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Post by skyship on Apr 3, 2012 3:22:41 GMT -5
Chitin is from insect cells, in the baculovirus, used in human vaccines. Fungi in the sense of rhizoids, mycelias, not reg fungi, these are small and need blue light.
photolyase....these are in these notice the change here: from native dna to dimers etc. they say is from UV light, however, it is not. this creates the dimer .....not the UV. The UV makes the dimer come alive!================================ Chlorella pyrenoidosa is a freshwater green alga and belongs to class Chlorophyceae, order Chlorellales and family Chlorellaceae. CPD photolyase is an enzyme found in Chlrella pyrnoidosa and responsible for repairing of DNA damages caused by UV radiations. The cyclobutane pyrimidine dimmer (CPDs) and 6-4 pyrimidone photoproducts (6-4 PPs) are major form of DNA damages and these damages are caused by various physical and chemical agents occurs in the environment such as UV and ionizing radiations, chemical mutagens fungal and bacterial toxins, and free radicals or alkalizing agents produced by metabolism.www.ijest.info/docs/IJEST10-02-08-90.pdf=================================== This cyclobutane pyrimidine dimer CPD and the 6-4 pyrimidone photoproducts ARE REPAIR SUBUNITS This two were created. This went inside the dna and created the dimer. lesion in the dna itself. We are being effected by these repair units. image:mol-biol4masters.masters.grkraj.org/html/DNA_Damage_And_Repair3-Repair_Mechanisms_files/image019.jpgnow what happens is the repair CPD, cyclobutane pyrimidine dimer,
"This diagram depicts how the Photolyase by using light radiation energy, breaks such bonds to restore the dimers into monomers, which facilitates the normal replication and even transcription. FADH provides electrons to cyclobutane rings for splitting the bonds.
The diagram .. shows how the Photolyase uses light energy and transfers the light energy to Cyclobutane rings to open up to generate individual nucleotide free to base pair with their normal bases. Before they execute repair functions they flip the dimers towards enzyme surface, then perform reaction.=================================================== So, when sun heats them up, they come out, these dimers are made of some kind of monomer? So what makes the dimers in the first place?
It is those dimers that are coming out. these are protofibrils as well.
So, this is inside of us already. What makes the monomer?
Cyclobutane rings? these themselves are toxic. When gets down to monomer level it begins to mutate again instead of being expelled out of skin. Here shows they are toxic.=========================== H-NMR Studies of Duplex DNA Decamer Containing a Uracil Cyclobutane Dimer: Implications Regarding the High UV Mutagenecity of CC Photolesions,PHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 4 2002 ABSTRACT T o determine the origin of the UV-specific CC to TT tandem mutation at the CC site, we made a duplex DNA decamer containing a uracil cis,syn cyclobutane dimer (CBD) as the deaminated model of a cytosine dimer. Two-dimensional 1H-NMR spectroscopy studies were performed on this sequence where two adenines (Ade) were opposite to the uracil dimer. Two imino protons of the uracil dimer were found to retain Watson,Crick hydrogen bonding with the opposite Ade, although the 5,-U(NH) of the dimer site showed unusual upfield shift like that of the 5,-T(NH) of the TT dimer, which seemed to be associated with deshielding by the flanking base rather than with reduced hydrogen bonding. (McAteer et al. 1998, J. Mol. Biol. 282:1013,1032). Hydrogen bondings at the dimer site were also supported by detecting typical strong nuclear Overhauser effects (NOE) between two imino protons and the opposite Ade H2 or NH2. But sequential NOE interactions of base protons with sugar protons were absent at the two flanking nucleotides of the 5, side of the uracil dimer and at the intradimer site, contrasting with its thymine analog where sequential NOE was absent only at the A4,T5 step. In addition, NOE cross peak for U5(NH) , A4(H2) was detected, although the NOE interactions of U6(NH) with A7(H2) and A17(H2) were not observed in contrast to the thymine dimer duplex. This different local structural alteration may be affected by the induced right-hand twisted puckering mode of cis,syn cyclobutane ring of the uracil dimer in the B-DNA duplex, even though the isolated uracil dimer had left-hand twisted puckering rigidly. In parallel, these observations may be correlated with observed differences in mutagenic properties between cis,syn UU dimer and cis,syn TT dimer. [source] www.academicconcepts.net/concepts/221/cyclobutane_ring.htm============================ Cyclobutane photodimers ("CPD's") are formed by photochemical reactions that result in the coupling of the C=C double bonds of pyrimidines.[4][5][6] T-T dimers thymine dimers formed in between two thymines are the most abundant of the CPD's. CPD's are readily repaired by nucleotide excision repair enzymes. In most organisms they can also be repaired by photolyases, a light-dependent family of enzymes. Xeroderma pigmentosum is a genetic disease where this damage can not be repaired,en.wikipedia.org/wiki/Cyclobutaneskyship
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Post by skyship on Apr 3, 2012 4:36:04 GMT -5
