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The Fiber Disease

Human Anatomy, Physiology, and Medicine. Anything human!

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Postby mfromcanada » Mon Sep 11, 2006 12:04 am

Antibitotic "Doxycycline" does not eradicate the organism. I took for over 1 1/2 years. It certainly made me feel better. I believe it reduced overall inflamation. In time I came down with Rosacea and fungal infection in mouth. Had to stop antiobiotic. My weight goes up and down rapidly and I now wonder if it has to do with the number of these things infesting the entire body. My weight can fluctate as must as 30% of the overall.
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Postby tamtam » Mon Sep 11, 2006 12:17 am

Best is to understand that most people have tried various combinations or long courses of anti microbial agents without being able to eradicate this infection.

Because of this fact it is likely that a trypanosome has been used. Infection eradicated, patient has died! This counts in africa until today...

About weight;

As far as I do remember doxycycline is an additive to e.g chicken and pig feed. It causes rapid gain of weight (growth promotor)
Swine practice///

Tetracycline resistance
Tetracyclines (tetracycline, doxycycline, minocycline, oxtetracycline, . ... human and veterinary medicine but also as growth promotor in animal husbandry. ...
http://www.antibioresistance.be/Tetracy ... u_Tet.html - 9k - Cached - Similar pages
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Postby London » Mon Sep 11, 2006 1:17 am

Sky (and all) you say if we keep our bacteria down, we can keep the worm down. I was wanting your opinion of whether you think you have a true worm parasite (filarial, Oncho....) Or do you think like I do and think they are alll just synthetic......?

As I said a couple of times before, there is a lot of informaion out on the parasitoid wasp, their toxins on the TG plants, the bee mites, etc.,,,,but if
I had to pick out just one about this aspect of our illness: (the wasp part)

I think the fact that the grain/wheats stored in a warehouse unopened
crates has done the most havoc. Remember, there is an organism that does indeed wrap itself in fibers...

Also, they have used the yeast S cervechei. That;s a fact. And, I dunno if anyone read it (maybe Systemic did) where I posted one that talked about the aspergillis spreading thru Cotton.....so now that would make the candida a part of this. I know that Strep is going to be involved.

Right now, my body shows signs that I have polycythremia vera>>>and NO cure....

Hey Sky, the CDC has Had the wolbachia on it's website for a couple of months now It is under recently emerging diseases......basically, it says this.....that the wolbachia causes Cytoplasmic I....gets into 12 insects...the main one id the flea, the mites, the head lice, etc. Says itwill show itself in 1 of 4 ways

trench fever, a???(heart prob;), CAT-SCRATCH disease>>>>they all all one and the ame >>>>>then, that is another name for AIDS.

Oh hell yeah, I think they are involved (the wasp) but if it did cause this murine Typhus in me> well it showed up 12 mo. lATER, NOt THE ususal 6 days,,,,,, My left forearm is still broke out....How can an insect do my arm like this for 8 Months? I don't think it can, ut I donno.,

It is in the water system, or A?C heat system perhaps as well as the lab


Hi, you asked about how to kill it if this think is antibiotic resistant. ( I never said it was that, but I did say that they are releasing these insecticide resistant pathengens....). Hey, So you are from Sliddel?
Was man-made hurricane not 0bvious of the racist F-sticks we have in running this country......You know, we v
Last edited by London on Mon Sep 11, 2006 1:18 am, edited 1 time in total.
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Postby Nadas Moksha » Mon Sep 11, 2006 1:18 am

man ....
who in the hell is this "sara" ... i mean damn if this is an example of what comes out of the US medical institutions we ARE DOOMED!!!!!!!!!

her narrowminded, self indulgent perspective on another persons illness has got me googling casket prices. anybody check ebay for grave plots?

and tamtam calm down you are right the communist intervention is real but dont go thrashing your statesmen, Sky troll is on our side, infected or not.

and is there any other case in history that assures us that tams approach will work?

gees how much money are we talking....
cause half the technical procedures could be done at the university by undergrads and as long as we keep the whole adgenda in pieces we wont go down the same path MRF , you know with a few gov. moles to absorb resources with bunk resources to avoid these AMA creeps.

