Abrus: A plant genus of the family FABACEAE. Members contain ABRIN.Castor Oil: Oil obtained from seeds of Ricinus communis that is used as a cathartic and as a plasticizer.Abrin: A toxic lectin from the seeds of jequirity, Abrus precatorius L. Very active poison. Five different proteins have so far been isolated: Abrus agglutinin, the component responsible for: hemagglutinating activity, & abrins a-d, the toxic principals each consisting of two peptide chains are held together by disulfide bonds.Ricinus: A plant genus of the family EUPHORBIACEAE, order Euphorbiales, subclass Rosidae. The seed of Ricinus communis L. is the CASTOR BEAN which is the source of CASTOR OIL; RICIN; and other lectins.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Ricin: A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally.Fossil Fuels: Any combustible hydrocarbon deposit formed from the remains of prehistoric organisms. Examples are petroleum, coal, and natural gas.Seeds: The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.Plant Lectins: Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.Castor Bean: Common name for Ricinus communis, a species in the family EUPHORBIACEAE. It is the source of CASTOR OIL.Copyright: It is a form of protection provided by law. In the United States this protection is granted to authors of original works of authorship, including literary, dramatic, musical, artistic, and certain other intellectual works. This protection is available to both published and unpublished works. (from Circular of the United States Copyright Office, 6/30/2008)Software: Sequential operating programs and data which instruct the functioning of a digital computer.Skin Neoplasms: Tumors or cancer of the SKIN.Skin: The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.Licensure: The legal authority or formal permission from authorities to carry on certain activities which by law or regulation require such permission. It may be applied to licensure of institutions as well as individuals.Moral Obligations: Duties that are based in ETHICS, rather than in law.Congresses as Topic: Conferences, conventions or formal meetings usually attended by delegates representing a special field of interest.United States Food and Drug Administration: An agency of the PUBLIC HEALTH SERVICE concerned with the overall planning, promoting, and administering of programs pertaining to maintaining standards of quality of foods, drugs, therapeutic devices, etc.Eye: The organ of sight constituting a pair of globular organs made up of a three-layered roughly spherical structure specialized for receiving and responding to light.Group Purchasing: A shared service which combines the purchasing power of individual organizations or facilities in order to obtain lower prices for equipment and supplies. (From Health Care Terms, 2nd ed)Mouth Protectors: Devices or pieces of equipment placed in or around the mouth or attached to instruments to protect the external or internal tissues of the mouth and the teeth.Cuspid: The third tooth to the left and to the right of the midline of either jaw, situated between the second INCISOR and the premolar teeth (BICUSPID). (Jablonski, Dictionary of Dentistry, 1992, p817)Orthodontic Appliances: Devices used for influencing tooth position. Orthodontic appliances may be classified as fixed or removable, active or retaining, and intraoral or extraoral. (Boucher's Clinical Dental Terminology, 4th ed, p19)Extraoral Traction Appliances: Extraoral devices for applying force to the dentition in order to avoid some of the problems in anchorage control met with in intermaxillary traction and to apply force in directions not otherwise possible.Sports Equipment: Equipment required for engaging in a sport (such as balls, bats, rackets, skis, skates, ropes, weights) and devices for the protection of athletes during their performance (such as masks, gloves, mouth pieces).Photography, Dental: Photographic techniques used in ORTHODONTICS; DENTAL ESTHETICS; and patient education.Mouth: The oval-shaped oral cavity located at the apex of the digestive tract and consisting of two parts: the vestibule and the oral cavity proper.Facial Injuries: General or unspecified injuries to the soft tissue or bony portions of the face.Tooth: One of a set of bone-like structures in the mouth used for biting and chewing.Maxilla: One of a pair of irregularly shaped bones that form the upper jaw. A maxillary bone provides tooth sockets for the superior teeth, forms part of the ORBIT, and contains the MAXILLARY SINUS.Mouth Protectors: Devices or pieces of equipment placed in or around the mouth or attached to instruments to protect the external or internal tissues of the mouth and the teeth.Cuspid: The third tooth to the left and to the right of the midline of either jaw, situated between the second INCISOR and the premolar teeth (BICUSPID). (Jablonski, Dictionary of Dentistry, 1992, p817)Orthodontic Appliances: Devices used for influencing tooth position. Orthodontic appliances may be classified as fixed or removable, active or retaining, and intraoral or extraoral. (Boucher's Clinical Dental Terminology, 4th ed, p19)Extraoral Traction Appliances: Extraoral devices for applying force to the dentition in order to avoid some of the problems in anchorage control met with in intermaxillary traction and to apply force in directions not otherwise possible.Sports Equipment: Equipment required for engaging in a sport (such as balls, bats, rackets, skis, skates, ropes, weights) and devices for the protection of athletes during their performance (such as masks, gloves, mouth pieces).Photography, Dental: Photographic techniques used in ORTHODONTICS; DENTAL ESTHETICS; and patient education.Mouth: The oval-shaped oral cavity located at the apex of the digestive tract and consisting of two parts: the vestibule and the oral cavity proper.Facial Injuries: General or unspecified injuries to the soft tissue or bony portions of the face.Tooth: One of a set of bone-like structures in the mouth used for biting and chewing.Maxilla: One of a pair of irregularly shaped bones that form the upper jaw. A maxillary bone provides tooth sockets for the superior teeth, forms part of the ORBIT, and contains the MAXILLARY SINUS.Patents as Topic: Exclusive legal rights or privileges applied to inventions, plants, etc.Dipeptides: Peptides composed of two amino acid units.Inventions: A novel composition, device, or process, independently conceived de novo or derived from a pre-existing model.Intellectual Property: Property, such as patents, trademarks, and copyright, that results from creative effort. The Patent and Copyright Clause (Art. 1, Sec. 8, cl. 8) of the United States Constitution provides for promoting the progress of science and useful arts by securing for limited times to authors and inventors, the exclusive right to their respective writings and discoveries. (From Black's Law Dictionary, 5th ed, p1014)Cholera Toxin: An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells, and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells.Foramen Ovale, Patent: A condition in which the FORAMEN OVALE in the ATRIAL SEPTUM fails to close shortly after birth. This results in abnormal communications between the two upper chambers of the heart. An isolated patent ovale foramen without other structural heart defects is usually of no hemodynamic significance.T-2 Toxin: A potent mycotoxin produced in feedstuffs by several species of the genus FUSARIUM. It elicits a severe inflammatory reaction in animals and has teratogenic effects.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Tetanus Toxin: Protein synthesized by CLOSTRIDIUM TETANI as a single chain of ~150 kDa with 35% sequence identity to BOTULINUM TOXIN that is cleaved to a light and a heavy chain that are linked by a single disulfide bond. Tetanolysin is the hemolytic and tetanospasmin is the neurotoxic principle. The toxin causes disruption of the inhibitory mechanisms of the CNS, thus permitting uncontrolled nervous activity, leading to fatal CONVULSIONS.Botulinum Toxins, Type A: A serotype of botulinum toxins that has specificity for cleavage of SYNAPTOSOMAL-ASSOCIATED PROTEIN 25.Protein Engineering: Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Tissue Engineering: Generating tissue in vitro for clinical applications, such as replacing wounded tissues or impaired organs. The use of TISSUE SCAFFOLDING enables the generation of complex multi-layered tissues and tissue structures.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Genetic Engineering: Directed modification of the gene complement of a living organism by such techniques as altering the DNA, substituting genetic material by means of a virus, transplanting whole nuclei, transplanting cell hybrids, etc.Research: Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Crystallization: The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Crystallography: The branch of science that deals with the geometric description of crystals and their internal arrangement. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
(1/73) Calorimetric studies on the stability of the ribosome-inactivating protein abrin II: effects of pH and ligand binding.

