"You can teach your cells anything" I know what this dream is about...it seems there is a way to teach all cells in your body just about anything from fighting cancer, to living to 300. I have dozens of drawings on this and I'm trying to make sense of it right now, however it is a little technical.
Your dream drawing says "You can teach your cells anything".
Brian, your dream included the word “apoptosis”. I just had seen that word in my research the Blaho/Polio dream, so I looked it up.
Apoptosis is an important concept to understand, in the context of this dream. Hope this helps! ~ Bonnie W. ~
reply
Thanks once again Bonnie...posted.
Brian
Apoptosis
From Wikipedia, the free encyclopedia
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In biology, apoptosis (from the Greek words apo = from and ptosis = falling, commonly pronounced ap-a-tow'-sis[1]) is one of the main types of programmed cell death (PCD). As such, it is a process of deliberate life relinquishment by an unwanted cell in a multicellular organism. In contrast to necrosis, which is a form of cell death that results from acute cellular injury, apoptosis is carried out in an ordered process that generally confers advantages during an organism's life cycle. For example, the differentiation of human fingers in a developing embryo requires the cells between the fingers to initiate apoptosis so that the fingers can separate. The way the apoptotic process is executed facilitates the safe disposal of cell corpses and fragments.Since the beginning of the 1990s, research on apoptosis has grown spectacularly. In addition to its importance as a biological phenomenon, defective apoptotic processes have been implicated in an extensive variety of diseases. Too much apoptosis causes cell-loss disorders, whereas too little results in uncontrolled cell proliferation, namely cancerous tumors.
Not all forms of PCD share the characteristic shapes (the morphology) and sequences of apoptosis, but all types of PCD are highly-regulated processes.
Functions of apoptosis
Cell damage or infection
Apoptosis can occur, for instance, when a cell is damaged beyond repair, or infected with a virus. The "decision" for apoptosis can come from the cell itself, from its surrounding tissue or from a cell that is part of the immune system.
If a cell's capability of apoptosis is damaged (for example, by mutation), or if the initiation of apoptosis is blocked (by a virus), a damaged cell can continue dividing without restrictions, developing into cancer. For example, as part of the hijacking of the cell's genetic system carried out by human papillomaviruses (HPV), a gene called E6 is expressed in a product that degrades p53 protein, which is a vital piece of the apoptotic pathway. This severe interference in the apoptotic capability of cells plays a critical role in the fact that persistent infection by oncogenic HPVs can result in the development of cervical cancer.
Response to stress or DNA damage
Stress conditions, such as starvation, as well as damage to the cell's DNA resulting from toxicity or exposure to ultraviolet or ionizing radiation, such as gamma rays or X-rays, can induce a cell to begin an apoptotic process. A fascinating example, resulting from damage to the genome in the cell nucleus, is apoptosis triggered by the nuclear enzyme poly ADP ribose polymerase-1, or PARP-1. This enzyme plays a crucial role in maintaining genomic integrity, and massive activation of PARP-1 can deplete the cell of energy-providing molecules, an event that sends signals from the nucleus for the mitochondria to start the apoptotic process.
Homeostasis
In the adult organism, the number of cells within an organ or tissue has to be constant within a certain range. Blood and skin cells, for instance, are constantly renewed by their respective progenitor cells; but proliferation has to be compensated by cell death. This balancing process is part of the homeostasis required by living organisms to maintain their internal states within certain limits. Some authors and researchers like Steven Rose and Antonio Damasio have suggested homeodynamics as a more accurate and eloquent term (Damasio 1999, p. 141). The related term allostasis reflects a balance of a more complex nature by the body.
Between 50 billion and 70 billion cells die each day due to apoptosis in the average human adult. In a year, this amounts to the proliferation and subsequent destruction of a mass of cells equal to an individual's body weight.
Homeostasis is achieved when the rate of mitosis (cell proliferation) in the tissue is balanced by cell death. If this equilibrium is disturbed, either of two things happen:
- The cells are dividing faster than they die, effectively developing a tumor.
