ライフサイエンスコーパス: ricin

1 he activity of cholera toxin but not that of ricin.

2 in, which has mechanism of action similar to ricin.

3 e susceptibility of human cells to the toxin ricin.

4 tected mice from lethal nasal challenge with ricin.

5 and thus inhibit the biological activity of ricin.

6 The best known example of type 2 RIPs is ricin.

7 powdered milk has a high binding affinity to ricin.

8 rest in identifying effective inhibitors for ricin.

9 This assay detects as little as 30pg of ricin.

10 plant, has similar structure and function as ricin.

11 confer both systemic and mucosal immunity to ricin.

12 sting macrophages may be a primary target of ricin.

13 ing in the inflammatory process triggered by ricin.

14 rticular was found to be highly specific for ricin.

15 We recently showed that ricin A chain (RTA) interacts with the P1 and P2 protein

16 to the endoplasmic reticulum (ER), where the ricin A chain (RTA) must cross the ER membrane to reach

17 plexes and C-terminally truncated forms with ricin A chain (RTA), which binds to the stalk to depurin

18 The method allows for identification of ricin A chain and B chain and for distinction of ricin f

19 Ricin A chain can cause toxicity by inhibiting protein s

20 Remarkably, ricin A chain dislocation occurred via a membrane-integr

21 The data support a model in which ricin A chain dislocation occurs via a novel strategy of

22 To study the molecular processes of ricin A chain dislocation, we have established, for the

23 lected on ricin were found to bind to either ricin A chain or the intact molecule; no ricin B chain b

24 ICs containing deglycosylated ricin A chain prepared from ricin toxin extracted from c

25 Subsequently, the ricin A chain traverses the ER bilayer by a process refe

26 this human cell-based system, we found that ricin A chains underwent a rapid dislocation event that

27 lamas, are known to have high affinities for ricin A or B chains and low cross-reactivity with RCA 12

28 Ricin A-chain (RTA) and saporin-L1 (SAP) catalyze adenos

29 tandard, namely, the uniformly (15)N-labeled ricin A-chain produced recombinantly in a bacterial expr

30 tibody is a full-length IgG and binds to the ricin A-chain subunit with a high affinity (KD=53pM).

31 security as the seeds contain high levels of ricin, a highly toxic, ribosome-inactivating protein.

32 Retro-2 that showed mouse protection against ricin, a notorious ribosome inactivating protein (RIP).

33 (HA) as a model protein and then applied to ricin, a potent protein toxin extracted from the castor

34 sonance (SPR) was used to monitor binding of ricin, a ribosome-inactivating protein, to the plasma me

35 Ricin, a toxic protein from the castor plant, is of fore

36 me-inactivating proteins (RIPs) family (e.g. ricin, abrin) are potent cytotoxins showing a strong let

37 The potent toxins ricin, abrin, and other ribosome-inactivating proteins d

38 the RIP-II family of plant proteins, such as ricin, abrin, viscumin, and volkensin was based on their

39 We then monitored the movement of ricin across polarized human HCT-8 intestinal monolayers

40 ming a role for this enzyme in intracellular ricin activation.

41 We report a single-step, real-time ricin activity assay that requires little or no sample p

42 The inhibitory effect of milk on ricin activity in Vero cells was at the same level as by

43 The ricin activity is determined by detecting the unique cle

44 Ricin added to beverage matrices was extracted using ant

45 We first showed that ricin adhered in a specific pattern to human small bowel

46 We demonstrated previously that ricin administered to the lungs of mice causes death of

47 to the alveolar region of human lungs, where ricin aerosol particles mostly accumulate.

48 nd B chain and for distinction of ricin from ricin agglutinin within a single analytical run.

49 dimers that were most effective at promoting ricin aggregation in solution were also the most effecti

50 o a case involving the illegal production of ricin and abrin toxins.

51 he cell intoxication operated by type 2 RIPs ricin and abrin.

52 us (jequirity seeds)--the natural sources of ricin and abrin.

53 ing system for rapid differentiation between ricin and agglutinin done in real time.

54 Ricin and cholera toxins are known to hijack the protein

55 philia could be restored by co-administering ricin and exogenous IL-1beta to IL-1alpha/beta(-/-) mice

56 d mice and assessed them for the presence of ricin and for histological damage.