The effects of pH and ligand binding on the stability of abrin II, a heterodimeric ribosome-inactivating protein, and its subunits have been studied using high-sensitivity differential scanning calorimetry. At pH7.2, the calorimetric scan consists of two transitions, which correspond to the B-subunit [transition temperature (Tm) 319.2K] and the A-subunit (Tm 324.6K) of abrin II, as also confirmed by studies on the isolated A-subunit. The calorimetric enthalpy of the isolated A-subunit of abrin II is similar to that of the higher-temperature transition. However, its Tm is 2.4K lower than that of the higher-temperature peak of intact abrin II. This indicates that there is some interaction between the two subunits. Abrin II displays increased stability as the pH is decreased to 4.5. Lactose increases the Tm values as well as the enthalpies of both transitions. This effect is more pronounced at pH7.2 than at pH4.5. This suggests that ligand binding stabilizes the native conformation of abrin II. Analysis of the B-subunit transition temperature as a function of lactose concentration suggests that two lactose molecules bind to one molecule of abrin II at pH7.2. The presence of two binding sites for lactose on the abrin II molecule is also indicated by isothermal titration calorimetry. Plotting DeltaHm (the molar transition enthalpy at Tm) against Tm yielded values for DeltaCp (change in excess heat capacity) of 27+/-2 kJ.mol-1.K-1 for the B-subunit and 20+/-1 kJ.mol-1.K-1 for the A-subunit. These values have been used to calculate the thermal stability of abrin II and to surmise the mechanism of its transmembrane translocation.  (+info)

(2/73) Restoration of lectin activity to an inactive abrin B chain by substitution and mutation of the 2 gamma subdomain.