- The cells are dividing slower than they die, which results in a disorder of cell loss.
Both states can be fatal or highly damaging.
For instance, misregulation of Hedgehog (Hgg) protein signalling (see Development, below) has been implicated in several forms of cancer. Hgg, which conveys an anti-apoptotic signal, has been found to be overexpressed in pancreatic adenocarcinoma tissues.
Development
Programmed cell death is an integral part of both plant and metazoan (multicellular animals) tissue development. It does not resemble the sort of reaction that comes as a result of tissue damage due to accident or pathogenic infection (cell death by necrosis). Instead of swelling and bursting - hence spilling their possibly damaging internal contents into extracellular space - apoptotic cells and their nuclei shrink, and often fragment. In this way, they can be efficiently phagocytosed (and, as a consequence of this, their components reused) by macrophages or by neighboring cells.
Research on chick embryos - specifically on chick neural tube development - has suggested how selective cell proliferation, combined with selective apoptosis, sculpts developing tissues in vertebrates. During vertebrate embryo development, structures called the notochord and the floor plate secrete a gradient of the signaling molecule Sonic hedgehog (Shh), and it is this gradient that directs cells to form patterns in the embryonic neural tube: Cells that receive Shh in a receptor in their membranes called Patched1 (Ptc1) survive and proliferate; but, in the absence of Shh, one of the ends of this same Ptc1 receptor (the carboxyl-terminal, inside the membrane) is cleaved by caspase-3, an action that exposes an apoptosis-producing domain (see the Perspective by Isabel Guerrero and Ariel Ruiz i Altaba [2] and the research report by Chantal Thibert et al.[3]).Research like the one carried out by Thibert and her colleagues has begun to clarify some of the fundamental aspects of morphogenesis, or the development of organisms from fertilized eggs to fully-developed animals and plants. It has also suggested specific answers to why normal cells carry out apoptosis when they end up outside the places they should be in body tissues.
Immune cell regulation
B cells and T cells are sophisticated — and very effective — front-line players in the body's defenses against infectious agents, as well as against local cells that have acquired or developed a malignancy. In order to carry out their job, B and T cells must have the ability to discriminate "self" from "nonself," and "healthy" from "unhealthy," antigens (protein segments that make a good fit, like a key and a lock, with specialized receptors in B and T cell membranes). For instance, "killer" T cells can be activated when presented with fragments of inappropriately expressed proteins (resulting, say, from a malignant mutation) or with foreign antigens produced as a consequence of a viral infection. After becoming activated, they migrate out of the lymph nodes in which they reside, proliferate, recognize the affected cells and commit them to programmed cell death.
The receptors in immature B and T cell membranes are not tailored precisely to coincide with "known" antigens. Rather, they are generated through a highly variable process that results in an immense variety, capable of making a good fit with an astounding number of precise molecular shapes. This means that most of these immature cells can be either ineffective (because the almost random shapes of their receptors do not engage any antigen of significance) or dangerous to their own organism, because their receptors could make a good molecular fit with healthy self antigens. If they were to be let loose without any further processing, many could become autoreactive and attack healthy body cells. The way the immune system regulates this process is by "deleting" both the ineffective and the potentially damaging immature cells via apoptosis.
As has just been described in the previous section on development, all tissue in multicellular animals depends on continuous receipt of survival signals. In the case of T cells, as they develop and mature in the thymus, the survival signal depends on their capability to engage foreign antigens. Those that fail in this test, amounting to about 97% of the freshly-produced T cells, are committed to programmed cell death. The survivors are tested as well for potentially damaging autoimmune reactions, and those that show high affinity to healthy self antigens are killed via apoptosis.
Be aware that such a portrayal presents a highly simplified picture: The actual process in which B and T cells are driven to proliferation, differentiation or apoptosis comprises a complex interplay between positive and negative regulators.