57 termining contamination of food product with ricin and human exposure to ricin is therefore an import

58 ort the development of a method that detects ricin and its activity in food or clinical samples.

59 The high toxicity of ricin and its ease of production have made it a major bi

60 the cytoprotective effect of Retro-2 against ricin and its inhibitory effect on ASNA1-mediated ER-tar

61 s of recurrent RNA 3D motifs (such as sarcin-ricin and kink-turn internal loops or T- and GNRA hairpi

62 Due to the potential use of ricin and other fast-acting toxins as agents of bioterro

63 are the roles of genes for susceptibility to ricin and Shiga toxin in different human cell lines and

64 ctively block endosome-to-Golgi retrieval of ricin and Shiga toxins and protect mice from ricin's dea

65 ut screening has shown that Retro-1 inhibits ricin and Shiga toxins by diminishing their intracellula

66 formation prior to exiting the cell, whereas ricin and Shiga-like toxins and some nonenveloped viruse

67 stances of GNRA tetraloop, kink-turn, sarcin-ricin and tandem-sheared motifs.

68 e VHH heterodimers had higher affinities for ricin and, in the case of heterodimer D10/B7, a 6-fold i

69 ay express multiple cell surface ligands for ricin and/or the inhibitor.

70 aeruginosa exotoxin A, Botulinum neurotoxin, ricin, and Zika virus.

71 Vero cells was at the same level as by anti-ricin antibodies.

72 thods for the detection of the protein toxin ricin are of interest to the law enforcement community.

73 s that the inflammatory effects triggered by ricin are responsible for its lethality.

74 Shiga-like toxins and ricin are ribosome-inactivating proteins (RIPs) that are

75 Qualitative methods to detect ricin are therefore needed.

76 B (SEB), shiga toxin (STX), and plant toxin ricin, are involved in a number of diseases and are cons

77 y the same degree of cell protection against ricin as (+/-)-Retro-2(cycl).

78 to establish the limit of detection for this ricin assay.

79 We were able to detect ricin at 100 pg/ml in buffer and at 1 ng/ml in spiked ap

80 edure yields an assay limit of detection for ricin at 42.5 ng on column or 21.25 ng/muL for a 2-muL i

81 We also found that (a) milk did not inhibit ricin at concentrations of 10 or 100 ng/ml; (b) autoclav

82 The Simoa was able to detect ricin at levels of 10 fg/mL, 100 fg/mL, and 1 pg/mL in b

83 recognition elements for direct detection of Ricin at temperatures great than 4 degrees C.

84 ion were also the most effective at blocking ricin attachment to cell surfaces.

85 ovalbumin-encapsulated AuNCs, can recognize ricin B because of the presence of Galbeta(1-->4)GlcNAc

86 oxicity by inhibiting protein synthesis, and ricin B can bind to the galactose ligand on the cell mem

87 her ricin A chain or the intact molecule; no ricin B chain binders were identified.

88 the proposed approach to selectively detect ricin B chain in complex samples.

89 and have characterized their binding to the ricin B chain.

90 , each of whose monomers consist of a single ricin B lectin domain with its beta-trefoil fold and one

91 The generated conjugates of AuNCs@ew and ricin B were heavy and readily settled down under centri

92 We have expressed CNL, a ricin B-like lectin from the basidiomycete Clitocybe neb

93 found to be thermal stable, regaining their ricin binding activity following heating to 85 degrees C

94 ing effectiveness of compounds at inhibiting ricin binding was ascertained by determining the IC(50)

95 ococcal enterotoxins A and B, cholera toxin, ricin, botulinum toxin A, and heat labile toxin of E. co

96 Milk also removes ricin bound to the microtiter plate.

97 Ricin-bound beads were also tested for deadenylase activ

98 The MCR allowed identification of ricin by signature peptides in all targeted mode injecti

99 Using Ricin Chain-A, a naturally occurring toxin, as a model a

100 their capacity to confer protection against ricin challenge in vivo was not determined.

101 of GD12 to serve as a therapeutic following ricin challenge was not explored in this study.

102 were able to completely protect mice against ricin challenge, even though the two classes of antibodi

103 red 100% survival in response to a 10 x LD50 ricin challenge, whereas a 2:1 heterodimer:toxin ratio c

104 ice against intraperitoneal and intragastric ricin challenges.

