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The Fiber Disease

Human Anatomy, Physiology, and Medicine. Anything human!

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Postby nettimo » Wed Oct 25, 2006 6:52 pm

Sabrina,
Thank you for your letter to NY Times. Talk about a negatively-leading "news" article. This discrimination hurts. Again, I hate to say it but I wish this on all doubters; not to suffer, but just to KNOW the truth.

Sky,
Thanks for all the research. I, too, have wondered about the function of different colored fibers, but my experience does not match your musings. Twice I SAW blue fibers move. Most recently a tiny one, requiring magnification, I SAW MOVE THRU WATER, by touching end-to-end. It was definitely motile, while a couple tiny reds, tiny blues, and a longer blue did not move. (I had brushed off whatever was causing a biting sensation from my forearm.)

I have been watching these things for six months, with magnification from 5x up to 400x (and occasionally 1000x). Months ago I SAW a blue fiber move on a slide (on uneven surface, the solution drop dripped 1/4"). Much to my surprise (and not), it lifted one end, waived it back and forth, then up and down like an inchworm, as if trying to lift the back end.

I had already experienced dozens of pairs CRAWLING (or however they locomote) out of my nose and onto my forehead, chin, cheek, nose. neck then drop to my arms. I once saw an article online months ago (not referenced in a journal) surmising that in some parasitic forms, the red one provides nourishment (blood supply) and the blue the mobility. As I have often seen mine in pairs in most of my body fluids, this seemed to be worth consideration.

Furthermore, when I placed a long "suspicious hair" in June in a small specimen vial in solution, a week later there were MANY TINY COLORED fibers in the vial as well, obviously coming from the unusual "hair." I recalled Tam reporting that the "hair is a pathway." Last time I looked at this vial the colored fibers were now LARGER and WHITISH/clear.

I have also seen the clear/whitish hairline ones wrap around grasses in my house (making me recall the farmers who had an outbreak). I have wondered about PYTHIOSIS INSIDIOSI, rather than Protothecosid. When my shower drain was clogged, I would find plantlike material enmeshed with hair and fibers. (I have some photos of this.)
Tam, has this been ruled out?
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Postby Nadas Moksha » Wed Oct 25, 2006 7:03 pm

Increasing Robustness in the Bio-Networking
Architecture: A Distributed Approach

The Bio-networking architecture, which uses
biologically-inspired methods for developing scalable
and adaptive network applications, is being developed
under Dr. Tatsuya Suda at UCI. Inspiration is drawn in
particular from large-scale systems, such as ant and wasp
colonies
. Mobile agents, called Cyber-Entities (CEs),
form the architecture and provide services to users in
return for “energy.” One of the issues under
investigation is how to make the architecture more
robust and adaptive. I have developed a model derived
from market economies to constantly propagate
information about population and energy-supply
distributions among CEs, called Price Propagation, to
ensure that more efficient reproductive and migratory
behaviors emerge. CEs continually inform each other
about prevailing conditions in their region. Using this
information, they get a sense of energy supply and
demand trends over the platform and base their
reproductive and migratory decisions on it. This is
similar to how prices are used as indicators of supply and
demand in market economies. A detailed simulation of
Price Propagation has been conducted, with encouraging
results. In all, it is hoped that when these ideas are
adapted fully into the development of the Bio-
networking architecture, we will observe near best-case
performance by the CEs.

Development of an Efficient Variable Optical
Attenuator (VOA) Using a Single-Mode Fiber with
Reduced Acoustic Reflection

There is a growing need for a fast tuning Variable
Optical Attenuator (VOA) in a dynamic optical network
with applications in optical blocking and gain
equalization. Currently, VOAs are realized in
microelectromechanical systems (MEMS) and silicon-
on-insulator (SOI) waveguide. The fast-tuning VOA
described in this work is based on a broadband all-fiber
acoustic optical tunable filter (AOTF), which has near-
zero insertion loss and is free of optical alignment. The
operation of a single-mode fiber (SMF) AOTF is
characterized by the coupling between the core and
cladding modes. By reducing the cladding diameter of
the fiber to 21um through chemical etching in a HF
acid solution, and by incorporating a tapered region
between the etched and unetched sections of the fiber to
reduce the acoustic reflection, both ultra-broadband and
large attenuation is achieved, enabling the best
attenuation of 65 dB compared to previous results of
18 dB. Cooking oil and soldering oil coatings were also
found to reduce acoustic reflection in the fiber but with
an increase of noise due to its non-uniformity. These
results indicate the dependency of acoustic reflection on
fiber cladding diameter and uniform material coating. The
experimental results show that a VOA based on
acousto-optic coupling on a cladding etched SM fiber
can be achieved by optimizing these parameters.