7.20.2006
I noticed in one of your drawings regarding long life cure/reverse ageing what looks like a cell with an elongated nucleus instead of the standard round nucleus.
If you haven't heard of the platinum elements these might explain your dream.
These atoms all have what is called a super-deformed nucleus, meaning it's not round like most nucleus but rather long and thin. When they are high-spun, the nucleus does something spectacular and "stretches out," protecting all the electrons in the atom so they can never combine with other atoms (they are called monatomic at this point) and hence are mono - or one - atom.
This is related to quantum physics, time, space and all that other strange stuff.
Essentially we age because of time & space restrictions. If you eliminate these issues, you can live for hundreds of years, like the Egyptian pharaohs used to do (through the use of alchemy).
David Hudson discovered this and the DoD shut him down over it. Not surprising.
Here is excellent information on it if people are interested, although there are a ton of companies that make this now, this one appears to be the best.
The theory is we can all "ascend" (after curing our bodies and minds and emotions through the earlier steps) to pure light energy and completeness with God.
Keep up the work, Edgar. :)
reply
Thanks Edgar, will post this.
Brian
From Wikipedia, the free encyclopedia
A cell undergoing apoptosis. In just one of many scenarios of apoptosis, the process is triggered by another neighboring cell; the dying cell eventually transmits signals that tell the
phagocytes, which are a part of the
immune system, to
engulf it.
Apoptosis (Greek: apo - from, ptosis - falling; commonly pronounced with a silent second p[1]) is a process of deliberate life relinquishment by a cell in a multicellular organism. It is one of the main types of programmed cell death (PCD), and involves an orchestrated series of biochemical events leading to a characteristic cell morphology and death. The apoptotic process is executed in such a way as to safely dispose of cell corpses and fragments.
In contrast to necrosis, which is a form of cells death that results from acute cellular injury, apoptosis is carried out in an orderly process that generally confers advantages during an organism's life cycle. For example, the differentiation of fingers and toes in a developing human embryo requires cells between the fingers to initiate apoptosis so that the digits can separate.
Research on apoptosis has increased substantially since the early 1990s. In addition to its importance as a biological phenomenon, defective apoptotic processes have been implicated in an extensive variety of diseases. Excessive apoptosis causes cell-lose disease, such as in ischemic damage, whereas an insufficient amount results in uncontrolled cell proliferation, such as cancer.
Between 50 billion and 70 billion cells die each day due to apoptosis in the average human adult. In a year, this amounts to the proliferation and subsequent destruction of a mass of cells equal to an individual's body weight.
Functions of apoptosis
Cell damage or infection
Apoptosis can occur when a cell is damaged beyond repair, infected with a virus, or undergoing stress conditions such as starvation. DNA damage from ionizing radiation or toxic chemicals can also induce apoptosis via the actions of the tumour-suppressing gene p53. The "decision" for apoptosis can come from the cell itself, from the surrounding tissue, or from a cell that is part of the immune system. In these cases apoptosis functions to remove the damaged cell, preventing it from sapping further nutrients from the organism, or to prevent the spread of viral infection.
Apoptosis also plays a role in preventing cancer; if a cell is unable to undergo apoptosis, due to mutation or biochemical inhibition, it can continue dividing and develop into a tumour. For example, infection by papillomaviruses causes a viral gene to interfere with the cell's p53 protein, an important member of the apoptotic pathway. This interference in the apoptotic capability of the cell plays a critical role in the development of cervical cancer in women.
Homeostasis
In the adult organism, the number of cells is kept relatively constant through cell death and division. Cells must be replaced when they become diseased or malfunctioning; but proliferation must be compensated by cell death[2]. This balancing process is part of the homeostasis required by living organisms to maintain their internal states within certain limits. Some scientists have suggested homeodynamics as a more accurate term[3]. The related term allostasis reflects a balance of a more complex nature by the body.
Homeostasis is achieved when the rate of mitosis (cell proliferation) in the tissue is balanced by cell death. If this equilibrium is disturbed, one of two potentially fatal disorders occurs:
- The cells are dividing faster than they die, effectively developing a tumor.