The repair mechanisms are causing the damage and the lesions in the DNA the monomers.. form the dimers which form the lesions. What triggers the monomer to expand to dimer and protofibril..... the photolyase. but it is the light source that triggers it. Why is the monomer in the body in the first place and what is that monomer that recognizes the light source? I quess they would be called UN Natural Building Blocks:"Synthesis of glycerol nucleic acid (GNA) phosphoramidite monomers and oligonucleotide polymers.Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ, USA. Abstract This unit describes a straightforward method for preparing glycerol nucleic acid (GNA) phosphoramidite monomers and oligonucleotide polymers using standard cyanoethyl phosphoramidite chemistry. GNA is an unnatural nucleic acid analog composed of an acyclic three-carbon sugar-phosphate backbone that contains one stereogenic center per repeating unit. [/b] GNA has attracted significant attention as a nucleic acid derivative due to its unique ability to form stable Watson-Crick anti-parallel duplex structures with thermal and thermodynamic stabilities rivaling those of natural DNA and RNA. The chemical simplicity of this nucleic acid structure provides access to enantiomerically pure forms of right- and left-handed helical structures that can be used as unnatural building blocks in DNA nanotechnology."...........www.ncbi.nlm.nih.gov/pubmed/20827716monomers are made of this: phosphoramidite monomers conjugation of these glycerol nucleic acid (GNA) phosphoramidite monomers and oligonucleotide polymersthere you have it. The perpendicular helix, no longer just linear. linear is now crossed. like this: +
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Post by skyship on Apr 3, 2012 5:04:47 GMT -5
OMgosh the tea cup and the black box, the tea.......here.......? and the black box is the secrets of the Cell. Darwin's black box. Tea is the secrets of the tea leaf? leaves in human dna? so the filaments of the cell and the spark in the tea? So the phosphoramidite monomer is sinking into the cell. The nanoparticle is sinking into the cell. ? make sense? phosphoramidite monomers
phosphoramidite?H-Phosphonate Chemistry H-phosphonate monomers are useful for the preparation of internucleotide linkages that are not attainable by standard phosphoramidite chemistry. Using this method, the monomer that is able to be activated is a 5'-DMT-base-protected, nucleoside 3'-hydrogen phosphonate. The presence of the H- phosphonate moiety on these monomers renders phosphate protection unnecessary. The same base protecting groups are used in phosphite triester chemistry. The H-phosphate synthesis cycle is very similar to that of the phosphoramidite method. Slight differences result from the properties of the monomers utilized. For instance, a different activating agent is used. In addition, the H-phosphonate diesteres generated by the coupling reactions are stable to the normal reaction conditions, so oxidation at every step is unnecessary. Instead, a single oxidation step can be performed at the end of the chain elongation. This single oxidation step makes it easy to produce modified DNA. For instance, if a sulfur containing compound is used as the oxidizing agent, all of the internucleotide bonds will then contain sulphur instead if oxygen attached to the phosphorous atom. The most popular use of this chemistry is for the radioactive labeling of all phosphodiester linkages to phosphorothioate by using radioactive sulfur. H-Phosphonate synthesis uses the same supports as does the ß-cyanoethyl phosphoramidite chemistry.The MonomersThe H-Phosphonate monomers are protected at the 5'-hydroxyl position with dimethoxytrityl groups. The exocyclic amines on the bases are protected by the same groups as in the ß-cyanoethyl phosphoramidite analogues. The phosphonate group is attached to the 3' position. see image O-Tea at bottom of images?www.genelink.com/newsite/products/phosphonate.asp============= phosphoramidite: synthetic DNA:www.csun.edu/~hcbio027/biotechnology/lec3/pitt8.html Phosphoramidate oligonucleotides as potent antisense molecules in cells and in vivo
Antisense oligonucleotides are designed to specifically hybridize to a target messenger RNA (mRNA) and interfere with the synthesis of the encoded protein...A large body of work on antisense oligonucleotides makes use of backbone-modified phosphorothioate oligonucleotides. Advances in chemical synthesis have brought forth a number of additional modifications, both on base residues (such as C5-propyne pyrimidines1 or a cytosine analog2), and on sugar (such as 2'-O-(2-methoxy)ethyl3) (for a review, see ref. 4). Significant increase in antisense activity can be obtained, as is the case for the three modifications mentioned above. Even though this effect was generally associated with high binding affinity to the RNA target, there could be other intracellular parameters that favor thermodynamic, kinetic, or structural characteristics of the hybrid duplex and enhance antisense-mediated activity. A large body of work on antisense oligonucleotides makes use of backbone-modified phosphorothioate oligonucleotides. Advances in chemical synthesis have brought forth a number of additional modifications, both on base residues (such as C5-propyne pyrimidines1 or a cytosine analog2), and on sugar (such as 2'-O-(2-methoxy)ethyl3) (for a review, see ref. 4). Significant increase in antisense activity can be obtained, as is the case for the three modifications mentioned above. Even though this effect was generally associated with high binding affinity to the RNA target, there could be other intracellular parameters that favor thermodynamic, kinetic, or structural characteristics of the hybrid duplex and enhance antisense-mediated activity." nanoparticle oligonucleotides:www.nature.com/nbt/journal/v19/n1/fig_tab/nbt0101_40_F4.htmlwww.nature.com/nbt/journal/v19/n1/full/nbt0101_40.html Note the Title:Phosphoramidate oligonucleotides as potent antisense molecules in cells and in vivoin cells and in live body. well, quess we are monitored in more ways than one, right down to our dna, and repairs are going on as we speak, however, some of these repairs are breaking down already, creating more chaos, they knew there would be risks. However, is there another motive? I think so. Well, God will set things straight, but, then again he does not exist for those folks. Men/women are the new gods and goddesses, they were created out of monomers anyway, right? Well the harvest is coming, right, in fact the reaping has started. skyship
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Post by aqt on Sept 19, 2012 10:14:06 GMT -5
moving this forward as I feel it is jam packed with info we need to review.....
