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Post by skyship on Nov 5, 2013 0:11:34 GMT -5
Molecular design of artificial fibrin glue ....."A totally synthetic fibrin glue was developed. The molecular structure is a copolymer composed of N-isopropyl acrylamide (NIPAM) units and vinyl monomer units which has a cell-adhesion peptidyl moiety (Arg-Gly-Asp- in the side chain. The buffer sollution is viscous and transparent at room temperature, but on elevation to physiological temperature, sponteneous precipitation occurs owing to a thermoresponsive phase transition derived from the NIPAM unit. On mixing with platelet-rich plasma, the peptidyl moieties bound to platelet receptors. When applied to living tissues, spontaneous precipitation and subsequent platelet aggregation occurred, indicating that the synthetic bioactive polymer effectively functions like fibrin glue. This indicates that the water-soluble copolymer developed here, which incorporates thermoresponsiveness and cell adhesivity, biomimics fibrin glue.www.sciencedirect.com/science/article/pii/092849319390007P
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Post by skyship on Nov 5, 2013 0:22:01 GMT -5
dimers, D-dimers, artificial fibrin glue These results emphasize the need for physicians to recognize that D-dimer assays have unique performance characteristics. Clini- cians need to be aware of the performance characteristics of the particular D-dimer test in use at their institution, because the D-dimer analyte is not a simple structure with a uniform composi- tion. The cutoff value used to exclude venous thromboembolism (VTE) needs to be confirmed by the clinical laboratory. Alterna- tively, the institution should use an assay that has been previously validated in clinical studies............. D-dimer antigen: current concepts and future prospects - Blood bloodjournal.hematologylibrary.org/content/113/13/2878.full.pdf
by SS Adam - 2009 - Cited by 120 - Related articles highly self-adhesive fibrin monomers after thrombin cleavage.1 A ... products of crosslinked fibrin containing D-dimer and fragment E ...... Synthetic peptide de-.PDF] TISSEEL - Baxter www.baxter.com/downloads/healthcare_professionals/.../Tisseel_PI.pdf Related articles Dec 3, 2012 - Hemostasis: TISSEEL is a fibrin sealant indicated for use as an adjunct to hemostasis in ..... increased D-Dimers may result at least partly from the degradation of Fibrin Sealant. ... Aprotinin (Synthetic) is manufactured by solid.
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Post by skyship on Nov 5, 2013 0:37:49 GMT -5
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Post by skyship on Nov 5, 2013 0:53:50 GMT -5
dityrosine-linked Aβ dimers are implicated in the progression of AD. tyrosine is being substituted with these toxic oligomers~! ======================= Genetic predictors of fibrin D-dimer levels in healthy adults PubMed Central Background Fibrin fragment D-dimer is one of several peptides produced when cross-linked fibrin is degraded by plasmin, and is the most widely-used clinical marker of activated blood coagulation. To identity genetic loci influencing D-dimer levels, we performed the first large-scale, genome-wide association search. Methods and Results A genome-wide investigation of the genomic correlates of plasma D-dimer levels was conducted among 21,052 European-ancestry adults. Plasma levels of D-dimer were measured independently in each of 13 cohorts. Each study analyzed the association between ~2.6 million genotyped and imputed variants across the 22 autosomal chromosomes and natural-log transformed D-dimer levels using linear regression in additive genetic models adjusted for age and sex. Among all variants, 74 exceeded the genome-wide significance threshold and marked 3 regions. At 1p22, rs12029080 (p-value 6.4×10?52) was 46.0 kb upstream from F3, coagulation factor III (tissue factor). At 1q24, rs6687813 (p-value 2.4×10?14) was 79.7 kb downstream of F5, coagulation factor V. At 4q32, rs13109457 (p-value 2.9×10?18) was located between 2 fibrinogen genes: 10.4 kb downstream from FGG and 3.0 kb upstream from FGA. Variants were associated with a 0.099, 0.096, and 0.061 unit difference, respectively, in natural-log transformed D-dimer and together accounted for 1.8% of the total variance. When adjusted for non-synonymous substitutions in F5 and FGA loci known to be associated with D-dimer levels, there was no evidence of an additional association at either locus. www.science.gov/topicpages/f/fibrin+d-dimer+levels.html
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Post by skyship on Nov 5, 2013 1:14:09 GMT -5
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Post by skyship on Nov 5, 2013 2:06:25 GMT -5
dityrosine-linked Aβ dimers We as researchers of the govt. sci researchers can now see the problem with the sci researchers.The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothesThe ' toxic Aβ oligomer' hypothesis has attracted considerable attention among Alzheimer's disease researchers as a way of resolving the lack of correlation between deposited amyloid-β (Aβ) in amyloid plaques—in terms of both amount and location—and cognitive impairment or neurodegeneration. However, the lack of a common, agreed-upon experimental description of the toxic Aβ oligomer makes interpretation and direct comparison of data between different research groups impossible. Here we critically review the evidence supporting toxic Aβ oligomers as drivers of neurodegeneration and make some suggestions that might facilitate progress in this complex fieldThe 'toxic Aβ oligomer' hypothesis has attracted considerable attention among Alzheimer's disease researchers as a way of resolving the lack of correlation between deposited amyloid-β (Aβ) in amyloid plaques—in terms of both amount and location—and cognitive impairment or neurodegeneration. However, the lack of a common, agreed-upon experimental description of the toxic Aβ oligomer makes interpretation and direct comparison of data between different research groups impossible. Here we critically review the evidence supporting toxic Aβ oligomers as drivers of neurodegeneration and make some suggestions that might facilitate progress in this complex field. Figure 1: Generation of Aβ from amyloid precursor protein. Generation of A[beta] from amyloid precursor protein.
