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Page "Apoptosis" ¶ 18
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proapoptotic and homodimers
This balance is the proportion of proapoptotic homodimers that form in the outer-membrane of the mitochondrion.

proapoptotic and are
Control of proapoptotic proteins under normal cell conditions of nonapoptotic cells is incompletely understood, but in general, Bax or Bak are activated by the activation of BH3-only proteins, part of the Bcl-2 family.
These homologs can inhibit proapoptotic proteins such as BAX and BAK, which are essential for the activation of apoptosis.

proapoptotic and mitochondrial
In parallel, these enzymes activate proapoptotic procaspase-8, which does directly activate the mitochondrial events of apoptosis.

proapoptotic and release
In other types of cells ( type II ), the Fas-DISC starts a feedback loop that spirals into increasing release of proapoptotic factors from mitochondria and the amplified activation of caspase-8.

proapoptotic and cytochrome
XIAPs bind to the processed form of caspase-9, and suppress the activity of apoptotic activator cytochrome c, therefore overexpression leads to a decrease in the amount of proapoptotic agonists.

proapoptotic and SMAC
They were able to synthesize a molecule that mimics the proapoptotic protein called SMAC ( whose function is described in biochemical execution of apoptosis ).

proapoptotic and .
Following TNF-R1 and Fas activation in mammalian cells a balance between proapoptotic ( BAX, BID, BAK, or BAD ) and anti-apoptotic ( Bcl-Xl and Bcl-2 ) members of the Bcl-2 family is established.
A remarkable feature of these KO mice is that they have a very restricted phenotype: Casp3, 9, APAF-1 KO mice have deformations of neural tissue and FADD and Casp 8 KO showed defective heart development, however in both types of KO other organs developed normally and some cell types were still sensitive to apoptotic stimuli suggesting that unknown proapoptotic pathways exist.
As a consequence, the balance of anti-apoptotic and proapoptotic effectors is upset in favour of the former, and the damaged cells continue to replicate despite being directed to die.
Treatments aiming to inhibit apoptosis work to simultaneously inhibit the expression of proapoptotic factors and promote the expression of anti-apoptotic factors.
NF-κB has been found to play both an antiapoptotic role and proapoptotic role depending on the stimuli utilized and the cell type.
Consequently p53 cannot induce apoptosis since it cannot induce the expression of proapoptotic proteins.
One analog, ABT-510, exhibits potent proapoptotic activity in cultured cells, while clinically it is very well tolerated with therapeutic benefits reported against several malignancies.
These results have been expanded and it has also been shown that p73 is present in early stages of neurological development and neuronal apoptosis by blocking the proapoptotic function of p53.
One of the most studied roles of ceramide pertains to its function as a proapoptotic molecule.

homodimers and are
Receptor binding as well as membrane fusion are catalyzed by the protein E, which changes its conformation at low pH, which causes a rearrangement of the 90 homodimers to 60 homotrimers.
* Ly49 ( homodimers ) — a relatively ancient, C-type lectin family receptor ; are of multigenic presence in mice, while humans have only one pseudogenic Ly49 ; the receptor for classical ( polymorphic ) MHC I molecules.
** receptor tyrosine kinase – Functional receptors are homodimers.
Both classes are flavoproteins which function as homodimers.
Type III filaments such as GFAP are capable of forming both homodimers and heterodimers ; GFAP can polymerize with other type III proteins or with neurofilament protein ( NF-L ).
Hormone-activated estrogen receptors form dimers, and, since the two forms are coexpressed in many cell types, the receptors may form ERα ( αα ) or ERβ ( ββ ) homodimers or ERαβ ( αβ ) heterodimers.
RPB3, RPB5, and RPB7 interact with themselves to form homodimers, and RPB3 and RPB5 together are able to contact all of the other RPB subunits, except RPB9.
The PKG-I and PKG-II are homodimers of two identical subunits (~ 75 kDa and ~ 85 kDa, respectively ) and share common structural features.
Less-common homodimers of the CD8-α chain are also expressed on some cells.
These are generally palindromic sequences ( because restriction enzymes usually bind as homodimers ), and a particular restriction enzyme may cut the sequence between two nucleotides within its recognition site, or somewhere nearby.
The cadherins are a family of transmembrane proteins that form homodimers in a calcium-dependent manner with other cadherin molecules on adjacent cells.
STAT1 homodimers are involved in type II interferon signalling, and bind to the GAS ( Interferon-Gamma Activated Sequence ) promoter to induce expression of ISG ( Interferon Stimulated Genes ).

homodimers and for
Glucosidases then remove terminal glucose residues ; it is believed that this glucose trimming is responsible for the conformational change needed for LPL to form homodimers and become catalytically active.
A similar RhoA-mediated mechanism is proposed for long range chemorepulsion whereby netrin-1 binding to UNC-5 homodimers alone motivates tyrosine phosphorylation requiring FAK and Src, which as a result active RhoA.

homodimers and such
In addition to forming homodimers after ligand binding, EGFR may pair with another member of the ErbB receptor family, such as ErbB2 / Her2 / neu, to create an activated heterodimer.

homodimers and .
It is possible that as neuroblasts reach the higher levels they stop their migration either because of the heightened combined expression of all forms of reelin, or due to the peculiar mode of action of the full-sized reelin molecules and its homodimers.
* Ly49 ( homodimers )-a C-type lectin family of receptors.
Though most TLRs appear to function as homodimers, TLR2 forms heterodimers with TLR1 or TLR6, each dimer having a different ligand specificity.
This acidic environment causes a conformational change in the E protein which disassociates it from the prM protein and causes it to form E homodimers.
These homodimers lie flat against the viral surface giving the maturing virion a smooth appearance.
Different STATs form hetero-or homodimers.
All PDGFs function as secreted, disulphide-linked homodimers, but only PDGFA and B can form functional heterodimers.
* Step 1: in the first step of IF assembly two parallel, unstaggered intermediate filament polypeptides chains form a dimer via their a-helical rod domains ; these dimers can be either homodimers or heterodimers.
It has been shown that some members of this family form homodimers.
In general, they bind to and activate the erbB family of receptor tyrosine kinases ( erbB2 ( HER2 ), erbB3 ( HER3 ), and erbB4 ( HER4 )), functioning both as heterodimers and homodimers.
VSGs form homodimers.

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