Abrin is a heterodimeric plant protein that occurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believed to either have (abrin-a and abrin-d) or lack (abrin-b and abrin-c) the ability to bind galactose. The 5' signal sequence and toxin B chain (ATB)-coding region were excised from a preproabrin cDNA [K. A. Wood, J. M. Lord, E. J. Wawrzynczak, and M. Piatak (1991) Eur. J. Biochem. 198, 723-732], tentatively identified as abrin-c, which was predicted to lack lectin activity, and fused in-frame to generate pre-ATB cDNA. Transcripts, synthesized in vitro from pre-ATB cloned into the transcription vector pSP64T, were expressed after microinjection into Xenopus oocytes. The recombinant ATB was shown, using a qualitative sugar-binding assay, to be devoid of lectin activity. Lectin activity could not be restored to this nonbinding ATB by replacing the 2 gamma subdomain with the corresponding galactose-binding 2 gamma subdomain from ricin B chain, but it was restored by replacement with the active galactose-binding 2 gamma subdomain from a different abrin isoform (abrin-a). The putative galactose-binding pocket of the nonbinding ATB 2 gamma subdomain contained a His residue at the position occupied by a residue with an aromatic side chain (Tyr or Trp) in functional 2 gamma subdomains. Mutationally converting this His to either Tyr or Trp restored lectin activity to the nonbinding ATB, emphasizing the contribution of an aromatic side chain in a functional 2 gamma subdomain galactose-binding site for members of this lectin family.  (+info)

(3/73) Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA: structural similarity to the B-chain from plant lectin, ricin.

CEL-III, a galactose/N-acetylgalactosamine (Gal/GalNAc) specific lectin purified from a marine invertebrate Cucumaria echinata has a strong hemolytic activity especially toward human and rabbit erythrocytes. We determined the primary structure of the CEL-III by examining the amino acid sequences of the protein and the nucleotide sequence of the cDNA. The cDNA encoding CEL-III has 1823 nucleotides and an open reading frame of 1296 nucleotides. CEL-III is composed of 432 amino acid residues with a M(r) of 47 inverted question mark omitted inverted question mark457 and has six internal tandem repeats, each with of 40-50 amino acids, comprising the N-terminal two-thirds of the molecule. Similar repeats are found in the B-chains of cytotoxic plant lectins, such as ricin and abrin, where six repetitive sequences extend throughout the molecules. A hydropathy plot predicts hydrophobic segments in the C-terminal region of CEL-III. These findings suggest that the N-terminal region of CEL-III plays an important role in binding to carbohydrate receptors on the target cell membranes, an event which triggers an intermolecular hydrophobic interaction of the C-terminal region, the result being oligomerization of CEL-III to lead to pore-formation in erythrocyte membrane.  (+info)

(4/73) Primary structure and function analysis of the Abrus precatorius agglutinin A chain by site-directed mutagenesis. Pro(199) Of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity.

Abrus agglutinin (AAG), a low-toxicity protein from the plant Abrus precatorius, is less lethal than abrina (ABRa) in mice (LD(50) = 5 mg/kg versus 20 microg/kg of body weight). Nucleotide sequence analysis of a cDNA clone encoding full-length AAG showed an open reading frame with 1641 base pairs, corresponding to a 547-amino acid residue preproprotein containing a signal peptide and a linker region (two amino acid residues) between the AAG-A and AAG-B subunits. AAG had high homology to ABRa (77.8%). The 13 amino acid residues involved in catalytic function, which are highly conserved among abrins and ricins, were also conserved within AAG-A. The protein synthesis inhibitory activity of AAG-A (IC(50) = 3.5 nM) was weaker than that of ABRa-A (0.05 nM). Molecular modeling followed by site-directed mutagenesis showed that Pro(199) of AAG-A, located in amphiphilic helix H and corresponding to Asn(200) of ABRa-A, can induce bending of helix H. This bending would presumably affect the binding of AAG-A to its target sequence, GpApGpAp, in the tetraloop structure of the 28 S rRNA subunit and could be one of the major factors contributing to the relatively weak protein synthesis inhibitory activity and toxicity of AAG.  (+info)

(5/73) Abrin triggers cell death by inactivating a thiol-specific antioxidant protein.