The sites of β- and γ-secretase–mediated cleavage are indicated with arrows, and the transmembrane domain of APP is highlighted in gray. γ-cleavage produces a pool of Aβ fragments that vary in length and hydrophobicity. The mutations i… www.nature.com/neuro/journal/v15/n3/carousel/nn.3028-F1.jpgFigure 2: Size overlap in major natural and in vitro–generated Aβ oligomers. Size overlap in major natural and in vitro-generated A[beta] oligomers. Note that dimers and amylospheroids—both Alzheimer's brain–derived species—are located at opposite ends of the spectrum. The Aβ preparation called ADDL (Aβ-derived diffusible ligands), may encompass the Aβ species known as low n-mers,… www.nature.com/neuro/journal/v15/n3/carousel/nn.3028-F2.jpgwww.nature.com/neuro/journal/v15/n3/full/nn.3028.html?WT.ec_id=NEURO-201203
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Post by skyship on Nov 5, 2013 3:22:53 GMT -5
nano-dimer or nano monomers. it all begins with the monomer.
It is known that Pd bulk crystal absorbs hydrogen in the lattice. One can expect that the electronic structure of Pd is affected by hydrogen adsorption. This means that plasmon resonances of Pd nanostructures may be changed by hydrogen adsorption. Hence, spectral variation of the Pd nano-dimer array was measured in-situ under hydrogen gas flow. Figure 3 shows temporal variation of extinction at 800 nm under 3 %-hydrogen or pure nitrogen flow. One can clearly see that plasmon resonance became weaker in the presence of hydrogen, and this variation was reproduced several times. When a similar measurement was carried out using Pt- or Au- nanostructures, the plasmon resonances were not affected by hydrogen gas. In conclusion, we have tuned the optical property of metal nanostructures by alternating chemical environment. Polarization-dependent extinction spectra of Pd nano-dimer array.
Extinction 1000 800 600 400 Wavelength / nm ma.ecsdl.org/content/MA2012-02/54/3800.full.pdf by K Ikeda - 2012 Pd nano-monomers and dimers are fabricated on a glass substrate using angle-resolved nanosphere lithography. Briefly, a monolayer of polystyrene-beads.
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Post by skyship on Nov 5, 2013 3:34:14 GMT -5
dityrosine: Dityrosine is a fluorescent molecule formed as a result of normal posttranslational processing. In many structural proteins, dityrosine confers resistance to proteolysis and physicochemical trauma as a stabilizing crosslink. Dityrosine has also been found in oxidative/nitrative stress under a variety of conditions and biological systems. In this regard, it has been used as an important biomarker for oxidatively modified proteins during UV and gamma-irradiation, aging, and exposure to oxygen free radicals, nitrogen dioxide, peroxynitrite, and lipid hydroperoxides. Renewed interest in dityrosine and other tyrosine oxidation products as clinical indicators of oxidative modification has driven the development of important techniques for the specific analysis and quantification of these molecules. The presence of elevated levels of dityrosine in mammalian tissue and urine samples has been measured by chromatographic separation followed by mass spectrometry GC-MS and HPLC-MS/MS. Increases in dityrosine levels have been associated with pathologies such as eye cataracts, atherosclerosis, acute inflammation, and Alzheimer's disease. The continued development of, and increased accessibility to, improved mass spectrometric instrumentation will expand the capability, feasibility, and sensitivity with which specific biomarkers like dityrosine can be measured. www.ncbi.nlm.nih.gov/pubmed/17019703Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19 S) proteasome. ..............."Proteasome (the 670-kDa multicatalytic proteinase complex, that we have previously called macroxyproteinase or MOP (Pacifici, R. E., Salo, D. C., and Davies, K. J. A. (1989) Free Radical Biol. & Med. 7, 521-526; Salo, D. C., Pacifici, R. E., Lin, S. W., Giulivi, C., and Davies, K. J. A. (1990) J. Biol. Chem. 265, 11919-11927; Pacifici, R. E., and Davies, K. J. A. (1991) Gerontology 37, 166-180) appears responsible for dityrosine release during the selective degradation of oxidatively modified proteins in red blood cells and red cell extracts" www.ncbi.nlm.nih.gov/pubmed/8473319macroxyproteinase or MOP Page 371 books.google.com/books?id=mckVFtJ7YecC&pg=PA371&lpg=PA371&dq=macroxyproteinase+or+MOP&source=bl&ots=K_TJz93cn8&sig=6xxA5tZLcoUYUoHgv7d05XX_jDM&hl=en&sa=X&ei=B614UsHBA6_isATjw4CoBw&ved=0CEcQ6AEwBQ#v=onepage&q=macroxyproteinase%20or%20MOP&f=falsehair as carrier of nanomonomers or nano dimers.