- The cells are dividing slower than they die, which results in a disorder of cell loss.
The organism must orchestrate a complex series of controls to keep homeostasis tightly controlled, a process which is ongoing for the life of the organism and involves many different types of cell signaling. Impairment of any one of these controls can lead to a diseased state: for example, dysregulation of hedgehog signaling has been implicated in several forms of cancer. The hedgehog pathway, which conveys an anti-apoptotic signal, has been found to be activated in pancreatic adenocarcinoma tissues.
Development
Incomplete differentiation in two toes due to lack of apoptosis
Programmed cell death is an integral part of both plant and animal tissue development. Development of an organ or tissue is often preceded by the extensive division and differentiation of a particular cell, with the resultant mass is then "pruned" into the correct form by apoptosis. Unlike cellular death caused by injury, apoptosis results in cell shrinkage and fragmentation. This allows the cells to be efficiently phagocytosed and their components reused without releasing potentially harmful intracellular substances into the surrounding tissue.
Research on chick embryos has suggested how selective cell proliferation, combined with selective apoptosis, sculpts developing tissues in vertebrates. During vertebrate embryo development, structures called the notochord and the floor plate secrete a gradient of the signaling molecule Sonic hedgehog (Shh), and it is this gradient that directs cells to form patterns in the embryonic neural tube: cells that receive Shh in a receptor in their membranes called Patched1 (Ptc1) survive and proliferate; but, in the absence of Shh, one of the ends of this same Ptc1 receptor (the carboxyl-terminal, inside the membrane) is cleaved by caspase-3, an action that exposes an apoptosis-producing domain[4][5].
During development, apoptosis is tightly regulated and different tissues use different signals for inducing apoptosis. In birds, bone morphogenetic proteins (BMP) signaling is used to induce apoptosis in the interdigital tissue. In Drosophila flies, steroid hormones regulate cell death. Developmental cues can also induce apoptosis, such as the sex-specific cell death of hermaphrodite specific neurons in C. elegans males through low TRA-1 transcription factor activity (TRA-1 helps prevents cell death).
Lymphocyte interaction
The development of B lymphocytes and the development of T lymphocytes in the human body is a complex process that effectively creates a large pool of diverse cells to begin with, then weeds out those potentially damaging to the body. Apoptosis is the mechanism by which the body removes both the ineffective and the potentially damaging immature cells, and in T-cells is initiated by the withdrawal of survival signals[6].
Cytotoxic T-cells are able to directly induce apoptosis in cells by opening up pores in the target's membrane and releasing chemicals which bypass the normal apoptotic pathway. The pores are created by the action of secreted perforin, and the granules contain granzyme B, a serine protease which activates a variety of caspases by cleaving aspartate residues[7].
Apoptotic process
The process of apoptosis
The process of apoptosis is controlled by a diverse range of cell signals which may originate either extracellularly (extrinsic inducers) or intracellularly (intrinsic inducers). Extracellular signals may include hormones, growth factors, nitric oxide[8] or cytokines, and therefore must either cross the plasma membrane or transduce to effect a response. These signals may positively or negatively induce apoptosis; in this context the binding and subsequent initiation of apoptosis by a molecule is termed positive, whereas the active repression of apoptosis by a molecule is termed negative.
Intracellular apoptotic signalling is a response initiated by a cell in response to stress, and may ultimately result in cell suicide. The binding of nuclear receptors by glucocorticoids, heat, radiation, nutrient deprivation, viral infection and hypoxia are all factors which can lead to the release of intracellular apoptotic signals by a damaged cell[7].
Before the actual process of cell death is carried out by enzymes, apoptotic signals must be connected to the actual death pathway by way of regulatory proteins. This step allows apoptotic signals to either culminate in cell death, or be aborted should the cell no longer need to die. Several proteins are involved, however two main methods of achieving regulation have been identified; targeting mitochondria functionality, or directly transducing the signal via adapter proteins to the apoptotic mechanisms. The whole preparation process requires energy and functioning cell machinery.
