| D007887 |
Fabaceae |
The large family of plants characterized by pods. Some are edible and some cause LATHYRISM or FAVISM and other forms of poisoning. Other species yield useful materials like gums from ACACIA and various LECTINS like PHYTOHEMAGGLUTININS from PHASEOLUS. Many of them harbor NITROGEN FIXATION bacteria on their roots. Many but not all species of "beans" belong to this family. |
Afzelia,Amorpha,Andira,Baptisia,Callerya,Ceratonia,Clathrotropis,Colophospermum,Copaifera,Delonix,Euchresta,Guibourtia,Legumes,Machaerium,Pithecolobium,Stryphnodendron,Leguminosae,Pea Family,Pithecellobium,Tachigalia,Families, Pea,Family, Pea,Legume,Pea Families |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D012639 |
Seeds |
The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield. |
Diaspores,Elaiosomes,Embryos, Plant,Plant Embryos,Plant Zygotes,Zygotes, Plant,Diaspore,Elaiosome,Embryo, Plant,Plant Embryo,Plant Zygote,Seed,Zygote, Plant |
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| D014315 |
Triterpenes |
A class of terpenes (the general formula C30H48) formed by the condensation of six isoprene units, equivalent to three terpene units. |
Triterpene,Triterpenoid,Triterpenoids |
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| D015854 |
Up-Regulation |
A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins. |
Receptor Up-Regulation,Upregulation,Up-Regulation (Physiology),Up Regulation |
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| D017209 |
Apoptosis |
A regulated cell death mechanism characterized by distinctive morphologic changes in the nucleus and cytoplasm, including the endonucleolytic cleavage of genomic DNA, at regularly spaced, internucleosomal sites, i.e., DNA FRAGMENTATION. It is genetically programmed and serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth. |
Apoptosis, Extrinsic Pathway,Apoptosis, Intrinsic Pathway,Caspase-Dependent Apoptosis,Classic Apoptosis,Classical Apoptosis,Programmed Cell Death,Programmed Cell Death, Type I,Apoptoses, Extrinsic Pathway,Apoptoses, Intrinsic Pathway,Apoptosis, Caspase-Dependent,Apoptosis, Classic,Apoptosis, Classical,Caspase Dependent Apoptosis,Cell Death, Programmed,Classic Apoptoses,Extrinsic Pathway Apoptoses,Extrinsic Pathway Apoptosis,Intrinsic Pathway Apoptoses,Intrinsic Pathway Apoptosis |
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| D045325 |
HCT116 Cells |
Human COLORECTAL CARCINOMA cell line. |
HCT 116 Cells,HCT-116 Cells,Cell, HCT 116,Cell, HCT-116,Cell, HCT116,Cells, HCT 116,Cells, HCT-116,Cells, HCT116,HCT 116 Cell,HCT-116 Cell,HCT116 Cell |
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| D053148 |
Caspase 3 |
A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA. |
CASP3,Apopain,Caspase-3,Pro-Caspase-3,Procaspase-3,Pro Caspase 3,Procaspase 3 |
|
| D053181 |
Caspase 8 |
A long pro-domain caspase that contains a death effector domain in its pro-domain region. Caspase 8 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS. |
CAP4 Protease,Caspase-8,FLICE Protein,MACH Protein,Mch5 Protease,Pro-Caspase-8,Procaspase-8,Pro Caspase 8,Procaspase 8 |
|
| D053220 |
Receptors, TNF-Related Apoptosis-Inducing Ligand |
Tumor necrosis factor receptor family members that are widely expressed and play a role in regulation of peripheral immune responses and APOPTOSIS. The receptors are specific for TNF-RELATED APOPTOSIS-INDUCING LIGAND and signal via conserved DEATH DOMAINS that associate with specific TNF RECEPTOR-ASSOCIATED FACTORS in the CYTOPLASM. |
Decoy Receptor 2, Tumor Necrosis Factor,Receptors, TRAIL,Receptors, Tumor Necrosis Factor, Member 10,Receptors, Tumor Necrosis Factor, Member 10b,TNF-Related Apoptosis-Inducing Ligand Receptors,Tumor Necrosis Factor Receptor Superfamily, Member 10,APO2 Receptor,CD261 Antigen,CD262 Antigen,CD264 Antigen,DCR2 Receptor,DR4 Receptor,DR5 Receptor,Death Receptor-4,Death Receptor-5,Receptor, TRAIL-1,Receptor, TRAIL-2,Receptor, TRAIL-4,Receptors, Tumor Necrosis Factor, Member 10a,Receptors, Tumor Necrosis Factor, Member 10d,TNF-Related Apoptosis-Inducing Ligand Receptor 2,TRAIL Receptor 1,TRAIL Receptor 2,TRAIL Receptor 4,TRAIL Receptors,Tumor Necrosis Factor Receptor Superfamily, Member 10a,Tumor Necrosis Factor Receptor Superfamily, Member 10b,Antigen, CD261,Antigen, CD262,Antigen, CD264,Death Receptor 4,Death Receptor 5,Receptor 4, TRAIL,Receptor, APO2,Receptor, DCR2,Receptor, DR4,Receptor, DR5,Receptor, TRAIL 1,Receptor, TRAIL 2,Receptor, TRAIL 4,Receptor-4, Death,Receptors, TNF Related Apoptosis Inducing Ligand,TNF Related Apoptosis Inducing Ligand Receptor 2,TNF Related Apoptosis Inducing Ligand Receptors,TRAIL-1 Receptor,TRAIL-2 Receptor,TRAIL-4 Receptor |
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