105 on of bioterrorism agents, as exemplified by ricin, cholera toxin (CT), and staphylococcal enterotoxi

106 and nonhuman primates have demonstrated that ricin delivered to the pulmonary system leads to acute l

107 for antibody affinity profiling and one-step ricin detection at concentrations down to 300 pM using a

108 Current ricin detection methods based on immunoassays lack the r

109 ricin, macrophage-depleted mice treated with ricin displayed a reduction in pulmonary IL-1beta.

110 the GTPase-associated center, and the sarcin/ricin domain (SRD) was determined.

111 duction and SDS denaturation in the isolated ricin domain and the larger fragment containing the rici

112 ajor epitope in the N-terminal cysteine-rich ricin domain of PLA2R that is recognized by 90% of human

113 Two peptides from the ricin domain showed strong inhibition, with a longer seq

114 Ricin enters cells via endocytosis, where only a minute

115 antibody VH domains (VHHs) specific for the ricin enzymatic (RTA) and binding (RTB) subunits.

116 omain and the larger fragment containing the ricin, fibronectin type II, first and second C-type lect

117 oped for detecting the highly lethal protein ricin from castor bean extract.

118 This method was used successfully to extract ricin from each beverage matrix.

119 ased methodologies are unable to distinguish ricin from RCA 120, a nontoxic protein also found in the

120 n A chain and B chain and for distinction of ricin from ricin agglutinin within a single analytical r

121 unknown samples requires differentiation of ricin from the highly homologous Ricinus communis agglut

122 Detection of ricin from unknown samples requires differentiation of r

123 addition, we harvested organs from unlabeled ricin-gavaged mice and assessed them for the presence of

124 re single copy, the number of members of the ricin gene family is larger than previously thought.

125 as a biowarfare agent and homicidal weapon, ricin has been classified as a category B bioterrorism a

126 Ricin has been proposed as a bioweapon because of its le

127 The toxic plant protein ricin has gained notoriety due to wide availability and

128 nd improve the ITs, different toxins such as ricin, have been used, aiming for higher efficacy agains

129 mers) had virtually identical affinities for ricin holotoxin and similar IC50 values in a Vero cell c

130 Ricin holotoxin did not bind ribosomes or depurinate the

131 Ricin holotoxin does not inhibit translation unless the

132 GD12 bound ricin holotoxin with high affinity (K(D) [dissociation c

133 erived from humans who had been treated with ricin immunotoxin.

134 itive analytical assays capable of detecting ricin in a variety of matrixes are urgently needed to li

135 100 ng/ml; (b) autoclaving 10 and 100 ng/ml ricin in DMEM at 121 degrees C for 30 min completely abo

136 nd toxicity of suspicious samples containing ricin in less than 30 minutes.

137 xin A, cholera toxin, botulinum toxin A, and ricin in model buffer (PBS-BSA) and 0.1 ng/mL for staphy

138 and convenient sensing methods for detecting ricin in suspicious samples must be developed.

139 ive mass spectrometry-based method to detect ricin in tap water, 2% milk, apple juice, and orange jui

140 racterized them for their ability neutralize ricin in vitro and in vivo.

141 s region of RTA were capable of neutralizing ricin in vitro, their capacity to confer protection agai

142 and B, cholera toxin, botulinum toxin A, and ricin increased 2- to 5-fold, while for LT the detection

143 loying mice deficient in IL-1, we found that ricin-induced inflammatory responses were suppressed, in

144 ignaling by corticospinal tract transection, ricin-induced motor neuron death, or neurodegeneration i

145 ient and approved treatment for poisoning by ricin inhalation, although there have been major improve

146 Ricin inhibits protein synthesis by depurinating the alp

147 chemistry values from buffer-treated versus ricin-intoxicated animals.

148 respiratory tract of mice 6h after pulmonary ricin intoxication allowed the rescue of 100% of intoxic

149 U145 reduced the sensitivity of the cells to ricin intoxication further confirming a role for this en

150 Although ricin intoxication is not transmittable from person to p

151 ntly no vaccine or therapeutic treatment for ricin intoxication, ultrasensitive analytical assays cap

152 Ricin is a family member of the lethal ribosome-inactiva

153 Ricin is a highly toxic protein produced by the castor p

154 Ricin is a highly toxic protein which causes cell death

155 Ricin is a lethal protein toxin derived from the castor

156 Ricin is a potent A-B toxin that is transported from the

157 Ricin is a potent ribotoxin considered to be a potential

158 Ricin is a potent toxin capable of inhibiting protein sy

159 Ricin is a potent toxin found in the beans of Ricinus co

160 Ricin is a ribosome inactivating protein that catalytica

161 Ricin is a select agent toxin and a member of the RNA N-

162 Ricin is an extremely potent ribosomal inactivating prot

163 In this method, the ricin is captured by a specific polycolonal antibody fol

164 ause of its high availability and lethality, ricin is considered a likely agent for bioterrorism.