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Post by skyship on Nov 5, 2013 3:41:46 GMT -5
the 19 S) proteasome. 19S regulatory particle The 19S particle in eukaryotes consists of 19 individual proteins and is divisible into two subassemblies, a 9-subunit base that binds directly to the α ring of the 20S core particle, and a 10-subunit lid. Six of the nine base proteins are ATPase subunits from the AAA Family, and an evolutionary homolog of these ATPases exists in archaea, called PAN (Proteasome-Activating Nucleotidase).[19] The association of the 19S and 20S particles requires the binding of ATP to the 19S ATPase subunits, and ATP hydrolysis is required for the assembled complex to degrade folded and ubiquitinated proteins. Regulation of the 20S by the 19S The 19S regulatory particle is responsible for stimulating the 20S to degrade proteins. A primary function of the 19S regulatory ATPases is to open the gate in the 20S that blocks the entry of substrates into the degradation chamber.[26] The mechanism by which the proteasomal ATPase open this gate has been recently elucidated.[15] 20S gate opening, and thus substrate degradation, requires the C-termini of the proteasomal ATPases, which contains a specific motif (i.e., HbYX motif). The ATPases C-termini bind into pockets in the top of the 20S, and tether the ATPase complex to the 20S proteolytic complex, thus joining the substrate unfolding equipment with the 20S degradation machinery. Binding of these C-termini into these 20S pockets by themselves stimulates opening of the gate in the 20S in much the same way that a "key-in-a-lock" opens a door.[15] The precise mechanism by which this "key-in-a-lock" mechanism functions has been structurally elucidated.[27] en.wikipedia.org/wiki/Proteasome#19S_regulatory_particle
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Post by skyship on Nov 5, 2013 3:55:55 GMT -5
www.rndsystems.com/Products/E-366JUNQ and IPOD are types of cytosolic protein inclusion bodies in eukaryotes. Neurodegenerative diseases, such as Parkinson’s, Alzheimer’s, and Huntington’s, are associated and correlated with protein aggregation and accumulation of misfolded proteins in inclusion bodies. For many years, protein aggregation was considered a random process by which misfolded proteins stick to each other to form inclusions[1] (imagine a bundle of hairs haphazardly piling up in a corner of a room). Moreover, protein aggregates were thought to be toxic agents and the cause for neuronal dysfunction and death. However, recent studies, using advanced methods (i.e. Fluorescence microscopy), show that protein aggregation may actually be a tightly regulated, organized process, by which the cell protects itself from toxic proteins by sequestration to inclusion bodies.[2] In 2008, Daniel Kaganovich showed that eukaryotic cells sort misfolded proteins into two distinct inclusion bodies in a well-managed cellular process:[3] The JUNQ (JUxta Nuclear Quality control compartment) The IPOD (Insoluble Protein Deposit) JUNQ and IPOD are evolutionarily conserved, and are found in specific and defined cellular sites. Delivery of misfolded, aggregated proteins to JUNQ and IPOD require an intact cytoskeleton and specific cellular quality control components, such as Heat Shock Proteins (HSPs).[4] The partition into the two distinct inclusion bodies is due to the different handling and processing of different kinds of misfolded proteins (e.g. ubiquitinated vs. non-ubiquitinated proteins). en.wikipedia.org/wiki/JUNQ_and_IPOD
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Post by skyship on Nov 6, 2013 23:23:55 GMT -5
synthetic fibrin glue was developed. The molecular structure is a copolymer composed of N-isopropyl acrylamide (NIPAM) units and vinyl monomer units
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Post by skyship on Nov 8, 2013 22:10:13 GMT -5
they say the serine from lichen is supposed to kill prions. Really now. If lichen is made of fungi and cyano or algae, than how and why is lichen made if prions are present? ..."The disease-associated prion protein (PrP(TSE)), the probable etiological agent of the transmissible spongiform encephalopathies (TSEs), is resistant to degradation and can persist in the environment. Lichens, mutualistic symbioses containing fungi, algae, bacteria and occasionally cyanobacteria, are ubiquitous in the environment and have evolved unique biological activities allowing their survival in challenging ecological niches. We investigated PrP(TSE) inactivation by lichens and found acetone extracts of three lichen species (Parmelia sulcata, Cladonia rangiferina and Lobaria pulmonaria) have the ability to degrade prion protein (PrP) from TSE-infected hamsters, mice and deer. " ./...." we found that PrP levels in PrP(TSE)-enriched preps or infected brain homogenates are also reduced following exposure to freshly-collected P. sulcata or an aqueous extract of the lichen. Our findings indicate that these lichen extracts efficiently degrade PrP(TSE) and suggest that some lichens could have potential to inactivate TSE infectivity on the landscape or be a source for agents to degrade prions. "............ europepmc.org/abstract/MED/21589935/reload=0;jsessionid=tNBAjGAtMksiL0lEvAnn.52P. sulcata? prions are from fungi. when are we going to get this? New amyloidosis involving hair and skin and brain.
