researched along with Cancer of Liver in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (50.00)18.2507
2000's2 (33.33)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Harada, M; Honma, Y; Shimizu, S; Takehara, T1
Domitrovich, AM; Felmlee, DJ; Siddiqui, A1
Cheng, J; Fujimoto, T; Fujita, A; Ohsaki, Y; Tokumoto, T1
Endo, A; Honda, M; Itakura, H; Kawabe, Y; Kodama, T; Matsumoto, A; Shimokawa, T; Wada, Y; Yazaki, Y1
Ingram, MF; Shelness, GS1
Adeli, K; Macri, J1

Other Studies

6 other study(ies) available for acetylleucyl-leucyl-norleucinal and Cancer of Liver

ArticleYear
Sorafenib enhances proteasome inhibitor-induced cell death via inactivation of Akt and stress-activated protein kinases.
    Journal of gastroenterology, 2014, Volume: 49, Issue:3

    Topics: Antineoplastic Agents; Apoptosis; Carcinoma, Hepatocellular; Cell Death; Cell Line, Tumor; Down-Regulation; Drug Synergism; Humans; Leupeptins; Liver Neoplasms; Molecular Targeted Therapy; Niacinamide; Oligopeptides; Phenylurea Compounds; Proteasome Inhibitors; Protein Kinase Inhibitors; Protein Kinases; Proto-Oncogene Proteins c-akt; Signal Transduction; Sorafenib

2014
Hepatitis C virus nonstructural proteins inhibit apolipoprotein B100 secretion.
    The Journal of biological chemistry, 2005, Dec-02, Volume: 280, Issue:48

    Topics: Apolipoprotein B-100; Apolipoproteins B; Carcinoma, Hepatocellular; Carrier Proteins; Cell Line, Tumor; Cysteine Proteinase Inhibitors; Genes, Reporter; Genome, Viral; Hepacivirus; Humans; Immunoprecipitation; Leupeptins; Lipids; Liver; Liver Neoplasms; Oleic Acid; Plasmids; Promoter Regions, Genetic; Protein Binding; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Time Factors; Transcription, Genetic; Transfection; Triglycerides; Viral Nonstructural Proteins

2005
Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B.
    Molecular biology of the cell, 2006, Volume: 17, Issue:6

    Topics: Apolipoproteins B; Autophagy; Carcinoma, Hepatocellular; Cell Line, Tumor; Cysteine Proteinase Inhibitors; Cytoplasm; Humans; Leupeptins; Lipids; Lipoproteins, VLDL; Liver Neoplasms; Proteasome Endopeptidase Complex

2006
The molecular mechanism of the induction of the low density lipoprotein receptor by chenodeoxycholic acid in cultured human cells.
    Biochemical and biophysical research communications, 1995, Mar-08, Volume: 208, Issue:1

    Topics: Alkyl and Aryl Transferases; Base Sequence; Cell Line; Chenodeoxycholic Acid; Codon; DNA-Binding Proteins; Farnesyl-Diphosphate Farnesyltransferase; Gene Expression; Geranyltranstransferase; Hepatoblastoma; Humans; Hydroxycholesterols; Hydroxymethylglutaryl CoA Reductases; Hydroxymethylglutaryl-CoA Synthase; Leupeptins; Liver Neoplasms; Phosphotransferases (Alcohol Group Acceptor); Protease Inhibitors; Receptors, LDL; Regulatory Sequences, Nucleic Acid; RNA, Messenger; Transferases; Tumor Cells, Cultured

1995
Apolipoprotein B-100 destined for lipoprotein assembly and intracellular degradation undergoes efficient translocation across the endoplasmic reticulum membrane.
    Journal of lipid research, 1996, Volume: 37, Issue:10

    Topics: Apolipoprotein B-100; Apolipoprotein B-48; Apolipoproteins B; Biological Transport; Carcinoma, Hepatocellular; Endoplasmic Reticulum; Humans; Immunoblotting; Intracellular Membranes; Leupeptins; Lipoproteins; Liver; Liver Neoplasms; Protease Inhibitors; Trypsin; Tumor Cells, Cultured

1996
Conformational changes in apolipoprotein B modulate intracellular assembly and degradation of ApoB-containing lipoprotein particles in HepG2 cells.
    Arteriosclerosis, thrombosis, and vascular biology, 1997, Volume: 17, Issue:11

    Topics: Animals; Apolipoprotein B-100; Apolipoproteins B; Carcinoma, Hepatocellular; Cystine; Dithiothreitol; Glycosylation; Humans; Leupeptins; Lipoproteins; Lipoproteins, HDL; Lipoproteins, LDL; Lipoproteins, VLDL; Liver; Liver Neoplasms; Microsomes, Liver; Molecular Weight; Neoplasm Proteins; Protease Inhibitors; Protein Conformation; Protein Denaturation; Protein Folding; Protein Processing, Post-Translational; Sulfhydryl Reagents; Tumor Cells, Cultured; Tunicamycin

1997