http://www.urop.uci.edu/symposium/past_ ... am_a-g.pdf
program_a-g.pdf (application/pdf Object)
http://www.patentstorm.us/patents-by-da ... 02-16.html
Patents by Date - PatentStorm - May. 02, 2000
-nadas
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Postby tamtam » Wed Oct 25, 2006 7:58 pm

Correction:


Try: google images
Search query: wing veination or wing venation
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Postby Barz » Wed Oct 25, 2006 8:41 pm

Try Google: Dek Woolfson
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Postby tamtam » Wed Oct 25, 2006 9:24 pm

Oilgae is an introduction I did not know about.
But it would link to e.g mesocosm experiment.

0.3 en-US https://www.blogger.com/atom/3715422 service.post Oilgae ...
If you are unfamiliar with wiki software, please refer to our help section. ... Typically, Synechococcus dominates the smaller picoalgae size class; ...
http://www.oilgae.com/blog/feed/atom.xml - 339k - Cached - Similar pages
[ More results from http://www.oilgae.com ]

However,

If you keep on making associations with a model organism you can end up
in nearly every scientific field.
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Postby Barz » Wed Oct 25, 2006 11:45 pm

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Postby Nadas Moksha » Thu Oct 26, 2006 12:47 am

due to the never ending phase shifting wormhole continuum my effort may once again be out of context ... . . . ahh..

Vibrio vulnificus Secretes a Broad-Specificity Metalloprotease Capable of Interfering with Blood Homeostasis through Prothrombin Activation and Fibrinolysis

http://jb.asm.org/cgi/content/full/187/20/6909?etoc


Vibrio vulnificus is a causative agent of serious food-borne diseases in humans related to the consumption of raw seafood. It secretes a metalloprotease that is associated with skin lesions and serious hemorrhagic complications. In this study, we purified and characterized an extracellular metalloprotease (designated as vEP) having prothrombin activation and fibrinolytic activities from V. vulnificus ATCC 29307. vEP could cleave various blood clotting-associated proteins such as prothrombin, plasminogen, fibrinogen, and factor Xa, and the cleavage could be stimulated by addition of 1 mM Mn2+ in the reaction. The cleavage of prothrombin produced active thrombin capable of converting fibrinogen to fibrin. The formation of active thrombin appeared to be transient, with further cleavage resulting in a loss of activity. The cleavage of plasminogen, however, did not produce an active plasmin. vEP could cleave all three major chains of fibrinogen without forming a clot. It could cleave fibrin polymer formed by thrombin as well as the cross-linked fibrin formed by factor XIIIa. In addition, vEP could also cleave plasma proteins such as bovine serum albumin and gamma globulin, and its broad specificity is reflected in the cleavage sites, which include Asp207-Phe208 and Thr272-Ala273 bonds in prothrombin and a Tyr80-Leu81 bond in plasminogen. Taken together, the data suggest that vEP is a broad-specificity protease that could function as a prothrombin activator and a fibrinolytic enzyme to interfere with blood homeostasis as part of the mechanism associated with the pathogenicity of V. vulnificus in humans and thereby facilitate the development of systemic infection.
Artificial antisense RNAs
The discovery of natural antisense RNA systems led to the idea of using artificial antisense RNAs as a means to control gene expression by specific inhibition of target RNA function. The first reports to demonstrate such an effect in prokaryotes and eukaryotes appeared in 1984 (Coleman et al., 1984; Izant & Weintraub, 1984). Since then, two different approaches have evolved. First, the use of exogenous short (15-25 bases), synthetic oligonucleotides, designed to hybridise to specific sequences of target mRNAs via Watson-Crick base pairs and predicted to act mainly by degradation of targeted mRNA by an RNase H mediated mechanism (Varga et al., 1999). Second, the use of endogenous antisense RNAs, transcribed from DNA cloned in antisense orientation, which possibly fold into higher order structures and act on their target sequences as such (exemplified by one of the earliest artificial systems reported in Coleman et al., 1984 and Green et al., 1985). Both methods have met with successes and setbacks. Important factors to consider, when using oligonucleotides, are e.g. stability, toxicity and delivery, while antisense RNA approaches are more difficult to control because these molecules are often longer and may adopt complex structures. Also, the inhibitory effect may depend on whether intracellular host proteins will support or counteract the binding between antisense and target RNA molecules. Continuous developments and modifications of both lines are being made, mainly in the light of new insights innatural occurring regulatory RNAs
Filamentous phage