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Post by aqt on Sept 30, 2012 16:45:04 GMT -5
our answers begin here
and end with pine tree resin perhaps???
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Post by aqt on Sept 30, 2012 16:58:39 GMT -5
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Post by aqt on Sept 30, 2012 17:02:00 GMT -5
Cbl (named after Casitas B-lineage Lymphoma) is a mammalian gene encoding the protein CBL which is an E3 ubiquitin- protein ligase involved in cell signalling and protein ubiquitination. Mutations to this gene have been implication in a number of human cancers, particularly acute myeloid leukaemia.[1] en.wikipedia.org/wiki/CBL_(gene)CBL-001? ? Homologues Three mammalian homologues have been characterized, which all differ in their ability to function as adaptor proteins due to the differing lengths of their C-terminal UBA domains: 1.c-Cbl: ubiquitously expressed, 906 amino acids in length. 2.Cbl-b: ubiquitously expressed, 982 amino acids long in length. 3.Cbl-c: lacks the UBA domain and is therefore only 474 amino acids in length. It is primarily expressed in epithelial cells however its function is poorly understood. Interestingly, both c-Cbl and Cbl-b have orthologues in D. melanogaster (D-Cbl) and C. elegans (Sli-1), hinting at a long evolutionary path for these proteins.[3] sound familiar? Ubiquitin ligase Ubiquitination is the process of chemically attaching ubiquitin monomers to a protein, thereby targeting it for degradation. As this is a multi-step process, several different enzymes are involved, the final one being a member of the E3 family of ligases. Cbl functions as an E3 ligase, and therefore is able to catalyse the formation of a covalent bond between ubiquitin and Cbl's protein substrate - typically a receptor tyrosine kinase. The RING-finger domain mediates this transfer, however like other E3 ligases of the RING type no intermediate covalent bond is formed between ubiquitin and the RING-finger domain. The stepwise attachment of ubiquitin to the substrate receptor tyrosine kinase can lead to its removal from the plasma membrane and subsequent trafficking to the lysosome for degradation.
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Post by aqt on Sept 30, 2012 17:13:08 GMT -5
sky...our first conversation EVER was about phosphorylation...do you rememeber??? CBL...a calcium sensor protein.... could this be CBL-001 from silent superbug?? www.ncbi.nlm.nih.gov/pubmed/22253446Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins.
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Post by aqt on Sept 30, 2012 17:16:16 GMT -5
CBL-c Signal transduction protein CBL-C is a protein that in humans is encoded by the CBLC gene.[1][2][3] CBL proteins, such as CBLC, are phosphorylated upon activation of a variety of receptors that signal via protein tyrosine kinases. Through interactions with proteins containing SRC (MIM 190090) homology-2 (SH2) and SH3 domains, CBL proteins modulate downstream cell signaling (Keane et al., 1999).[supplied by OMIM][3] cell signaling...quorum sensing... en.wikipedia.org/wiki/CBLC
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Post by aqt on Sept 30, 2012 17:37:01 GMT -5
Entrez Gene summary for CBL: The cbl oncogene was first identified as part of a transforming retrovirus which induces mouse pre-B and pro-B cell lymphomas. As an adaptor protein for receptor protein-tyrosine kinases, it positively regulates receptor protein-tyrosine kinase ubiquitination in a manner dependent upon its variant SH2 and RING finger domains. Ubiquitination of receptor protein-tyrosine kinases terminates signaling by marking active receptors for degradation. (provided by RefSeq, Jul 2008) www.genecards.org/cgi-bin/carddisp.pl?gene=CBLUniProtKB/Swiss-Prot: CBL_HUMAN, P22681 Function: Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The Tyr-731 phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function Human promoter reporter construct: transfection-ready on this site you can add luciferase reagents to your shopping cart......hmmmmmm..as well as control vectors... switchgeargenomics.com/genecards.php?id=707425
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do we need to re-look at this?
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