165 Ricin is one of the most toxic plant toxins known.

166 ood product with ricin and human exposure to ricin is therefore an important public health goal.

167 mmalian cells, the heterodimeric plant toxin ricin is transported to the endoplasmic reticulum (ER),

168 The extreme potency of the plant toxin, ricin, is due to its enzymatic subunit, RTA, which inact

169 ws for a sensitive and selective analysis of ricin isolated from a food or clinical sample.

170 rt flexible linker: a catalytic domain and a ricin-like lectin carbohydrate binding domain.

171 domains: a catalytic domain and a C-terminal ricin-like lectin domain comprised of three potential Ga

172 so propose that mice intoxicated orally with ricin likely die from distributive shock.

173 rsally conserved adenine in the alpha-sarcin/ricin loop (SRL) and inhibit protein synthesis at the tr

174 mes and an RNA stem-loop mimic of the sarcin/ricin loop (SRL) at a higher catalytic rate and is a mor

175 cleavage of the universally conserved Sarcin-Ricin loop (SRL) in 23S rRNA.

176 The sarcin-ricin loop (SRL) is one of the longest conserved sequenc

177 A (rRNA) at the universally conserved sarcin-ricin loop (SRL) leading to complete inactivation of the

178 pact on structure formation using the sarcin-ricin loop (SRL) motif.

179 hibits translation by cleavage of the Sarcin-Ricin loop (SRL) of 23S ribosomal RNA at the same positi

180 ical RIP target site within the alpha-sarcin/ricin loop (SRL) of 28S rRNA.

181 lational GTPases (trGTPases) with the sarcin-ricin loop (SRL) of ribosomal RNA (rRNA) is pivotal for

182 ally conserved adenine from the alpha-sarcin/ricin loop (SRL) of the 28S rRNA.

183 n family site-specifically cleave the sarcin/ricin loop (SRL) on the ribosome to inhibit translation

184 o stalk P-proteins to reach the alpha-sarcin/ricin loop (SRL) where it cleaves a conserved adenine.

185 n synthesis by depurinating the alpha-sarcin/ricin loop (SRL).

186 to release a single adenine from the sarcin-ricin loop (SRL).

187 binds to the stalk to depurinate the sarcin/ricin loop (SRL).

188 the stalk in toxin recruitment to the sarcin/ricin loop and may provide a new target for inhibitor di

189 ractions, including those between the sarcin-ricin loop and the P loop of EF-Tu, and between the effe

190 interactions of restrictocin with the sarcin/ricin loop are particularly favorable.

191 rate of restrictocin to the isolated sarcin/ricin loop is electrostatically enhanced by approximatel

192 ific adenine residue in the conserved sarcin/ricin loop of 28S rRNA.

193 ves specific purine residues from the sarcin/ricin loop of large rRNA, arresting protein synthesis at

194 on of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA.

195 of the 30S subunit docks EF-Tu at the sarcin-ricin loop of the 50S subunit, activating EF-Tu for GTP

196 ne how individual ribose hydrogens of sarcin/ricin loop RNA participate in strand cleavage.

197 cupy the P site and extend toward the sarcin-ricin loop to interact with Tif6.

198 differences in the interaction of the sarcin ricin loop with the two elongation factors and (iii) net

199 ) share the same substrate, the alpha-sarcin/ricin loop, but differ in their specificities towards pr

200 ant rRNA regions, including the alpha-sarcin-ricin loop, have different relative positions within the

201 uberculosis that cuts 23S rRNA at the sarcin-ricin loop, VapC-mt4 selectively targets three of the 45

202 rtion of 28S rRNA intact at the alpha-sarcin/ricin loop.

203 to remove a specific adenine from the sarcin/ricin loop.