The filamentous phage constitute a large family of bacterial viruses, which infect a variety of Gram-negative bacteria, using pili as receptors. The Ff group, including the virtually identical strains M13, fd and f1 and their derivatives, is the most frequently used for phage display purposes. The phage capsid appears as a thin and flexible tubular structure of about 900 x 10 nm (figure 1). The single-stranded DNA genome is composed of approximately 6400 nucleotides from which 11 proteins are encoded. A non-coding intergenic region contains the signals for initiation of DNA synthesis, for termination of RNA synthesis, and the packaging
signal. Although different designations have been assigned to the phage genes and proteins, the one used throughout this thesis applies Roman numerals e.g. gIII and pIII for gene III and protein III, respectively. Five coat proteins encompass the circular genome, three proteins are needed for DNA synthesis (pII, pV, and pX), and three others are involved in phage assembly and export (pI, pIV, and pXI). The phage coat consists mainly of pVIII, present in approximately 2800 copies. About five copies each of the minor coat proteins are located at the particle ends.
Protein III and pVI are at the end involved in infection, and both are required for particle stability. Protein VII and pIX, necessary for efficient particle assembly, are at the other end (reviewed in e.g. Russel, 1995 and Russel et al., 1997). The negatively charged amino-terminal (N-terminal) regions of mature pVIII molecules
are exposed on the outer surface of the virion, whereas the carboxy-terminal (C- terminal) segments line the cylindrical hole generated by the protein sheath in which the DNA is contained. An apolar domain in the interior of the pVIII molecule hydrophobically interacts with corresponding domains of other pVIII molecules, to hold the capsid subunits together (Glucksman et al., 1992; Marvin et al., 1994). Also, similar apolar domains are found in all four minor coat proteins
suggesting that they are associated with the pVIII sheath in the same way as pVIII molecules are associated to each other. Protein VII has been proposed to interact with the pVIII array and to be shielded from the environment, whereas pIX interacts with pVII and is exposed to the environment. The pIII and pVI proteins form a stable entity in the virion (Gailus & Rasched, 1994). The C-terminal end of
pVI in the virion is not accessible to anti-pVI serum (Endemann & Model, 1995), still, structural data suggest that it is exposed to the surrounding medium. (Makowski, 1992).

Plasma and extracellular matrix proteins shown to promote S. aureus attachment to coated polymer surfaces Host protein



http://diss-epsilon.slu.se/archive/0000 ... /Kappa.pdf

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Postby London » Thu Oct 26, 2006 1:28 am

Skytroll,

Hi, have not been here in 24 hrs and just seeing your post. Oh hell yeah, I'm tallking about C3......get this:

or google it as you guys were doing: C3-fibres

This is it but it's not the main one. The maiin one is made from a honeycomb like shape and it hardens up after water....does not get and stay soft like the others.

Yes, there is more and yes, for a fact., we have been given markers.

These f-ers have put electromagnetic or maybe electrochemical fibers in us. The only thing I have seen, yet it stated it in a very nanchalant way

was that some people do already have the fibres if they were considered high risk.

Well who the hell are they? If it's the gov't or law inforcment they are the HIGH RISK ones. Liars and criminals.

Whoever did it was wrong and evil and should be destroyed. I'm not off on one of my tangents either. Very mild and calmly I just stated the truth. Now how f-ing stupid do they think we are....to have the gd audacity to put the FBI on national tv and say they could not find anything in their database.

What, they did not have polmer (sp?) in their database? Most people just sat their and did not stop to think that maybe something was fishy about that???? what? They did not have fiber optics in their database?

Lucent and Bell should be a good sport and take their lil buddies they paid off to lie some fiber optics THEN see if we have a match.

Yes, Nadas, I did just see (glancing) that you posted about the internet/computer and that is good to knowl.....b/c that is all this **** is.

It's friggin mems. They are burning the retina/cornea of our eyes and going that way., You can do a nerural interface or they can put the disease right down on the new chip.

It;s the film in it that is causing the radiation burns. Hey, Nadas, I gotta run but I will get back and read your post later tonight.
*************************

Lady Sabrina,

Thanks for posting all that. I could not make it open last night but did so manage to today.