Abrin A-chain (ABRA) inhibits protein synthesis by its N-glycosidase activity as well as induces apoptosis, but the molecular mechanism of ABRA-induced cell death has been obscure. Using an ABRA mutant that lacks N-glycosidase activity as bait in a yeast two-hybrid system, a 30-kDa antioxidant protein-1 (AOP-1) was found to be an ABRA(E164Q)-interacting protein. The interaction was further confirmed in vitro by a glutathione S-transferase pull-down assay. The colocalization of endogenous AOP-1 and exogenous ABR proteins in the cell was demonstrated by confocal immunofluorescence. We also demonstrated that ABRA attenuates AOP-1 antioxidant activity in a dose-dependent manner and the intracellular level of reactive oxygen species (ROS) increases in ABR-treated cells. Moreover, ROS scavengers N-acetylcysteine and 4-hydroxy-2,2,6,6-tetramethylpiperidine-1-oxyl delayed programmed cell death. This indicates that ROS are important mediators of ABR-induced apoptosis. When ectopically expressed, AOP-1 blocked the release of cytochrome c and prevented apoptosis in ABR-treated cells. These findings suggest that the binding of ABRA to AOP-1 promotes apoptosis by inhibiting the mitochondrial antioxidant protein AOP-1, resulting in the increase of intracellular ROS and the release of cytochrome c from the mitochondria to the cytosol, which activates caspase-9 and caspase-3.  (+info)

(6/73) Ribosome inactivation by the toxic lectins abrin and ricin. Kinetics of the enzymic activity of the toxin A-chains.

A sensitive test system for toxin-treated ribosomes was worked out by treating rabbit reticulocyte ribosomes with abrin A-chain, ricin A-chain or ricinus agglutinin A-chain, adding neutralizing amounts of specific antitoxins and testing for polyphenylalanine-synthesizing activity in a system where the concentration of elongation factors and ribosomes were varied. The strongest inhibition was obtained in the presence of low concentrations of elongation factor (EF-2). The activity of the ribosomes decreased with time of incubation with the toxin A-chains. Addition of anti-toxins stopped further inactivation. In systems containing untreated and toxin-treated ribosomes the ability to polymerize phenylalanine was proportional to the concentration of untreated ribosomes. There was a linear relationship between toxin A-chain concentration and the number of ribosomes inactivated per minute. The inactivation rate increased with temperature, and the estimated activation energy was 10.6 kcal (44.3 kJ). Linewaver-Burk plots of the data obtained by incubating various ribosome concentrations with toxins indicated a molecular activity of about 1500 ribosomes/minute for abrin and ricin A-chains and 100 ribosomes/minute for ricinus agglutinin A-chain. The apparent Michaelis constant was 0.1-0.2 muM for all three A-chains. The activity of the A-chains in the intact cell is discussed.  (+info)

(7/73) Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro.

The eye lens small heat shock proteins (sHSP), alphaA- and alphaB-crystallins, have been shown to function like molecular chaperones, both in vitro and in vivo. It is essential to assess the protective effect of alphaA- and alphaB-crystallins under native conditions to extrapolate the results to in vivo conditions. Insulin and alpha-lactalbumin have widely been used to investigate the chaperone mechanism of alpha-crystallin under native conditions. Due to its smaller size, insulin B-chain may not represent the binding of putative physiological substrate proteins. As it stands, the aggregation of alpha-lactalbumin and binding of alpha-crystallin to it varies under different experimental conditions. Abrin, a ribosome inactivating protein isolated from the seeds of Abrus precatorius, consists of a 30 kDa A-chain and a lectin-like B-chain of 33 kDa joined by a single disulfide bond. Reduction of the disulfide link between the two chains of abrin leads to the aggregation of the B-chain. In this study, we demonstrate that dithiothreitol (DTT)-induced aggregation of abrin B-chain could be monitored by light scattering similar to that of insulin. Moreso, this process could be suppressed by recombinant human alphaA- and alphaB-crystallins in a concentration dependent manner, notably by binding to aggregation prone abrin B-chain. SDS-PAGE and HPLC gel filtration analysis indicate that there is a soluble complex formation between alpha-crystallin and abrin B-chain. Interestingly, in contrast to insulin, there is no significant difference between alphaA- and alphaB-crystallin in suppressing the aggregation of abrin B-chain at two different temperatures (25 and 37 degrees C). HSP26, an another small heat shock/alpha-crystallin family protein, was also able to prevent the DTT-induced aggregation of abrin. These results suggest that due to relatively larger size of its B-chain (33 kDa), compared to insulin B-chain (about 3 kDa), abrin may serve as a better model substrate for in vitro chaperone studies of alpha-crystallin and as well as other sHSP.  (+info)

(8/73) Cloning, expression of the abrin-a A-chain in Escherichia coli and measurement of the biological activities in vitro.

