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Post by skyship on Feb 25, 2009 8:46:16 GMT -5
Was it the Dimer, a biosensor, used to sense bioweapons, integrated into our physique or to keep track of degradation of our fibrin? Seems I recently have a D-Dimer count at 698. Now, what does that mean? Seems the D-Dimer was inserted many years ago. Just what is that and why important in medical tests? "D-dimer is a fibrin degradation product, a small protein fragment present in the blood after a blood clot is degraded by fibrinolysis."en.wikipedia.org/wiki/D-dimer_proteinah...........the third element of the blood? fibrinolysis? " Fibrinolysis is the process wherein a fibrin clot, the product of coagulation, is broken down.[1] Its main enzyme plasmin cuts the fibrin mesh at various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney and liver.",,,,,,,,,,,,,, en.wikipedia.org/wiki/FibrinolysisFor breakfast? www.kringle.com/shopping/kringle_multi_packs.lassoor........... "Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases. Patthy L, Trexler M, Váli Z, Bányai L, Váradi A. Prothrombin, plasminogen, urokinase- and tissue-type plasminogen activators contain homologous structures known as kringles . The kringles correspond to autonomous structural and folding domains which mediate the binding of these multidomain proteins to other proteins. During evolution the different kringles retained the same gross architecture, the kringle -fold, yet diverged to bind different proteins. We show that the amino acid sequences of the type II structures of the gelatin-binding region of fibronectin are homologous with those of the protease- kringles . Prediction of secondary structures revealed a remarkable agreement in the positions of predicted beta-sheets, suggesting that the folding of kringles and type II structures may also be similar. As a corollary of this finding, the disulphide-bridge pattern of type II structures is shown to be homologous to that in kringles . It is noteworthy that protease- kringles and fibronectin type II structures have similar functions inasmuch as they mediate the binding of multidomain proteins to other proteins. It is proposed that the kringles of proteases and type II structures of fibronectin evolved from a common ancestral protein binding module."...... www.ncbi.nlm.nih.gov/pubmed/6373375seems these new terms are made up as the evolution is made. Skyship
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Post by skyship on Feb 25, 2009 8:54:36 GMT -5
protease- kringles melanin related? "Extracellular SH3 domain containing proteins--features of a new protein family. Stoll R, Bosserhoff A. Faculty of Chemistry and Biochemistry, University of Bochum, Bochum, Germany. In the year 1994, the protein MIA (melanoma inhibitory activity) was found to be strongly expressed and secreted by malignant melanomas and subsequent studies revealed that MIA has an important function in melanoma development and invasion. Multidimensional NMR-spectroscopy and x-ray crystallography revealed that recombinant human MIA adopts a Src homology 3 (SH3) domain-like fold in solution, a structure with two perpendicular antiparallel three- and five-stranded beta-sheets. SH3 domains are protein modules that are found in many intracellular signalling proteins and mediate protein-protein interactions by binding to proline-rich peptide sequences. Unlike previously described protein structures with SH3 domain folds, MIA is a secreted single-domain protein of 12 kDa that contains an additional antiparallel beta-sheet and two disulfide bonds. Furthermore, the charge surrounding the canonical binding site differs from that of classical SH3 domains. The two disulfide bonds are crucial for correct folding and function as revealed by mutation analysis. Therefore, MIA appears to be the first extracellular protein adopting an SH3 domain-like fold. MIA was shown to interact with fibronectin, and MIA-interacting peptide ligands identified by phage display screening are similar to the consensus sequence of type III human fibronectin repeats, especially FN14. Interestingly, recent data revealed that MIA can also directly bind to integrin alpha 4 beta 1 and alpha 5 beta1 and that it modulates integrin activity negatively. These findings suggest an interesting role of the SH3-domain proteins in the extracellular compartment. Recently, MIA homologous proteins with a sequence identity of 44% and a sequence homology of approximately 80% were determined (TANGO, MIA-2, OTOR). This clearly suggests that this structural device is used more frequently, in processes ranging from developmental changes to the interference of cell attachment in the extracellular matrix. Detailed studies are necessary to determine the exact function of the MIA homologous proteins. It will be interesting to know whether additional protein families can be identified which are secreted and carry SH3 domain-like modules, in addition to elucidate what the specific physiological targets of this protein family are." www.ncbi.nlm.nih.gov/pubmed/18537677?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_ DiscoveryPanel.Pubmed_Discovery_RA&linkpos=5&log$=relatedreviews&logdbfrom=pubmed High circulating D-dimers are associated with presence of ascites Published: Friday, May 2, 2008 - 10:28 in Health & Medicine Learn more about: accurate marker d dimers liver cirrhosis liver failure presence world journal of gastroenterology The liver is the production site of most of the proteins which favour and inhibit the process of coagulation and fibrinolysis. Patients with liver cirrhosis may develop serious coagulopathy and a hyperfibrinolytic state, which contributes to the bleeding tendency. Plasma levels of fragment D-dimer (D-dimer) represent an accurate marker of fibrinolytic activity. The finding of a high plasma D-dimer concentration in patients with liver cirrhosis, decompensated with ascites, led Agarwal et al. to suggest the major role of ascites in the pathogenesis of the hyperfibrinolytic state associated with liver failure. This study, published in the March 14, 2008, issue of the World Journal of Gastroenterology, shows that high circulating D-dimer levels are associated with the presence of ascites, and these decrease or return to normal following its resolution. The depletion of ascitic fluid might prevent bleeding complications, especially if invasive procedures become necessary. Interestingly enough, in the absence of ascites, high D-dimer levels are associated with the presence of hepatocellular carcinoma (HCC). HCC is a frequent complication of liver cirrhosis and its detection at an early stage is important. The finding of high plasma D-dimer levels in cirrhotic patients without ascites may represent a marker of HCC. Source: World Journal of Gastroenterology esciencenews.com/articles/2008/05/02/high.circulating.d.dimers. are.associated.with.presence.ascites Skyship