Mitochondrial regulation
The mitochondria are essential to multicellular life, without them a cell ceases to respirate aerobically and quickly dies - a fact exploited by some apoptotic pathways. Apoptotic proteins which target mitochondria affect them in different ways; they may cause mitochondrial swelling through the formation of membrane pores, or they may increase the permeability of the mitochondrial membrane and cause apoptotic effectors to leak out[7].
Mitochondrial proteins known as SMACs (second mitochondria-derived activator of caspases) are released into the cytosol following an increase in permeability. SMAC binds to inhibitor of apoptosis proteins (IAPs) and inhibits them, preventing the IAPs from arresting the apoptotic process and therefore allowing apoptosis to proceed. IAP also normally suppresses the activity of a group of cysteine proteases called caspases[9], which carry out the degradation of the cell, therefore the actual degradation enzymes can be seen to be indirectly regulated by mitochondrial permeability.
Cytochrome c is also released from mitochondria due to increased permeability of the outer mitochondrial membrane, and serves a regulatory function as it precedes morphological change associated with apoptosis[7]. Bcl-2 proteins are able to promote or inhibit apoptosis by either direct action on mitochondrial permeability, or indirectly through other proteins. Importantly, the actions of some Bcl-2 proteins are able to halt apoptosis even if cytochrome c has been released by the mitochondria[7] coupled to extrinsic signals.
TNF is a cytokine produced mainly by activated macrophages, and is the major extrinsic mediator of apoptosis. Most cells in the human body have two receptors for TNF: TNF-R1 and TNF-R2. The binding of TNF to TNF-R1 has been shown to initiate the pathway that leads to caspase activation via the intermediate membrane proteins TNF receptor-associated death domain (TRADD) and Fas-associated death domain protein (FADD)[10]. Binding of this receptor can also indirectly lead to the activation of transcription factors involved in cell survival and inflammatory responses[11]. The link between TNF and apoptosis shows why an abnormal production of TNF plays a fundamental role in several human diseases, especially in autoimmune diseases.
The Fas receptor (also known as Apo-1 or CD95) binds the Fas ligand (FasL), a transmembrane protein part of the TNF family[12]. The interaction between Fas and FasL results in the formation of the death-inducing signaling complex (DISC), which contains the FADD, caspase-8 and caspase-10. In some types of cells (type I), processed caspase-8 directly activates other members of the caspase family, and triggers the execution of apoptosis. In other types of cells (type II), the Fas-DISC starts a feedback loop that spirals into increasing release of pro-apoptotic factors from mitochondria and the amplified activation of caspase-8[13].
Following TNF-R1 and Fas activation in mammalian cells a balance between pro-apoptotic (BAX[14], BID, BAK, or BAD) and anti-apoptotic (Bcl-Xl and Bcl-2) members of the Bcl-2 family is established. This balance is the proportion of pro-apoptotic homodimers that form in the outer-membrane of the mitochondrion. The pro-apoptotic homodimers are required to make thie mitochondrial membrane permeable for the release of caspase activators such as cytochrome c and SMAC. Control of pro-apoptotic proteins under normal cell conditions of non-apoptotic cells is incompletely understood, but it has been found that a mitochondrial outer-membrane protein, VDAC2, interacts with BAK to keep this potentially-lethal apoptotic effector under control[15]. When the death signal is received, products of the activation cascade displace VDAC2 and BAK is able to be activated.
Execution
Although many pathways and signals lead to apoptosis, there is only one mechanism which actually causes the death of the cell in this process; after the appropriate stimulus has been received by the cell and the necessary controls exerted, a cell will undergo the organised degradation of cellular organelles by activated proteolytic caspases. A cell undergoing apoptosis shows a characteristic morphology that can be observed with a microscope:
- Cell shrinkage and rounding due to the breakdown of the proteinaceous cytoskeleton by caspases.
