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Caspase 1
|
D020170 |
[A long pro-domain caspase that has specificity for the precursor form of INTERLEUKIN-1BETA. It plays a role in INFLAMMATION by catalytically converting the inactive forms of CYTOKINES such as interleukin-1beta to their active, secreted form. Caspase 1 is referred as interleukin-1beta converting enzyme and is frequently abbreviated ICE.
] |
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Caspase 10
|
D053455 |
[A long pro-domain caspase that contains a death effector domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS. Caspase 10 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
] |
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Caspase 12
|
D053454 |
[A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Caspase 12 is activated by pro-apoptotic factors that are released during cell stress and by CARD SIGNALING ADAPTOR PROTEINS. It activates APOPTOSIS by cleaving and activating EFFECTOR CASPASES.
] |
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Caspase 14
|
D053456 |
[A short pro-domain caspase that is almost exclusively expressed in the EPIDERMIS and may play a role in the differentiation of epidermal KERATINOCYTES.
] |
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Caspase 2
|
D053143 |
[A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its caspase recruitment domain with CARD SIGNALING ADAPTOR PROTEINS. Caspase 2 plays a role in APOPTOSIS by cleaving and activating effector pro-caspases. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
] |
|
Caspase 3
|
D053148 |
[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.
] |
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Caspase 6
|
D053178 |
[A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 7; CASPASE 8; and CASPASE 10. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
] |
|
Caspase 7
|
D053179 |
[A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 3 and CASPASE 10. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
] |
|
Caspase 8
|
D053181 |
[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.
] |
|
Caspase 9
|
D053453 |
[A long pro-domain caspase that contains a CASPASE RECRUITMENT DOMAIN in its pro-domain region. Caspase 9 is activated during cell stress by mitochondria-derived proapoptotic factors and by CARD SIGNALING ADAPTOR PROTEINS such as APOPTOTIC PROTEASE-ACTIVATING FACTOR 1. It activates APOPTOSIS by cleaving and activating EFFECTOR CASPASES.
] |
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Caspase Activation and Recruitment Domain
|
D000071476 |
[A homotypic protein interaction module of the death domain superfamily. It is composed of a bundle of six alpha-helices that is related in sequence and structure to the DEATH DOMAIN and DEATH EFFECTOR DOMAIN. The Caspase Activation and Recruitment Domain (CARD domain) typically associates with other CARD-containing proteins, forming either dimers or trimers. CARD domains may occur in isolation, or in combination with other domains in CARD signaling adaptor proteins and initiator CASPASES that function in APOPTOSIS.
] |
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Caspase Inhibitors
|
D061945 |
[Endogenous and exogenous compounds and that either inhibit CASPASES or prevent their activation.
] |
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Caspases
|
D020169 |
[A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.
] |
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Caspases, Effector
|
D053470 |
[A subclass of caspases that contain short pro-domain regions. They are activated by the proteolytic action of INITIATOR CASPASES. Once activated they cleave a variety of substrates that cause APOPTOSIS.
] |
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Caspases, Initiator
|
D053471 |
[A subtype of caspases that contain long pro-domain regions that regulate the activation of the enzyme. The pro-domain regions contain protein-protein interaction motifs that can interact with specific signaling adaptor proteins such as DEATH DOMAIN RECEPTORS; DED SIGNALING ADAPTOR PROTEINS; and CARD SIGNALING ADAPTOR PROTEINS. Once activated, the initiator caspases can activate other caspases such as the EFFECTOR CASPASES.
] |
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Caspian Sea
|
D000077228 |
[The largest inland body of water, located between ASIA and EUROPE.
] |
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Caspofungin
|
D000077336 |
[A cyclic lipopeptide echinocandin and beta-(1,3)-D-glucan synthase inhibitor that is used to treat internal or systemic MYCOSES.
] |
|
Cassia
|
D002366 |
[A plant genus of the family FABACEAE. Many species of this genus, including the medicinal C. senna and C. angustifolia, have been reclassified into the Senna genus (SENNA PLANT) and some to CHAMAECRISTA.
] |
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Castanospermum
|
D031291 |
[A plant genus of the family FABACEAE that contains castanospermines, swainsonine, and triterpenoid saponins.
] |
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Castleman Disease
|
D005871 |
[Large benign, hyperplastic lymph nodes. The more common hyaline vascular subtype is characterized by small hyaline vascular follicles and interfollicular capillary proliferations. Plasma cells are often present and represent another subtype with the plasma cells containing IgM and IMMUNOGLOBULIN A.
] |