im thinking we should cut off all corrispondance to CDC,AMA,NIH,US GOV.....set array Black Widow Bots on shifting proxy at slow bit rates on their networks get a few in recon and DATA MINE those who DATA MINE us!!!!!!!!!!!!

if they dont shut down the net..... . we could have incriminating evidence within a week .....
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Postby Nadas Moksha » Mon Sep 11, 2006 1:38 am

what do we have here?.....
until now they were working in the wet lab as molecular biologists and biochemists, now their work will be carried out on computers. Another issue is that the diffraction experiment is within the domain of physics, and while physicists and chemists might be familiar with it, biologists, who were the majority, felt uncomfortable. The students and/or PIs carried out data processing of the oscillation images of those crystals that had interpretable diffraction with close and extensive supervision. They were taught not only how to run the programs, but also the ideas behind them: notions of real and reciprocal space, the physics of diffraction, reflection's intensities and indices, the concepts of unit cell, asymmetric unit, space group, integration, scaling, merging, etc.

Phase determination / structure solution was usually a straightforward procedure since most of the structures were solved by molecular replacement. The only exception was a hypothetical protein (''f'' in Table I) that was solved by multiwavelength anomalous dispersion (MAD). This rather interesting case demanded extra input from the particular group such as growing selenium methionine protein crystals and is described in another part of this manuscript. Structure building and refinement is a procedure that still demands weeks and perhaps months of work. This was accomplished by having the people from the network coming over to the CeBiME for these periods of time. This part helped the students to learn about the protein databank format, atom coordinates, R factor, temperature factor, electron density and many other concepts. Structure analysis would be the final step and as the groups moved towards this, it could be foreseen that difficulties arose when trying to explore completely unrelated structures. Here, there is no clear path to be followed, except for comparing the structures to their homologues when they are present. In most cases some unique features of the proteins will need to be addressed, such as: why is the lysozyme (''b'' in Table I) capable of working in a basic pH, what is the information that the hypothetical protein (''f'') can give about its function or what makes the infestin 4 (''j'') such a good inhibitor of blood coagulation-cascade factor XIIa.
Last edited by Nadas Moksha on Mon Sep 11, 2006 1:48 am, edited 2 times in total.
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Postby Nadas Moksha » Mon Sep 11, 2006 1:39 am

holy defractions sky troll what do we have here?.....

these students are playing with bio crystallization, common for weaponized pathogens........................


Trypanosomes have a unique RNA processing mechanism and translation initiation control, which therefore constitute interesting drug targets. Most of the genes are transcribed as polycystronic units that are processed by trans-splicing and poly-adenylation. All mRNAs receive a 30-40 nt-capped RNA derived from the splice leader gene in the 5' terminal ends (Gull 2001). Both the cap structure and the enzymes involved in the cap synthesis are different in trypanosomes as compared to mammalian enzymes. For example, a guanilyl transferase of T. brucei has an extra N-terminal portion (Silva et al. 1998) that seems to carry an adenylate kinase domain. The RNA triphosphatase activity is also catalyzed by an unique enzyme (Ho and Shuman 2001). Therefore we selected as targets for structural studies the RNA adenosine triphosphatase from T. cruzi and T. brucei. These enzymes have been cloned, expressed in E. coli, purified, and submitted to crystallization assays. Three conditions were found promising and are used in refinements.

Two targets were also selected for proteins involved in the translation initiation control of trypanosomes. One is the eukaryote translation initiation factor 4E of T. brucei (TBeIF4E), which is the cap-binding protein. It has 251 amino acids and was chosen as a target for two reasons: a) it has only 24% similarity to the mammalian counterpart, thus representing an interesting drug target; b) the structures of the mammalian and yeast homologues have been determined (PDBs:1L8B, 1EJ1, 1AP8), which might help in the analysis of this protein. TBeIF4E was cloned in pET28a, expressed, purified and submitted to crystallization screenings. The other target was the eIF2a of T. brucei. It is a 419 amino acid protein that contains an extension of ca. 120 residues in the N-terminal relative to all other known eIF2a sequences. The same extension is present in T. cruzi and Leishmania major. The complete ORF as well as only the N-terminal half was cloned into pET28a and the protein expressed, purified and submitted to crystallization assays.