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Post by skyship on Nov 8, 2013 22:31:45 GMT -5
amyloid fibrils or filaments compared to nanotubes: Recently, a number of examples of functional amyloid have been identified including a constituent of melanosomes, curli and hydrophobins.2 The History of Amyloid The term ‘amyloid’ was coined initially by Schleiden and then by Virchow in the mid-19th century to describe the iodine stained deposits seen in liver at autopsy. Consequently the deposits were thought to be carbohydrate in nature until their high nitrogen content was later established.3 Nevertheless, the inaccurately descriptive name was retained for these highly proteinaceous deposits. Further tinctorial properties included the specific binding of amyloid to the dye Congo Red which produced an apple green birefringence when examined between cross polarisers in a light microscope4 (Fig. 1). This finding suggested that amyloid was fibrillar in structure and subsequent transmission electron micrographs of amyloid confirmed this.5 Further progress in biochemical and biophysical techniques enabled the isolation of amyloid fibrils from tissues and their now characteristic cross-β structure was interpreted from X-ray fiber diffraction patterns......."In the evolution of mature fibrils, several metastable intermediates have been identified and isolated.22,24–26 These include very early species: dimers, trimers, tetramers (collectively known as oligomers27), Aβ derived diffusible ligands or ADDLs28 and the later bead-like structures up to 200 nm in length called protofibrils. Figure 2Synthetic amyloid fibrils made from Aβ peptide (A) electron micrograph showing long, straight, unbranching fibrils. (B) X-ray fiber diffraction pattern from partially aligned amyloid fibrils showing the characteristic “cross-β” ... www.ncbi.nlm.nih.gov/pmc/articles/PMC2634529/figure/F2/?report=objectonly ........"“Exploiting Amyloid” Functional Amyloid.Amyloid fibrils are extremely stable and resistant to degradation. They have been described as having a similar tensile strength to steel,75 a property that they share with their structural cousin, silk. Recently, a number of nonpathogenic, functional forms of amyloid have been identified in bacteria, fungi, insects and mammals.2 Curli is a functional fiber found on the surface of bacteria such as E. coli. The fibers share structural similarities to amyloid and formed by a protein called CsgA. Fibrillization is carefully regulated by a protein machine complex.76,77 Many fungi produce amphipathic proteins called hydrophobins"............ FIRST TIME I HAVE SEEN NANOWIRES IN RELATION TO SUP35 THE ARTIFICIAL OLIGOMER OR EVOLUTIONARY CAPACITOR INVOLVING HEAT SHOCK PROTEINS WHICH UNFOLD EVEN IF THERE IS NO HEAT SHOCK. SO UNFOLDING THEN HAS ANOTHER PURPOSE, AND THESE WERE USED AS FUNCTIONAL IN THE MINDS OF THESE EVOLUTIONARY DEVELOPMENT AND CELL FREE CONTROL OF THE HUMAN BODY. NANOWIRES WERE SHOWN TO PRES. OBAMA BY THE INVENTOR WHO ALSO WAS AFFILIATED WITH NAVY, AIRFORCE PROJECTS AND DARPA PROJECTS INCLUDING GEOENGINEERING. " Nanowires have been fabricated by assembling proteins such as the N-terminal region of the yeast prion, Sup35. Conjugate colloidal gold particles were associated along the fibers using exposed cysteine residues of a variant Sup35,80 yielding wires around 100 nm in diameter (Fig. 4A). A very short peptide, composed of two phenylalanine residues, assembles to form amyloid-like nanotubes and these may be functionalised using ionic silver in the centre of the nanotube (Fig. 4B).82 This work yielded nanowires around 20 nm in diameter.",,,,,,,,,,,, www.ncbi.nlm.nih.gov/pmc/articles/PMC2634529/================================ sup 35 prion amyloid maker, is the evolutionary capacitor......... the foreign adaptive protein. It has heat shock proteins, it has a nanowire, and phenylalanine part of a new amino acid number 23....... amyloid like nanotubes..........there are the intermediates the cells snakes, the amyloid filaments are of different sizes as proven by Lindquist and Whitesidess(who hid in the background) as did many others\, but reports from clinics showing that sup 35 is showing up as pathogenic is a true proof of its existence and its damage to the human body. Now for the report saying amyloids are in skin, hair and brain and other organs. In fact AA is found in the duodenum, the prions are evident. image of amyloids(prions ) in small bowel, or duodenum. en.wikipedia.org/wiki/File:Small_bowel_duodenum_with_amyloid_deposition_congo_red_10X.jpg www.hindawi.com/crim/gastrointestinal.medicine/2013/525439/In the heart: en.wikipedia.org/wiki/Amyloidosis
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Post by kritters on Nov 8, 2013 22:36:45 GMT -5