The coding sequence of abrin-a A-chain (ABRaA) gene was obtained by RT-PCR and cloned into the expression vector pET28b. The mature ABRaA has been highly expressed in the cytoplasm of Escherichia coli by 1 mmol/L IPTG induction, and the yield of the soluble recombinant protein was 4 mg/L of induced culture. The recombinant ABRaA was purified to be homogeneity. The biological activities of expressed ABRaA were demonstrated in vitro. It strongly inhibited the protein biosynthesis of rabbit reticulocyte lysates, with an IC(50) of 0.08 nmol/L. It also depurinated 28 S rRNA through cleaving at the A4324 site in rat liver ribosomes by its N-glycosidase activity. These data suggested that the recombinant ABRaA could be used for the preparation of immunotoxins as a potential cancer chemotherapeutic agent.  (+info)

*  Abrin
... is not known to have been weaponised. Abrin naturally occurs in the seeds of the rosary pea, a plant common to tropical ... Abrin has been shown to act as an immunoadjuvant in the treatment of cancer in mice. Abrin works by penetrating the cells of ... Abrin is a water-soluble lectin. Abrin in powdered form is yellowish-white. It is a stable substance and can withstand extreme ... Abrin at the US National Library of Medicine Medical Subject Headings (MeSH) "Abrin: Biotoxin". The Emergency Response Safety ...
*  List of cities, towns and villages in Sistan and Baluchestan Province
Abrin , Abtar , Abzan , Achkidar , Achu Bazar , Adamabad-e Baluchi Now , Adelabad , Adernag , Adimi , Adireh , Afghan , ...
*  Toxalbumin
Typical toxalbumins are abrin and ricin. Ingestion of seed containing toxalbumins is not necessarily fatal as the hard seed ...
*  Fūrin Kazan (Taiga drama)
Fūrin Kazan (風林火山) was the 46th NHK Taiga drama beginning on January 7, 2007. It was aired throughout 2007. The story, to a large extent, was an adaptation of Yasushi Inoue's 1959 historical novel of the same title (published in English under the title The Samurai Banner of Furin Kazan). The four characters of the title, from left to right are wind, woods, fire, and mountain. The title is a reference to the war banner used by Takeda Shingen, which in turn was taken from Sun Tzu's The Art of War. It means "Swift as the Wind, Silent as a Forest, Fierce as Fire and Immovable as a Mountain." Like many of the previous Taiga dramas, Fūrin Kazan deals with the Sengoku period. Based on Yasushi Inoue's novel by the same title, it depicts the life of Yamamoto Kansuke who is known as one of Takeda Shingen's renowned strategists. Original : Yasushi Inoue Screenwriter : Sumio Ōmori Music : Akira Senju Titling : Kōji Kakinuma Narrator : Sachiko Kagami Historical research : Shunroku Shibatsuji ...
*  Sfida për Shqipërinë
SFIDA! për Shqipërinë (CHALLENGE! for Albania or simply SFIDA!) is an Albanian political party, founded in 2016. SFIDA is an anti-establishment party that promotes direct democracy, mandate limitation and vetting for politicians. SFIDA is a follow-up of the movement "Ne, Tirana" which supported Gjergj Bojaxhi during local elections in 2015 where he ran as an independent candidate for Tirana's city hall. The party does not have a traditional leader. Instead this role is split between an administrative chairman (held by Hektor Ruci) and a political representative, Gjergj Bojaxhi. In June 2015, Bojaxhi ran as an independent candidate in the local elections for the city hall of Tirana. This candidacy was supported by an organized civil movement called "Ne, Tirana". The elections were won by Erion Veliaj, however Bojaxhi won over 16,000 votes. Based on this significant public support, in 2016 Bojaxhi and several other founders created "SFIDA! për Shqipërinë" in order to extend "Ne, Tirana" to a ...
*  PRDX3
Shih SF, Wu YH, Hung CH, Yang HY, Lin JY (2001). "Abrin triggers cell death by inactivating a thiol-specific antioxidant ...
*  Abrus precatorius
The toxin abrin is a dimer consisting of two protein subunits, termed A and B. The B chain facilitates abrin's entry into a ... One molecule of abrin will inactivate up to 1,500 ribosomes per second. Symptoms are identical to those of ricin, except abrin ... Abrin has an LD50 of only 0.56 μg/kg in mice, and Kingsbury lists a toxic dose in humans at 0.00015% body weight, or ... though the abrin in ingested seeds may be absorbed much more slowly than the ricin in Ricinus communis even if the seeds are ...