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Post by skyship on Feb 25, 2009 9:05:35 GMT -5
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Post by skyship on Feb 25, 2009 9:08:09 GMT -5
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Post by skyship on Feb 26, 2009 9:45:11 GMT -5
dendrimer issue: Bioinspired molecular design of functional dendrimers References and further reading may be available for this article. To view references and further reading you must purchase this article. Dong-Lin Jianga, E-mail The Corresponding Author and Takuzo Aidaa, b, aERATO AIDA Nanospace Project, Japan Science and Technology Agency (JST), 2-41 Aomi, Koto-ku, Tokyo 135-0064, Japan bDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan Available online 13 March 2005. Abstract The present article focus on a series of our recent work on bioinspired molecular design of functional dendrimers, in particular, dendrimer cobalt porphyrins as novel coenzyme B12 mimics, dendrimers for light harvesting and photoinduced electron transfer, and dendrimers for controlled self-assembly and their functions. Special emphasis is placed on size and morphology dependent properties of these dendritic macromolecules. Keywords: Dendrimer; Porphyrin; Conjugated polymer; Metal-coordination polymer; Fullerene; Hydrogen evolution; Light harvesting; Organic transformation; Energy transfer; Photoinduced electron transfer; Photosynthesis; Spin transition Article Outline 1. Introduction 2. Dendrimer cobalt porphyrin as a novel coenzyme B12 Mimic 3. Dendrimers for photoinduced energy transfer 3.1. Design and functions of giant dendritic multiporphyrin arrays 3.2. Design of conjugated wires bearing light-harvesting dendritic envelopes and insulated discrete molecular wires 4. Dendrimers for photoinduced electron transfer 4.1. Photoinduced charge separation within the dendrimer framework 4.2. Photosensitized hydrogen evolution from water using dendritic conjugated wires 5. Dendrimers for controlled self-assembly and their functions 5.1. Design of dendritic porphyrin–fullerene nanopeapods 5.2. Design of photoactive vesicles assembled from amphiphilic dendritic porphyrin–fullerene dyads 5.3. Design of soft magnetic materials and switching of spin states triggered by phase transition 6. Summary References Thumbnail image Scheme 1. Schematic representation of light harvesting and emission of the dendritic conjugated wire 19. View Within Article Thumbnail image Scheme 2. Schematic diagram of photosensitized hydrogen evolution from water using water-soluble dendritic conjugated polymers. The insets show the molecular modeling of an octamer of 27 and a reaction scheme for hydrogen evolution from water. Thumbnail image Scheme 3. Self-assembly of a dendritic zinc porphyrin dimer with fullerenes to form supramolecular peapods. tinyurl.com/aeyqqfwww.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TX2-4FPDPW6-1&_user=10&_coverDate=04%2F30%2F2005&_rdoc=1&_ fmt=high&_orig=browse&_sort=d&view=c&_acct=C000050221&_version= 1&_urlVersion=0&_userid=10&md5=fba53ef1d07dbe4c32f13e02a69fbf91 THESE ARE MIMICS OF B12? mimic vitamins but are artificial? Artificial evolution? skyship
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Post by skyship on Feb 26, 2009 16:27:26 GMT -5
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Post by aqt on Mar 2, 2009 15:07:56 GMT -5
Lookie here www.scs.uiuc.edu/suslick/execsummporph.htmlThe research team led by Professor Suslick has been at the leading edge of research on synthetic metalloporphyrins for applications as synthetic analogs of heme proteins, shape selective oxidations, , and diverse materials chemistry applications including nanoporous network solids, non-linear optical materials, and selective sensors.aqt
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Post by skyship on Mar 2, 2009 16:29:24 GMT -5
Excellent article on heme, blood product, so tell me they are not working on synthetic blood, have been for some time, but they are taking this into the alkenes and alkoids, definite sensors and replacers of natural substances and body parts. Those who integrate this are being transformed, they lose weight, the look like walking bones, folks. That is why any artificial is being dissed by us, either the old fibronectin is leaving or the new is being rejected. I think it is being rejected, because it is not needed. Why give the body something that is not needed? The fibers look plastic, nylonish or metallic to me. Darwins geological dream has to have some intermediates to make the evolution to artificial life work. yep, those porphyrins. why needed? for that SS or Solid State? well that makes it more 3 dimensional in a 5 dimensional world. right CR? " We are also developing new nanoporous network solids of highly functionalized porphyrins to provide controlled porphyrin orientation in the solid state and to produce molecularly-designed molecular sieves [6]. We intend to explore the use of these solids as heterogeneous shape-selective oxidation catalysts. An example of one such structure is shown below: www.scs.uiuc.edu/suslick/execsummporph.htmlit is that darn "substituted porphyrin" that gives it away. mmmmmmmmmmmm that would be "artificial" with controls, has to have the metal for the spark, and then the solid state bioelectric does it thing. dendrimers, dimers and dendrites, getting it down, can only work on the artificial, the natural doesn't need that much spark, does it? skyship
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