THAT'S IT, SKY!!! It's what I've been waiting to hear! As I read through the advanced stuff you posted as usual, I focused on these two things: prions are from fungi. when are we going to get this? New amyloidosis involving hair and skin and brain. PRIONS are from FUNGI??? This explains EVERYTHING!!! Can't wait to see this connection. I'm just a lay person but I know this is significant. en.wikipedia.org/wiki/Fungal_prions LOL even from Wikipedia! A connection! So, how easy is it to splice genes into this to wreak havoc on us or just by mistake (can't forget the incompetence factor, right?) PROTEINS! seriously scary shit. Kritts
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Post by skyship on Nov 8, 2013 23:47:15 GMT -5
Krits, It has been a long time coming, but, I never forgot about the dimers that showed up in my blood tests. I do not know if they are even listed anymore, but, I believe they are the two cell stage of the filaments, monomer, dimer, protocells, and the use of SYNTHETIC amyloids, however, the heat shock protein unfolds the proteins that make up our RNA DNA. Now, knowing that nanowires made from sup35 is a go. And the bragging about evolutionary capacitors or should I say Evo Devos? sup35 forms fibrils of different sizes. it can relate to nanotube size on one level, the others are large OLIGOMERS. THESE ARE NOW PROVEN TO BE TOXIC. HOW?: FUNGI USED FOR SUP35...THEY CALL IT YEAST?
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Post by skyship on Nov 9, 2013 0:07:32 GMT -5
First, The New Amyloidosis: A new amyloidosis caused by fibrillar aggregates of mutated corneodesmosin ......" Hypotrichosis simplex of the scalp (HSS, MIM 146520) is a rare, autosomal dominant form of alopecia that affects men and women equally. Patients have normal hair at birth, but experience progressive loss of scalp hair that leads to almost complete hair loss in adulthood. In contrast, beard, eyebrows, axillary hair, teeth, and nails develop normally (5⇓ , 6)⇓ . Patients show no other cutaneous abnormality. HSS is caused by nonsense mutations in the corneodesmosin gene (CDSN; refs. 7⇓ , 8⇓ ). Corneodesmosin (CDSN) is a 529-aa glycoprotein exclusively found in the cornified squamous epithelia and involved in the cohesion of the upper epidermis. CDSN is synthesized by the differentiated keratinocytes in the uppermost epidermal layers, namely the upper spinous and granular layers. On secretion, it localizes in the extracellular core of desmosomes (9⇓ , 10)⇓ . CDSN is also expressed in the 3 epithelial components of the inner root sheath of hair follicles, where it is probably associated with desmosomal cohesive structures (9)⇓ . A striking feature of CDSN is its very high serine and glycine content. With >74% of serine and glycine, the N-terminal domain between aa 60 and 171, so-called GS domain, confers homophilic adhesive properties to the protein (11)⇓ and is able to spontaneously form large homo-oligomers in vitro (12)⇓ . T hree heterozygous nonsense mutations have been reported to date in HSS in 4 unrelated families of different ethnic origin: Q215X, Q200X, and Y239X (7⇓ , 8)⇓ . All of the mutated alleles encode truncated CDSN polypeptides in which the GS domain is entirely preserved. Immunohistological analyses of skin biopsies from patients have shown alterations in the hair follicle structure and an aberrant location of the mutated CDSN (mutCDSN). The latter was indeed shown to be present in deposits of variable size, located in the dermal papillae and at the periphery of the hair follicles deeper in the dermis. Western blotting analyses have shown that the truncated mutCDSN in the deposits corresponds to SDS- and boiling-resistant dimers, trimers, and larger oligomers (8)"......www.fasebj.org/content/24/9/3416.full========================= the serine protein is from lichen and there is evidence from biopsies of Civatte bodies and possibly lichen planus or mislabeled as that and is really lichen amyloidosis. Serine is from lichen which has fungus and algae in it in the wild. serine is in the GS constuction of elements they say destroy prions, but,.... ....not if the lichen already has prions in it from the prions of the fungi.............so we are being inducted with prions, synthetic formers of amyloids, however the prions come from the fungi. which fungi? =========================== but. knowing that sup 35 is a player, tells us a lot............ a nanowire.............where nano comes in. I have said this before, but, not all the info was out there, now there is a def find there.....in the above report.
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Post by skyship on Nov 9, 2013 0:59:50 GMT -5
Second, Association of skin with the pathogenesis and treatment of neurodegenerative amyloidosis www.ncbi.nlm.nih.gov/pmc/articles/PMC3262151/"The conformational diseases or amyloid diseases include Alzheimer’s disease (AD), Parkinson diseases, amyotrophic lateral sclerosis (ALS), type 2 diabetes mellitus, and various forms of cutaneous amyloidosis (Botelho and Lupi, 2008). Hence, the question arose whether there may be evidence supporting a link between cutaneous manifestations of amyloid deposits and neurodegenerative amyloidosis. This review aims to address this question and give a novel perspective on the relation of amyloid in skin and brain."....................