204 When compared with control mice treated with ricin, macrophage-depleted mice treated with ricin displ

205 Inhalation or ingestion of ricin may even lead to death.

206 LDI TOF MS-based activity assay that detects ricin mediated depurination of synthetic substrates was

207 ermore, IL1Ra/anakinra cotreatment inhibited ricin-mediated inflammatory responses, including recruit

208 rement for macrophages in the development of ricin-mediated pulmonary inflammation by employing trans

209 ittable from person to person, even a single ricin molecule can lead to cell necrosis because it inac

210 a endocytosis, where only a minute number of ricin molecules reach the endoplasmic reticulum (ER) lum

211 munosensor fabricated using the conventional Ricin monoclonal and polyclonal antibodies have also bee

212 nor-coaxial stacking combinations and sarcin/ricin motif variants.

213 We describe the development of an anti-ricin neutralizing monoclonal antibody (IgG 43RCA-G1) an

214 VHHs, V5E1, ranks as one of the most potent ricin-neutralizing antibodies described to date.

215 ess this question, we assessed the impact of ricin on the gastrointestinal tract and organs of mice a

216 549 cells resulted in a dramatic increase of ricin or abrin cytotoxicity compared with control mock-t

217 als for (15)N and natural isotopic abundance ricin peptides are distinct, with mass shifts that corre

218 the probability of detection for individual ricin peptides at different concentrations.

219 nce of Tween-20 did not prevent detection of ricin peptides, and indeed assays performed in buffers t

220 to be 53 +/- 2 pmol adenine per picomole of ricin per hour.

221 ng of transferrin, retrograde trafficking of ricin, phagolysosomal trafficking, or phagosome permeabi

222 Ribosome inactivating proteins (RIPs) like ricin, pokeweed antiviral protein (PAP) and Shiga-like t

223 Ricin produced from the castor oil plant, Ricinus commun

224 toxin, an examination of the activity of the ricin protein upon a DNA substrate that mimics the toxin

225 ter as capture reagents for the detection of ricin, providing a limit of detection in enzyme linked i

226 Ricin purification from the source castor seeds is essen

227 two plant toxins, recombinant A chains from ricin (RAC) and pulchellin (PAC) toxins, for their abili

228 any indication of enterocyte damage and that ricin rapidly reaches the kidneys of intoxicated mice.

229 se tight-binding inhibitors mimic the sarcin-ricin recognition loop of 28S rRNA and the dissociative

230 that milk can bind competitively to 1 ng/ml ricin, reducing the amount of toxin uptake by the cells,

231 is depleted from cell fraction preparations ricin reduction can still take place, indicating that al

232 emonstrated to be involved in the process of ricin reduction; however, when PDI is depleted from cell

233 We also present GI maps based on growth and ricin-resistance phenotypes, and we demonstrate how such

234 d by searching for kink-turn, C-loop, sarcin-ricin, reverse kink-turn and E-loop motifs against a 23S

235 ng GNRA tetraloop, kink-turn, C-loop, sarcin-ricin, reverse kink-turn, hook-turn, E-loop and tandem-s

236 ystal structures of the enzymatic subunit of ricin (RTA) in complex with the antigen binding domains

237 several of the sdAb were observed to bind to ricin's A chain, cell free translation assays were perfo

238 monitor the ability of the sdAbs to inhibit ricin's biological activity.

239 ricin and Shiga toxins and protect mice from ricin's deadly effects.

240 One challenge in the forensic analysis of ricin samples is determining the method and extent of sa

241 y (GC/MS) to assess compositional changes in ricin samples purified by different methods.

242 ll survival under selective conditions (i.c. ricin selection).

243 immunoglobulin E and the bioterrorist agent ricin, sequentially captured by the immobilized aptamer

244 Like Ricin, Shiga, and Cholera toxins, yeast K28 is an A/B to

245 eins while differentiating by injection of a ricin-specific antibody (R18) in a subsequent enhancemen

246 The two additional ricin-specific heterodimers, when tested in vivo, provid

247 urrent study we produced a new collection of ricin-specific VHH heterodimers, as well as VHH homodime

248 Among the 20 unique ricin-specific VHHs we identified, six had toxin-neutral

249 ters, the limit of detection of 0.2 ng/mL of ricin spiked in buffer and milk was accomplished, repres

250 e utility of this method was demonstrated on ricin spiked into food and clinical samples consisting o

251 e three potential biological warfare agents, ricin, staphylococcal enterotoxin B, and epsilon toxin,