- The cytoplasm appears dense, and the organelles appear tightly packed.
- Chromatin undergoes condensation into compact patches against the nuclear envelope in a process known as pyknosis, a hallmark of apoptosis[16][17].
- The nuclear envelope becomes discontinuous and the DNA inside it is fragmented in a process referred to as karyorrhexis. The nucleus breaks into several discrete chromatin bodies or nucleosomal units due to the degradation of DNA[18].
- The cell membrane shows irregular buds known as blebs.
- The cell breaks apart into several vesicles called apoptotic bodies, which are then phagocytosed.
Removal of dead cells
Dying cells that undergo the final stages of apoptosis display phagocytotic molecules, such as phosphatidylserine, on their cell surface[19]. Phosphatidylserine is normally found on the cytosolic surface of the plasma membrane, but is redistributed during apoptosis to the extracellular surface by a hypothetical protein known as scramblase[20]. These molecules mark the cell for phagocytosis by cells possessing the appropriate receptors, such as macrophages[21]. Upon recognition, the phagocyte reorganizes its cytoskeleton for engulfment of the cell. The removal of dying cells by phagocytes occurs in an orderly manner without eliciting an inflammatory response.
Implication in disease
Defective apoptotic pathways
The many different types of apoptotic pathways contain a multitude of different biochemical components, many of them not yet understood[2]. As a pathway is more or less sequential in nature it is a victim of causality; removing or modifying one component leads to an effect in another. In a living organism this can have disastrous effects, often in the form of disease or disorder. A discussion of every disease caused by modification of the various apoptotic pathways would be impractical, but the concept overlying each one is the same: the normal functioning of the pathway has been disrupted in such a way as to impair the ability of the cell to undergo normal apoptosis. This results in a cell which lives past its "use-by-date" and is able to replicate and pass on any faulty machinery to its progeny, increasing the likelihood of the cell becoming cancerous or diseased.
A recently described example of this concept in action can be seen in the development of a lung cancer called NCI-H460[22]. The X-linked inhibitor of apoptosis protein (XIAP) is overexpressed in cells of the H460 cell line. 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 pro-apoptotic agonists. Consequently, the balance of anti-apoptotic and pro-apoptotic effectors is upset in favour of the former and the damaged cells continue to replicate despite being told to die.
p53 dysregulation
The tumor-suppressor protein p53 accumulates when DNA is damaged due to a chain reaction of biochemical reactions. Part of this pathway includes interferon-alpha and interferon-beta, which induce transcription of the p53 gene and result in the increase of p53 protein level and enhancement of cancer cell-apoptosis[23]. p53 prevents the cell from replicating by stopping the cell cycle at G1 to give the cell time to repair, however it will induce apoptosis if damage is extensive and repair efforts fail. Logically, any disruption to the regulation of the p53 or interferon genes will result in impaired apoptosis and the possible formation of tumors.
HIV progression
The progression of the human immunodeficiency virus (HIV) to AIDS is primarily due to the depletion of CD4+ T-helper lymphocytes, which leads to a compromised immune system. The mechanism by which T-helper cells are depleted is apoptosis, which can be the end product of multiple biochemical pathways[24]:
- HIV enzymes inactivate anti-apoptotic Bcl-2 and simultaneously activate pro-apoptotic procaspase-8. This does not directly cause cell death but primes the cell for apoptosis should the appropriate signal be received.
- HIV products may increase levels of cellular proteins which have a promotive effect on Fas-mediated apoptosis.
- HIV proteins decrease the amount of CD4 glycoprotein marker present on the cell membrane.
- Released viral particles and proteins present in extracellular fluid are able to induce apoptosis in nearby "bystander" T-helper cells.
- HIV decreases the production of molecules involved in marking the cell for apoptosis, giving the virus time to replicate and continue releasing apoptotic agents and virions into the surrounding tissue.