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Post by skyship on Nov 9, 2013 1:08:34 GMT -5
Acknowledgements R.N.R. is supported by a grant from the BBSRC, L.C.S. would like to acknowledge the support of the BBSRC, Alzheimer's research trust, Royal Society and Wellcome Trust. The authors would like to express their thanks to Dr. Vestergaard for kind contribution of Figure 3 and to Dr. Scheibel for Figure 4A and to Dr. Gazit for Figure 4B. They would also like to thank Dr. Curtis Rambaran for critical reading of the manuscript. www.ncbi.nlm.nih.gov/pmc/articles/PMC2634529/#!po=52.2727
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Post by skyship on Nov 9, 2013 1:23:16 GMT -5
Amyloid-like fibers for bionanotechnology. (A) Nanowires based on the N-terminal region of the yeast prion, Sup35. Nanogold was covalently linked to the engineered cysteine residues in the protein and conjugate colloidal gold and silver particles were associated along the fibers to form wires,80 (B) assembly of diphenylalanine to form nanotubes that can be filled with silver to make nanowires.82 a larger image of the nanowires: www.ncbi.nlm.nih.gov/pmc/articles/PMC2634529/figure/F4/
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Post by skyship on Nov 9, 2013 1:42:15 GMT -5
yeast prion, Sup35.en.wikipedia.org/wiki/Fungal_prion Wickner was given a bad rap, accused of things like the military high ranks are facing today. Truth tellers are destroyed in more ways than one. But, we will not give up. Morgellons is about discovery of the evo devos and the actual cause of this malady, not a disease but an instigated unfolding mechanism to fold in the artificial or synthetic amyloid, to either destroy or make one live longer. Even Lindquist admitted this. That depending on variations in certain humans or genetics, these will either maim or increase life. So, it becomes an evolutionary extinction of certain humans who cannot integrate the mechanism or one incorporates the tranformation.
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Post by skyship on Nov 9, 2013 1:53:04 GMT -5
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Post by skyship on Nov 9, 2013 2:15:28 GMT -5
N and M terminals and the C terminus form binding sites to Sup45p Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. ...... Two sites for Sup45p binding were found within Sup35p: one is formed by the N and M domains, and the other is located within the C domain. Similarly to Sup35p, in [PSI+] cells Sup45p was found in aggregates. The aggregation of Sup45p is caused by its binding to Sup35p and was not observed when the aggregated Sup35p fragments did not contain sites for Sup45p binding. The incorporation of Sup45p into the aggregates should inhibit its activity. The N domain of Sup35p, responsible for its aggregation in [PSI+] cells, may thus act as a repressor of another polypeptide chain release factor, Sup45p. This phenomenon represents a novel mechanism of regulation of gene expression at the posttranslational level"............ www.ncbi.nlm.nih.gov/pmc/articles/PMC232131/N and M terminals C terminus Conducting nanowires: Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. Scheibel T, Parthasarathy R, Sawicki G, Lin XM, Jaeger H, Lindquist SL. Source Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA. Abstract Recent research in the field of nanometer-scale electronics has focused on the operating principles of small-scale devices and schemes to realize useful circuits. In contrast to established "top-down" fabrication techniques, molecular self-assembly is emerging as a "bottom-up" approach for fabricating nanostructured materials. Biological macromolecules, especially proteins, provide many valuable properties, but poor physical stability and poor electrical characteristics have prevented their direct use in electrical circuits. Here we describe the use of self-assembling amyloid protein fibers to construct nanowire elements. Self-assembly of a prion determinant from Saccharomyces cerevisiae, the N-terminal and middle region (NM) of Sup35p, produced 10-nm-wide protein fibers that were stable under a wide variety of harsh physical conditions. Their lengths could be roughly controlled by assembly conditions in the range of 60 nm to several hundred micrometers. A genetically modified NM variant that presents reactive, surface-accessible cysteine residues was used to covalently link NM fibers to colloidal gold particles. These fibers were placed across gold electrodes, and additional metal was deposited by highly specific chemical enhancement of the colloidal gold by reductive deposition of metallic silver and gold from salts. The resulting silver and gold wires were approximately 100 nm wide. These biotemplated metal wires demonstrated the conductive properties of a solid metal wire, such as low resistance and ohmic behavior. With such materials it should be possible to harness the extraordinary diversity and specificity of protein functions to nanoscale electrical circuitry. www.ncbi.nlm.nih.gov/pubmed/12672964/