252 A candidate ricin subunit vaccine (RiVax) consisting of a recombinan

253 d the assay to study enzymatic properties of ricin such as pH and temperature optima (pH 4.5-5.0 and

254 A GI map focused on ricin susceptibility broadly recapitulates known pathway

255 The LC-MS detection limit achieved for ricin target peptides was 10 amol and the corresponding

256 Depurination of the ribosomal sarcin-ricin tetraloop (GAGA) causes inhibition of protein synt

257 ntaining DADMeA and based on the GAGA sarcin-ricin tetraloop gave slow-onset tight-binding inhibition

258 geted by cytotoxins such as alpha-sarcin and ricin that completely abolish translation.

259 h is used as a model to study the binding of ricin to galactose cell-surface receptors.

260 Administration of aerosolized ricin to macrophage-depleted mice led to reduced inflamm

261 ethal dose of purified fluorescently-labeled ricin to mice by oral gavage and followed transit of the

262 These observations suggest that ricin toxicity may possibly be reduced at room temperatu

263 The small molecule Retro-2 prevents ricin toxicity through a poorly-defined mechanism of act

264 iously unidentified GIs between modifiers of ricin toxicity.

265 Ricin toxin (RT) is the second most lethal toxin known;

266 Ricin toxin A chain (RTA) binds to stalk P-proteins to r

267 sport to the endoplasmic reticulum (ER), and ricin toxin A chain (RTA) enters the cytosol from the ER

268 k is required for depurination of the SRL by ricin toxin A chain (RTA).

269 he light chain of Botulinum Neurotoxin A and Ricin Toxin A chain, which could be specifically and rep

270 ell system in which enzymatically attenuated ricin toxin A chains (RTA(E177D) and RTA(Delta177-181))

271 ithin a different surface pocket relative to ricin toxin A subunit and trichosanthin, suggesting diff

272 Ricin toxin A-chain (RTA) from castor beans catalyzes th

273 otein synthesis and induce cell death, plant ricin toxin and bacterial Shiga toxins enter the cell th

274 g deglycosylated ricin A chain prepared from ricin toxin extracted from castor beans were the most ef

275 -molecule array (Simoa) for the detection of ricin toxin in human urine and serum.

276 Rapid and sensitive detection of ricin toxin in various types of sample matrices is neede

277 Ricin toxin is a heterodimer consisting of RTA, a riboso

278 ormation required for the rational design of ricin toxin subunit vaccines.

279 city to protect human cells and mice against ricin toxin without toxicity.

280 enes affecting growth and sensitivity to the ricin toxin.

281 agnetic beads for the sensitive detection of ricin toxin.

282 n the development of countermeasures against ricin toxin.toxin, antibody, structure, intracellular.

283 tulinum, Clostridium difficile, anthrax, and ricin toxins.

284 e display library from llamas immunized with ricin toxoid and selected a number of single domain anti

285 We observed that, in both systems, ricin trafficked through the cells without apparent dama

286 We conclude that ricin transverses human intestinal cells and mouse intes

287 a stable-isotope-labeled standard for every ricin tryptic peptide in the sample.

288 Ricin undergoes retrograde transport to the endoplasmic

289 elow 100 pg/mL and excellent specificity for ricin versus the highly related RCA 120 (1 to 10 000).

290 The activity of recovered ricin was assessed, and quantification was achieved, wit

291 Depurination of the substrate by ricin was confirmed by matrix-assisted laser desorption

292 In the case of sdAb immunosensor, Ricin was detected in a linear range of 1log(fg/mL)-1log

293 inhomogeneous substrate herring sperm DNA by ricin was determined to be 53 +/- 2 pmol adenine per pic

294 eer countermeasures for the category B toxin ricin, we produced and characterized a collection of epi

295 Phage selected on ricin were found to bind to either ricin A chain or the

296 deglycosylated A chain prepared from native ricin were the most effective in killing cells, but thei

297 era toxin, staphylococcal enterotoxin B, and ricin) were 1.6, 0.064, and 1.6 ng/mL for the microflow

298 f RTA in vitro and protected Vero cells from ricin when expressed as intracellular antibodies ("intra

299 Unlike ricin, which is internalized into the cells via a galact

300 it possible to quantitatively detect active ricin with 3 orders of magnitude dynamic range.