Apoptosis in invertebrates
C. elegans
Cells express pro-apoptotic factor, EGL-1, when they are fated to die. EGL-1 is a BH3 domain containing protein and is homologous to the vertebrates BAD and BIK. EGL-1 binds to CED-9 (homolog of Bcl-2) and prevents CED-9 from binding to adaptor protein CED-4 (homolog of Apaf-1, Cytochrome c). When released, CED-4 is capable of binding to CED-3 and activating the caspase CED-3. CED-3 is the key protein involved in executing the death of the cell.
See also
References
- ^ Apoptosis Interest Group (1999). About apoptosis. Retrieved on [[2006-12-15]].
- ^ a b Thompson, CB (1995). "Apoptosis in the pathogenesis and treatment of disease". Science 267 (5203).
- ^ Damasio, Antonio; (1999). The Feeling of What Happens. New York: Harcourt Brace & Co..
- ^ Guerrero I, Ruiz i Altaba A. (2003). "Development. Longing for ligand: hedgehog, patched, and cell death". Science 301 (5634).
- ^ Thibert C, Teillet MA, Lapointe F, Mazelin L, Le Douarin NM, Mehlen P. (2003). "Inhibition of neuroepithelial patched-induced apoptosis by sonic hedgehog.". Science 301 (5634).
- ^ Werlen G, et al. (2003). "Signaling life and death in the thymus: timing is everything". Science 299 (5614).
- ^ a b c d e Cotran; Kumar, Collins. Robbins Pathologic Basis of Disease. Philadelphia: W.B Saunders Company. 0-7216-7335-X.
- ^ Bernhard Brüne (2003). "Nitric oxide: NO apoptosis or turning it ON?". Nature 10 (8).
- ^ Fesik SW, Shi Y. (2001). "Controlling the caspases". Science 294 (5546).
- ^ Chen G, Goeddel DV (2002). "TNF-R1 signaling: a beautiful pathway". Science 296 (5573).
- ^ Goeddel, DV et al. "Connection Map for Tumor Necrosis Factor Pathway". Science.
- ^ Wajant H (2002). "The Fas signaling pathway: more than a paradigm". Science 296 (5573).
- ^ Wajant, H.. "Connection Map for Fas Signaling Pathway". Science.
- ^ Murphy, KM et al (2000). "Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells". Cell Death and Differentiation 7 (1).
- ^ Cheng EH (2003). "VDAC2 inhibits BAK activation and mitochondrial apoptosis". Science 301 (5632).
- ^ Santos A. Susin, et al. (2000). "Two Distinct Pathways Leading to Nuclear Apoptosis". Journal of Experimental Medicine 192 (4).
- ^ Madeleine Kihlmark, et al. (2001). "Sequential degradation of proteins from the nuclear envelope during apoptosis". Journal of Cell Science (114).
- ^ Nagata S (2000). "Apoptotic DNA fragmentation". Experimental Cell Research 256 (1).
- '^ Li MO, et al. (2003). "Phosphatidylserine receptor is required for clearance of apoptotic cells". Science 302 (5650).
- ^ Wang X, et al. (2003). "Cell corpse engulfment mediated by C. elegans phosphatidylserine receptor through CED-5 and CED-12". Science 302 (5650).
- ^ Savill J, Gregory C, Haslett C. (2003). "Eat me or die". Science 302 (5650).
- ^ Yang, L. et al. (2003). "Predominant suppression of apoptosome by inhibitor of apoptosis protein in non-small cell lung cancer H460 cells: therapeutic effect of a novel polyarginine-conjugated Smac peptide.". Cancer Research 63 (4).
- ^ Takaoka A, et al. (2003). "Integration of interferon-alpha/beta signalling to p53 responses in tumour suppression and antiviral defence.". Nature 424 (6948).
- ^ Judie B. Alimonti, T. Blake Ball, Keith R. Fowke (2003). "Mechanisms of CD4+ T lymphocyte cell death in human immunodeficiency virus infection and AIDS". J Gen Virology (84).
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