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Post by skyship on Nov 9, 2013 2:26:47 GMT -5
www.ncbi.nlm.nih.gov/pmc/articles/PMC153589/figure/F1/www.ncbi.nlm.nih.gov/pmc/articles/PMC153589/figure/F2/www.ncbi.nlm.nih.gov/pmc/articles/PMC153589/figure/F3/www.ncbi.nlm.nih.gov/pmc/articles/PMC153589/figure/F4/all images and article:www.ncbi.nlm.nih.gov/pubmed/12672964/========================= So can we dis assemble them by light?Light-triggered disassembly of amyloid fibrils.Measey TJ, Gai F. Source Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States. Abstract There is growing demand for novel methods that could render the controlled disassembly of higher-order structures formed, for example, by peptides. Herein, we demonstrate such a method based on the application of a photocaged variant of the amino acid lysine, namely, lys(Nvoc). Specifically, we introduce lys(Nvoc) into the primary sequence of the amyloidogenic peptide, Aβ(16-22), at a position where the native side chain is known to play a key role in fibril formation via hydrophobic interactions. Both AFM and infrared spectroscopic measurements indicate that the resultant Aβ(16-22) mutant is able to form fibrils whereas, more importantly, the fibrils thus formed can be completely disassembled upon irradiation with near-UV light, which cleaves the photolabile Nvoc moiety and triggers the restoration of the lysine side chain. These results suggest that the generation of a single charge in a highly hydrophobic region of the fibrils is sufficient to promote their dissociation. Thus, we envisage that the current approach will find useful applications wherein controlled structural disassembly or content release is required. www.ncbi.nlm.nih.gov/pubmed/22867440Images: all 7 images and descriptions: www.ncbi.nlm.nih.gov/pmc/?term=22867440[PMID]&report=imagesdocsum
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Post by skyship on Nov 9, 2013 2:56:15 GMT -5
near-UV light, hyperphysics.phy-astr.gsu.edu/hbase/ems3.htmlso does the Spitzenkorper in fungi have some value? or is it misnamed? spitzenkorpers are in fungi, n. crassa, candida, yeasts, etc. some info: Analyses of Dynein Heavy Chain Mutations Reveal Complex ... www.ncbi.nlm.nih.gov › NCBI › Literature › PubMed Central (PMC) by S Sivagurunathan - 2012 - Cited by 2 - Related articles Vanadate-mediated UV photolysis of N. crassa dynein ... µM Na3VO4 were irradiated with UV (365 nm) light using UVL-56 BLAK-RAY ... with segments of the tubulin GFP signals near the hyphal tips (Figure 2A). ...... Evidence that Spitzenkorper behavior determines the shape of a fungal hypha: a test of the hyphoid model. Results for similar searches Apical growth archive.bio.ed.ac.uk/jdeacon/microbes/apical.htm The importance of the Spitzenkörper was recognised long before the advent of ..... structures of several fungi are induced to develop by light (or near-UV). More results for near uv light and the spitzenkorper prion Ultraviolet - Wikipedia, the free encyclopedia en.wikipedia.org/wiki/Ultraviolet Jump to Near and medium UV - [edit]. Main article: Ultraviolet photography. A portrait taken using only UV light between the wavelengths of 335 ... More results for near uv rays Black light - Wikipedia, the free encyclopedia en.wikipedia.org/wiki/Black_light The purple glow of a black light is not the UV light itself, which is invisible, but ... The phosphor typically used for a near 368 to 371 nanometre emission peak is ... More results for near ultraviolet light Oxidative mechanisms of toxicity of low-intensity near-UV light in ... www.ncbi.nlm.nih.gov › Journal List › J Bacteriol › v.169(5); May 1987 by GF Kramer - 1987 - Cited by 63 - Related articles The exposure of Salmonella typhimurium to environmentally relevant near-UV light stress has been studied by the use of a low-intensity, broad-band light ...
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Post by lilsissy on Nov 10, 2013 1:12:18 GMT -5
I remember this part from early on,
Some of these are not associated with any disease state and may possibly have a beneficial role by giving an evolutionary advantage to their host.
Wondering if it is a part of a design to help give us an evolutionary change to man machine interfaces.
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Post by skyship on Nov 10, 2013 19:52:30 GMT -5
Lil sis,
So good to hear from you. yes, they give evolutionary advantage to the right kind of variation in the heat shock protein. and yes, walks right into the interface. That evolutionary advantage or disadvantage is related to the capacitor. And that is through sup35 and sup45 and effects the skin(acting as brain), using amyloids as the circuit. So, amyloids can remain latent, until disturbed by either sound frequencies, and follicles are the first effected by the signals.
If the nanowire, from sup35 is to be useful, it would have to be in the cytokeratin, the change in the cytoskeletal cells involving the N and M terminal and the C- Terminal or neuro connection points. neuro, muscular and carboxyl junctions.