*  Ribosome-inactivating protein
Examples include: Abrin Beetin Ricin Saporin Shiga toxin Spiroplasma proteins Trichosanthin They exist in bacteria and plants. ... agglutinin and abrin) ribosome inactivating proteins (RIPs). All these toxins are structurally related. RIPs have been of ...
*  Ricin
Abrin (similar to ricin but even more toxic) Incidents involving ricin European mistletoe "What Makes Ricin So Deadly[1] - What ... Kuntal Patel from London attempted to poison her "controlling and selfish" mother with abrin after the latter interfered with ...
*  Humoral immunity
In 1897, Paul Ehrlich showed that antibodies form against the plant toxins ricin and abrin, and proposed that these antibodies ...
*  Saporin
Among the RIPs are some of the most toxic molecules known, including ricin and abrin (the latter is the poison preferred by the ...
*  Lectin
Abrin from the jequirity pea is similar: One domain is a lectin that binds cell surface galactosyl residues and enables the ...
*  Biosecurity in the United States
HHS SELECT AGENTS AND TOXINS) Abrin Cercopithecine herpesvirus 1 (Herpes B Virus) Coccidioides posadasii Conotoxins Crimean- ...
*  Viscum album
The structure of this protein is very similar to other RIPs, showing the most resemblance to ricin and abrin European mistletoe ...
*  Select agent
Abrin Botulinum neurotoxins* Clostridium perfringens epsilon toxin Conotoxins Ricin Saxitoxin Shiga-like ribosome inactivating ...
Abrus precatorius - definition of Abrus precatorius by The Free Dictionary  Abrus precatorius - definition of Abrus precatorius by The Free Dictionary
Abrin and agglutinin, lectins from the seeds of Abrus precatorius are type II ribosome-inactivating proteins that inhibit ... It has been reported that Abrus abrin, isolated from the seeds of Abrus precatorius, showed in vitro and in vivo antitumor ... Inhibitory effect of Abrus abrin-derived peptide fraction against Dalton's lymphoma ascites model ...
more infohttp://www.thefreedictionary.com/Abrus+precatorius
Saga/Red Lucky Seed (Abrus precatorius Linn) | CCRC  Saga/Red Lucky Seed (Abrus precatorius Linn) | CCRC
Abrin and agglutinin-I from the seeds of Abrus precatorius are type II ribosome-inactivating proteins that inhibit protein ... Abrin and agglutinin-I from the seeds of Abrus precatorius are type II ribosome-inactivating proteins that inhibit protein ... Structure-Function Analysis and Insights into the Reduced Toxicity of Abrus precatorius Agglutinin I in Relation to Abrin, The ... Structure-Function Analysis and Insights into the Reduced Toxicity of Abrus precatorius Agglutinin I in Relation to Abrin, The ...
more infohttp://ccrc.farmasi.ugm.ac.id/en/?page_id=129
Abrin - Wikipedia  Abrin - Wikipedia
Abrin is not known to have been weaponised. Abrin naturally occurs in the seeds of the rosary pea, a plant common to tropical ... Abrin has been shown to act as an immunoadjuvant in the treatment of cancer in mice. Abrin works by penetrating the cells of ... Abrin is a water-soluble lectin. Abrin in powdered form is yellowish-white. It is a stable substance and can withstand extreme ... Abrin at the US National Library of Medicine Medical Subject Headings (MeSH) "Abrin: Biotoxin". The Emergency Response Safety ...
more infohttps://en.wikipedia.org/wiki/Abrin
Abrin Poisoning | SpringerLink  Abrin Poisoning | SpringerLink
Abrin is highly toxic, with an estimated human fatal... ... Abrin is a toxic protein obtained from the seeds of Abrus ... Many of the features observed in abrin poisoning can be explained by abrin-induced endothelial cell damage, which causes an ... Experimental studies have shown that vaccination with abrin toxoid may offer some protection against a subsequent abrin ... Toxicity of abrin and ricin in mice and dogs. J Toxicol Environ Health 1979; 5: 1073-84PubMedCrossRefGoogle Scholar ...
more infohttps://link.springer.com/article/10.2165/00139709-200322030-00002
Abrin
     Summary Report | CureHunter  Abrin Summary Report | CureHunter