We are also interested in the structure of merozoite surface proteins (MSP) of Plasmodium sp, most of them involved in the erythrocyte and reticulocyte invasion. Merozoites correspond to blood stages of the Plasmodium species released by infected cells. These studies can help understanding the biology of these organisms and designing potential agents to block its growth. We have focused on fragments of these major surface proteins, as the entire proteins are too large and insoluble when produced in recombinant form. We expressed fragments corresponding to the C-terminus of MSP3a and the N and C terminus of MSP3b based on the formation of coiled-coil structure as demonstrated (Galinski et al. 1999). Five recombinant proteins were obtained in fusion with His-tags and purified by affinity chromatography and ion exchange. MSP3a e MSP3b have been produced in appropriate levels, purified and submitted to crystallization assays.

We adopted as a general strategy in SmolBNet to select protein targets exclusively related to our current research lines. In a few cases we were successful; this is the case of the trialysin peptides solved by NMR and the serine protease inhibitors solved by diffraction studies. For most of the chosen targets we failed in obtaining structural data,
http://www.scielo.br/scielo.php?script= ... 6000200006
Anais da Academia Brasileira de Ciências - The structural molecular biology network of the State of São Paulo, Brazil

Last edited by Nadas Moksha on Mon Sep 11, 2006 2:13 am, edited 1 time in total.
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Protease and Morgellons

Postby WLR » Mon Sep 11, 2006 1:44 am


Thank you for the welcome. I hope I will be able to offer something to this forum instead of just ask questions.

On the subject of protease, I find it strange that since protease digest protein and insects are protein that they not only continue to thrive in my body but they love the stuff. It leads me to believe that it is the bacteria that poses the greatest risk to our health but yet it seems to be highly resistant to drugs as well as alternative therapies. Is the bacteria protecting the parasite then and or is it the other way around? Do they both give something to the other to survive in our bodies?

I have been able to eliminate all symptoms of this disease and have done it four times on purpose. Each time I get the same results. The first time I was symptom free it took me almost a month to remove all symptoms but when I stopped the treatment it only took 2 days for the biting, lesions and crawling sensations to return. The second time I stopped the treatment it took 3 days for the same symptoms to return and 7 days to stop them again and I repeated that 2 mores times successfully. Then I had increased the protease and within 2 hours the same symptoms returned even though I was still on the treatment but I was able to eliminate them again in 3 days after stopping the protease. To make sure it was the protease 2 days later I took the same dose of protease again along with the treatment and within 2 hours the same symptoms returned. This time it took me 4 days to remove all symptoms. Is it the amount of protease or just protease? I was on a pancreatin formula which supplied 40 mg of Amylase, Lipase and Protease and was able to remove all symptoms with my treatment while on that. The question is was that an acceptable amount to take without increasing my symptoms or was even that amount causing problems and I just had not recognized it yet?

Sorry if I affending anyone with my crack about doctors. Maybe I have just had the wrong doctors. Then again maybe not. Ha HA Ha Sorry.

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Postby Skytroll » Mon Sep 11, 2006 1:50 am

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Postby Skytroll » Mon Sep 11, 2006 2:04 am

911 story and filming by one brave soul, showed firemen and in one instance one fireman said to another, to wipe the fibers out of his eyes. It was the brother of the filmer. He was WASHING FIBERS OUT OF HIS EYES.
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Postby Nadas Moksha » Mon Sep 11, 2006 2:05 am

any need a shovel ?

cause man we got a lot of dirt......................