This report talks of the skin-brain connection. circuit board? I betcha~! A setup for the Interface machine/man. below the cure or non soluable oligomer(peptide) in particular the neuropeptide, is artificial and is supposed to cure the prion, amyloid condition, however, these a proving to be evolutionary determinants of life or death of the cell. Apoptosis of even good cells, for this cell free system. ===========================
============================================ So, I believe that Morgellons is more closely related to AD than Lymes Disease. but, it was done by "foreign adaptive heat shock protein which unfolds proteins even when there is no heat shock, as in the "climate change" Its purpose was to inundate the human body with the the tools for machine/human interface. a process. and it can delete or add just like a computer, because it has the "wireless signal" to do this. that signal is inside in the nanowire, made from the artificial or man made capacitor. An Evolutionary extinction or prolongation of life depending on the type variation of genetic background. A Selection process so to speak.
Skyship
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Post by lilsissy on Nov 10, 2013 22:53:03 GMT -5
The cytoskeletal cells , yes, this is where I had read
that these where the target for wireless connection.Been a while....so much has happened, my memory poor right now. My Doctor told me that I must the have shot this year because the flu is bad this year. To late I told my Doctor, my mother passed from complications from the flu on September 20 and I caught it from her about Aug 30. Mom called me over Aug 30 , she was having back pain and anxiety because she had not completed her final paper work ,( her will), to protect me as I was her care giver and lost a very well paying career and house to help her after her sudden paralysis. Well that night she was very lucid and told me with tears in her eyes to please forgive her that she was certain she would die soon because she could see from the corner of her eye a man standing partially behind the curtain that surrounded her bed. He was looking at her and every time she looked at him , he stepped back. That was the only strange thing she told me that night. I took her vital. signs which where good , her Doctor had just been out and felt that she was having muscle spasms from the spondylosis that runs in the family. She refused to go to the hospital , I slept on the floor by her bed and spent the whole next day and night with her. I tried to calm her about my well being if she were to pass and went over funeral arrangements she wanted. She seemed to fully recover and I became very ill and felt I too was dying, 2 days after rubbing her back that first night. About 1 week later she became sick again in right in the middle of my husbands leg surgery. I stayed at the hospital with her day and night from Sept 11 till she came home with hospice on Sept 19. She was fraught with terrible dreams of her children fighting which indeed erupted horribly as soon as she was taken out of the house to the funeral home. It seemed as though a demon did not like the circle of prayer about 20 family members took with her hands shortly after she passed. Mom and I prayer many times in a circle of prayer around her bed, just the two of us sometimes other times with other family neighbors and friends . We did this often when we heard of family or friends who were in trouble or need . Her last hours she occasionally smiled sweetly at us and was talking with Karen ( Chaos-on-line, and my late sister Debbie as well as my late father. Such a beautiful gathering of love encircled the whole family around the now deceased mother. Then just as soon as mom left all hell broke loose as if a demon jumped into the midst of everyone, everyone was acting possessed and of great violence. A sister demanded everyone to leave suddenly, this is what set off the hellish fight. That fight ended up most likely the factor that saved my sister-in-laws life as she had a mild heart attack when she was thrown to the ground as she attempted to swing and hit others . She had been walking around with about 90 % of her heart blocked. So mom's death saved her daughter-in-laws life, My daughter being into the medical field helped her breath thru it and would not let her lay down. The whole family seems to be shattered right now and greed has taken over love but God is still on the throne and gets me through every day. My husband admitted to me he was having an affair the next night and about that time I just started to laugh inside, that old Wiley Devil likes to give us the one two but God the trinity will deliver me as he did Mother. The man behind the curtain walks us through the valley and the shadow of death, which in my opinion is every day of our life. So they can make all the artificial glue they want but how does that go? ?
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Post by lilsissy on Nov 10, 2013 22:57:26 GMT -5
Romans…38
For I am convinced that neither death, nor life, nor angels, nor principalities, nor things present, nor things to come, nor powers,
39 nor height, nor depth, nor any other created thing, will be able to separate us from the love of God, which is in Christ Jesus our Lord.
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Post by lilsissy on Nov 10, 2013 23:14:38 GMT -5
But this flu thing...well yea I do believe we had a flu but I detected a strange smell in the house and had the furnace checked today. We had both a carbon monoxide and a gas leak . So I am quiet sure this added to our illness. I lost my appetite and would fall asleep sitting up and was suffering from terrible headaches. Maybe now I can get my strength back but I miss mom so. Thou I know in my heart we are just a curtain away and she is now dancing with my Dad , Karen and Debbie. So sad the dwelling on those things mom could not take with her. We should dwell on gift God gave us of a loving mother.
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Post by lilsissy on Nov 11, 2013 11:27:06 GMT -5
The skin was mentioned as the richest place of the vascular system as well as scalp and nail beds.
The vascular system was mentioned ( or shall I say the empty spaces that exist in it) as the place where the artificial polymers branch out, the PEDOT was chosen as best, from the quarterly reports from U. of M. on research into the Human Brain Machine done for our Government.
Yes, a fungus was also mentioned as found to much joy. It was what was needed for the Pedot to branch out, it is the ground work , first platform for the growth of the artificial polymers but a problem occurred because in some it caused an over immune reaction, so Dex fibers were thought to be the answer.
Some of our fibers are Dex.
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