Abrin: A toxic lectin from the seeds of jequirity, Abrus precatorius L. Very active poison. Five different proteins have so far ... Abrin. Subscribe to New Research on Abrin A toxic lectin from the seeds of jequirity, Abrus precatorius L. Very active poison. ... 07/01/1982 - "Studies on the mechanisms of the immunizing effect with the abrin-treated tumor cells demonstrated that abrin ... 05/18/1988 - "In the melanoma and Rael cells, the indirect method gave a higher cell kill than even native abrin. ". 12/01/1987 ...
more infohttp://www.curehunter.com/public/keywordSummaryD000036-Abrin.do
Toxins | Free Full-Text | Simultaneous Detection of Ricin and Abrin DNA by Real-Time PCR (qPCR)  Toxins | Free Full-Text | Simultaneous Detection of Ricin and Abrin DNA by Real-Time PCR (qPCR)
Therefore, we have developed a duplex real-time PCR assays for simultaneous detection of ricin and abrin DNA based on the ... However, as the production of highly purified ricin or abrin requires sophisticated equipment and knowledge, it may be more ... The suitability of the assays was exemplified by detection of ricin and abrin contaminations in a food matrix. ... probability of detection at 3 genomes per reaction for ricin DNA and 1.2 genomes per reaction for abrin DNA. ...
more infohttp://www.mdpi.com/2072-6651/4/9/633
Biological activities of the lectin abrin-a, against human lymphocytes and cultured leukemic cell lines  - ABIM - An Annotated...  Biological activities of the lectin abrin-a, against human lymphocytes and cultured leukemic cell lines - ABIM - An Annotated...
Biological activities of the lectin abrin-a, against human lymphocytes and cultured leukemic cell lines ... Biological activities of the lectin abrin-a against human lymphocytes and cultured leukemic cell lines. ... Biological activities of the lectin abrin-a, against human lymphocytes and cultured leukemic cell lines. [Publication] ...
more infohttp://indianmedicine.eldoc.ub.rug.nl/21633/
How to Get Rid of Back Fat: 10 Steps (with Pictures) - wikiHow  How to Get Rid of Back Fat: 10 Steps (with Pictures) - wikiHow
How to Get Rid of Back Fat. The back is one of the hardest places to tone and decrease body fat when you're trying to lose weight. Unfortunately, it's not possible to 'spot treat' any part of your body.http://www.medicaldaily.com/weight-...
more infohttps://www.wikihow.com/Get-Rid-of-Back-Fat
Toxins | Free Full-Text | Llama-Derived Single Domain Antibodies Specific for Abrus Agglutinin  Toxins | Free Full-Text | Llama-Derived Single Domain Antibodies Specific for Abrus Agglutinin
... a recombinant abrin A-chain), purified abrin fractions, Abrus agglutinin (a protein related to abrin but with lower toxicity), ... Abrin is a potent toxin similar to ricin in structure, sequence and mechanism of action. The selected sdAb were evaluated for ... The best binders were specific for the Abrus agglutinin, showing minimal binding to purified abrin fractions or unrelated ... Used in conjunction with anti-abrin monoclonal and polyclonal antibodies, these reagents can fill a role to discriminate ...
more infohttps://www.mdpi.com/2072-6651/3/11/1405
Call for continuous collection of chemical contaminants occurrence  Call for continuous collection of chemical contaminants occurrence
Background In the framework of Articles 23 and 33 of Regulation (EC) No 178/2002 EFSA has received from the European Commission a mandate (M-2010-0374) to
more infohttps://www.efsa.europa.eu/en/consultations/call/180307
Patente US5469865 - Mouthguard having an extra-oral portion and an intra-oral portion - Google Patentes  Patente US5469865 - Mouthguard having an extra-oral portion and an intra-oral portion - Google Patentes
Billy Abrin. Method of fitting dentures. US2693182 *. 9 Sep 1953. 2 Nov 1954. Phillips John W. Oro-tracheal tube positioner and ...
more infohttp://www.google.es/patents/US5469865?dq=flatulence
Patente US5533524 - Mouthguard having an extra-oral portion and an intra-oral portion - Google Patentes  Patente US5533524 - Mouthguard having an extra-oral portion and an intra-oral portion - Google Patentes
Billy Abrin. Method of fitting dentures. US2693182 *. 9 Sep 1953. 2 Nov 1954. Phillips John W. Oro-tracheal tube positioner and ...
more infohttp://www.google.es/patents/US5533524?dq=flatulence
Category:Ribbon diagrams - Wikimedia Commons  Category:Ribbon diagrams - Wikimedia Commons
Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. ...