One thing the article said that caught my attention was:

While much has been made of the Internet as a medium for psychological support, experts have only begun to ponder its potential for spreading delusional thinking.

hehehe yes it can do that but I do not think it is us that has the delusion, know what I mean?

These people are hiding b/c they want to run and ruin the world at the same time. They can manipulate the weather, change voter's already cast ballot, or they can steal money off the lotteries by all hooking their lil laptops up and rigging it. Just the F. like they did at that warehoiuse in Scotland, eh boys? Oh, I know.....remember the Celadian (sp?) Games?

Anyway, my opinion is this:

The organisms in question are endosymbionts, free-floating cells that take up residence inside of animal cells, forming a symbiotic relationship. Apparently some of these species have extremely tiny genomes. So genomes on the internet. Why and how did they pick us?

Saturday I was reading this jewish guys postings and he said they did it, the computer graphic guys b/c they are pissed at America for not helping them all of these years and ruining their country with our Western highrises, etc. Just and FYI to you all.

But in 2001 they said there was an internet worm that effected 400.000 computers w. in a matter of three hours and that this worm could not be stopped. Did you all hear that ? I just read it the other day and did not know about it.


I do.!!!!

Later all.

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Postby RANDY » Thu Oct 26, 2006 1:55 am

Barz,
We are getting all the states to follow Jane's lead and have a national agency that will keep the CDC honest. You sound very bitter btu you have done nothing to help. It is like complaining about the results of an election when you never even voted.
Randy

You want to be in charge of your state or just want to rank on Rutz?
During the End Times, Good will battle Evil. Where do you stand?
http://unknownskindisease.com
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Postby Barz » Thu Oct 26, 2006 2:47 am

My state is spoken for. I followed up with a letter to my senator.
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Postby tamtam » Thu Oct 26, 2006 9:17 am

Identifying Protein Interactions

While it is convenient to think of proteins as discrete and independent molecules, this is actually an oversimplified view. Many proteins require other proteins or cofactors for activity; and proteins involved in signal transduction, protein trafficking, cell cycle, and gene regulation must interact with other proteins in those processes. Many of these interactions require particular domains called interaction domains. Proteins involved in the interactions contain combinations of interaction domains (for interaction with other proteins) and catalytic domains (for function of the protein). The interaction domain can bind the partner protein, even in the absence of the rest of the protein. Interaction domains are often quite versatile, capable of binding a variety of related ligands. In addition, one protein may contain several different interaction domains. The modular nature of these domains allows the protein to interact with multiple target proteins in the cell; thus it provides a mechanism for integration and control of information from protein to protein in a cell. Such protein-protein interactions form the basis for our current understanding of cell signaling pathways and protein networks that regulate all the activities in a cell.

Because protein-protein interactions regulate the activities of cells, identifying them is critical to understanding cellular processes. Mass spectrometry techniques have been developed for large-scale screening to identify interacting proteins. For example, hundreds of known proteins in yeast were engineered to contain a biochemical tag that would allow the tagged protein to be separated from other proteins in a cell extract. This was done gently so that other proteins bound to the tagged protein would still be attached. The tagged protein, along with any associated proteins, was then analyzed by mass spectrometry. The results revealed that about eighty-five percent of these proteins were associated with other proteins. Although most interacted with many other proteins, in some cases two different protein complexes had at least one protein in common. Among the most intriguing questions to come out of this research were what controls which proteins interact and - for those that interact in multiple complexes - how do these proteins know which complex to join?

Help your self website:

http://images.google.com/imgres?imgurl= ... D%26sa%3DN

------------------------------------------------------------------------------------

The Extracellular Matrix (ECM)

While it is true that all living things are made of cells, that is only part of the story. Most of the cells in multicellular organisms are surrounded by a complex mixture of nonliving material that makes up the extracellular matrix (ECM). In some cases, the ECM accounts for more of the organism's bulk than its cells.

Examples:


http://users.rcn.com/jkimball.ma.ultran ... E/ECM.html

http://web.indstate.edu/thcme/mwking/ex ... atrix.html

----------------------------------------------------------------------------------

New video footage at Google Video (reference 001)
Updated with a few minutes.

http://video.google.com/videosearch?q=s ... rbug&hl=en
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Postby Sabrina » Thu Oct 26, 2006 12:45 pm

Thank you Tamtam. I will pass on the information that you have updated your new video.

I see the importance of your above post, once again.

Peace,
Sabrina
:D
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