The principal activity which drives microbivore scaling and design is the process of digestion of organic substances

"the nanorobotic device brings their surfaces into intimate contact, allowing reversible binding sites on the microbivore hull to recognize and weakly bind to the bacterium. Binding sites can already be engineered [77, 78]. Bacterial membranes are quite distinctive, including such obvious markers as the family of outer-membrane trimeric channel proteins called porins in gram-negative bacteria like E. coli [79, 80] and other surface proteins such as Staphylococcal protein A [81] or endotoxin (lipopolysaccharide or LPS), a variable-size carbohydrate chain that is the major antigen of the outer membrane of gram-negative bacteria. Mycobacteria contain mycolic acid in their cell walls [82]. And only bacteria employ right-handed amino acids in their cellular coats, which helps them resist attack by digestive enzymes in the stomach and by other organisms. Peptidoglycans, the main structural component of bacterial walls, are cross-linked with peptide bridges that contain several unusual nonprotein amino acids and D-enantiomeric forms of Ala, Glu, and Asp [83]. D-alanine is the most abundant D-amino acid found in most peptidoglycans and the only one that is universally incorporated [84]. Macrophages have evolved a variety of plasma membrane receptors that recognize conserved motifs having essential biological roles for pathogens, hence the surface motifs are not subject to high mutation rates; these pathogen receptors on macrophages have been called "pattern recognition receptors" and their targets "pathogen-associated molecular paterns"anchorage between the nanorobot and the bacterium assuming a single-lipid extraction force of ~1 pN [1]. In the case of gram-negative bacteria, a footpad with binding sites for ~3 murein-linked covalently attached transmembrane protein molecules would provide a secure 120-480 pN anchorage, assuming 40-160 pN/molecule and ~9 such molecules per 1000 nm2 of microbial surface (Section 3.1.1). In either case, undesired adhesions with bacterial slime must be avoided. The footpad tool is rotated into, or out of, an exposed position from behind a protective cowling, using countercoiled internal pull cables.

The tiniest bacterium to be digested may be ~200 nm in diameter (Section 2.1.4), but the smallest virus can be only ~16 nm wide (Section 2.2). Since the work envelopes of adjacent grapples picking particles bound to the hull surface extend 150 nm toward each other from either side, the maximum center-to-center intergrapple separation that permits the ciliary transport of 16 nm objects is ~300 nm. This requires 1 grapple per 0.09 micron2 of nanorobot surface, for a total of 277 grapple silos uniformly distributed over the entire 26.885 micron2 microbivore outer hull, excluding the two 1-micron2 port doors. (One or more grapple-containing bridges across the annular exhaust port aperture (Section 3.1.4) may be necessary if it is desired to transport targets <200 nm in diameter from the circular DC exhaust port island to the main grapple field of the microbivore, allowing subsequent transport to the ingestion port inlet; such bridges are not included in the present design.) During transport, a bacterium of more typical size such as a 0.4 micron × 2 micron P. aeruginosa bacillus may be supported by up to 9 grapples simultaneously. "

Microbivores: Artificial Mechanical Phagocytes using Digest using Digest and Discharge Protocol

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Postby Nadas Moksha » Mon Sep 11, 2006 2:32 am

sunday closet cleaners group presents:
Heres a new one on me ..... the iron and p.aeruginosa connection.....

It has been reported that lactoferrin can cause
deprivation of iron, thus inhibition of biofilm formation in Pseudomonas aeruginosa[/size].
We have observed that biofilm
formation can be blocked using iron chelators such as lactoferrin, EDTA(ethylenediaminetetraacetic acid), and EDDS
(ethylenediaminedisuccinic acid).
Project Leaders:
Janice D. Thomas and Jeffrey H. Toney
Department of Chemistry and Biochemistry
Montclair State University
Montclair, NJ 07043
The shuttle DNA vector pSP3 was constructed to generate mutations by DNA insertion. This construct can replicate in E. coli and in Xylella fastidiosa (Xf). If a DNA fragment containing part of the Xf rpfA gene encoding for aconitase is cloned into pSP3, specific integration of this construct into the rpfA gene will be induced. Previous results with the Xf xpsD gene, using a pSP3(xpsD600) construct, indicate that this vector is useful in generating gene disruption by homologous recombination. We are currently investigating the potential role of the rpfA gene in biofilm production using this gene
disruption technique.
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