lysyl-aspartyl-glutamyl-leucine and oleic acid

lysyl-aspartyl-glutamyl-leucine has been researched along with oleic acid in 2 studies

Compound Research Comparison

Studies (lysyl-aspartyl-glutamyl-leucine)	Trials (lysyl-aspartyl-glutamyl-leucine)	Recent Studies (post-2010) (lysyl-aspartyl-glutamyl-leucine)	Studies (oleic acid)	Trials (oleic acid)	Recent Studies (post-2010) (oleic acid)
121	0	22	8,768	248	3,051

Protein Interaction Comparison

Protein	Taxonomy	lysyl-aspartyl-glutamyl-leucine (IC50)	oleic acid (IC50)
Tyrosine-protein phosphatase non-receptor type 1	Homo sapiens (human)		6.2

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Grundy, SM; Patel, SB	1
Alam, M; Gao, W; Gilham, D; Lehner, R; Vance, DE	1

Other Studies

2 other study(ies) available for lysyl-aspartyl-glutamyl-leucine and oleic acid

Article	Year
Interactions between microsomal triglyceride transfer protein and apolipoprotein B within the endoplasmic reticulum in a heterologous expression system. The Journal of biological chemistry, 1996, Aug-02, Volume: 271, Issue:31 Topics: Amino Acid Sequence; Animals; Apolipoproteins B; Calcium-Binding Proteins; Calnexin; Carrier Proteins; Cell Line; Cholesterol Ester Transfer Proteins; Endoplasmic Reticulum; Glycoproteins; Humans; Lipids; Microsomes; Molecular Sequence Data; Molecular Structure; Oleic Acid; Oleic Acids; Oligopeptides; Peptide Fragments; Protein Sorting Signals; Recombinant Proteins; Tunicamycin	1996
Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates. Molecular biology of the cell, 2005, Volume: 16, Issue:2 Topics: Animals; Cell Line, Tumor; Centrifugation, Density Gradient; Chlorocebus aethiops; COS Cells; Endoplasmic Reticulum; Fluorescein; Fluorescent Dyes; Gene Deletion; Hydrazines; Hydrolysis; Lipase; Lipoproteins; Lipoproteins, VLDL; Liver Neoplasms, Experimental; Microscopy, Confocal; Oleic Acid; Oligopeptides; Protein Sorting Signals; Rats; Substrate Specificity; Transfection; Tritium; Xanthenes	2005

Article

Year

Interactions between microsomal triglyceride transfer protein and apolipoprotein B within the endoplasmic reticulum in a heterologous expression system.

The Journal of biological chemistry, 1996, Aug-02, Volume: 271, Issue:31

Topics: Amino Acid Sequence; Animals; Apolipoproteins B; Calcium-Binding Proteins; Calnexin; Carrier Proteins; Cell Line; Cholesterol Ester Transfer Proteins; Endoplasmic Reticulum; Glycoproteins; Humans; Lipids; Microsomes; Molecular Sequence Data; Molecular Structure; Oleic Acid; Oleic Acids; Oligopeptides; Peptide Fragments; Protein Sorting Signals; Recombinant Proteins; Tunicamycin

1996

Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates.

Molecular biology of the cell, 2005, Volume: 16, Issue:2

Topics: Animals; Cell Line, Tumor; Centrifugation, Density Gradient; Chlorocebus aethiops; COS Cells; Endoplasmic Reticulum; Fluorescein; Fluorescent Dyes; Gene Deletion; Hydrazines; Hydrolysis; Lipase; Lipoproteins; Lipoproteins, VLDL; Liver Neoplasms, Experimental; Microscopy, Confocal; Oleic Acid; Oligopeptides; Protein Sorting Signals; Rats; Substrate Specificity; Transfection; Tritium; Xanthenes

2005