more infohttps://commons.wikimedia.org/wiki/Category:Ribbon_diagrams
Optometrist Licensure Examination | Philstar.com  Optometrist Licensure Examination | Philstar.com
136 LACISTE, CLARICE AMOR ABRIN. 137 LACUANAN, MEAGAN LEIGH SEGOCIO. 138 LAHOM, ERIKA PRINCESS GARCIA ...
more infohttps://www.philstar.com/exam-results/2019/07/25/1937760/optometrist-licensure-examination
Anticancer Activity of Uncommon Medicinal Plants from the Republic of Suriname: Traditional Claims, Preclinical Findings, and...  Anticancer Activity of Uncommon Medicinal Plants from the Republic of Suriname: Traditional Claims, Preclinical Findings, and...
However, they are very toxic because of their high content of the toxalbumin abrin, and ingestion of a single well-chewed seed ... Importantly, administration of Meth-A tumor cells which had been treated in vitro with abrin, induced strong antitumor immunity ... On the other hand, this mechanistic feature of abrin presents the opportunity of inhibiting the proliferation of cancerous ... Support for this presumption came from the immunopotentiating and immunostimulatory properties of abrin [107, 110] and the ...
more infohttps://www.intechopen.com/books/pharmacognosy-medicinal-plants/anticancer-activity-of-uncommon-medicinal-plants-from-the-republic-of-suriname-traditional-claims-pr
Chemophobia - RationalWiki  Chemophobia - RationalWiki
and Abrin. *↑ Alex Jones: Chemicals in the water are turning "the freaking frogs gay Right Wing Talk (YouTube) ...
more infohttps://rationalwiki.org/wiki/Chemophobia
Federal Select Agent Program - Select Agents and Toxins List  Federal Select Agent Program - Select Agents and Toxins List
Abrin5. *Bacillus cereus Biovar anthracis*. * Botulinum neurotoxins*,5. * Botulinum neurotoxin producing species of Clostridium ...
more infohttps://www.selectagents.gov/selectagentsandtoxinslist.html
Toxins of Biological Origin  Toxins of Biological Origin
Abrin. 1000 mg. Botulinum neurotoxins. 1 mg. Short, paralytic alpha conotoxins. 100 mg. ...
more infohttp://www.ehs.ufl.edu/programs/bio/toxins/
  • Experimental studies have shown that vaccination with abrin toxoid may offer some protection against a subsequent abrin challenge, although such an approach is unlikely to be of benefit in a civilian population that in all probability would be unprotected. (springer.com)
  • Llama derived single domain antibodies (sdAb), the recombinantly expressed variable heavy domains from the unique heavy-chain only antibodies of camelids, were isolated from a library derived from llamas immunized with a commercial abrin toxoid preparation. (mdpi.com)
  • 77: 1247-1253, 1986) that the sensitivities of different melanoma cell lines to a conjugate of abrin with the anti-melanoma antibody 9.2.27 was correlated with their sensitivities to native abrin. (curehunter.com)
  • Abrin naturally occurs in the seeds of the rosary pea, a plant common to tropical regions that is occasionally employed as an herbal remedy for certain conditions. (wikipedia.org)
  • This satisfies one criterion of a potential chemical warfare agent, although the lack of large scale production of jequirity seeds means that quantity is unavailable for ready mass production of abrin for weapons. (springer.com)
  • Abrin works by penetrating the cells of the body and inhibiting cell protein synthesis. (wikipedia.org)
  • By attaching to a carbohydrate chain on the cell surface, the abrin molecule anchors itself to the cell, is subsequently engulfed and enters the inner parts of the cell where it reacts with a ribosomal subunit and interferes with the normal protein synthesis process of the cell. (wikipedia.org)
  • At the cellular level, abrin inhibits protein synthesis, thereby causing cell death. (springer.com)
  • Many of the features observed in abrin poisoning can be explained by abrin-induced endothelial cell damage, which causes an increase in capillary permeability with consequent fluid and protein leakage and tissue oedema (the so-called vascular leak syndrome). (springer.com)
  • However, as the production of highly purified ricin or abrin requires sophisticated equipment and knowledge, it may be more likely that crude extracts would be used by non-governmental perpetrators. (mdpi.com)