Review Sheet for MCB 411 with Professor Fares at UA
Review Sheet for MCB 411 with Professor Fares at UA
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between 02 and 10 in nestlings As not all individuals were typed with the same set of microsatellite markers we calculated standardized individual heterozygositym proportion of heterozygous locimean hetero zygosity of typed lo ci This measure is used in all analyses and is referrm to as individual heterozygosityi for simplicity We also calculated two other previously suggested measures of individual genetic diversity internal relatednessm and mean dzevalue where a 2 is the squared length difference between the alleles at a locus Heterozygosity standardized heterozygosity and internal relatedness were highly correlated all r gt 089 P lt 0 0001 and all three measures led to similar conclusions data not shown Mean dzevalues were weakly correlated with the other measures 1 024e032 all P lt 00001 and explained comparatively little variation in individual tness The assumption that heterozygosity measured at a limited number of loci re ects genomeewide heterozygosity can be questioned Any relationship between average heterozygosity and tness mightbe due to close linkage between a microsatellite locus and loci coding for tnesserelated traits To check whether the effect of overall heterozygosity on tness depended on one or a few ofthe microsatellite loci we repeated all analyses for eachlocus separately data not shown Heterozygosity at six out of seven loci signi cantly affected at least one tness measure and different tness measures were predicted by heterozygosity at different loci so we only present data on overall heterozygosity We calculated pairwise relatedness between partners using Relatedness 50 httpI wwwgsoftnetusGSofthtn11 The average relatedness between adult males and females expected 1 0 in our studypopulation was 00007 sem calculated by iaclclcninngi over loci 00009 In a random sample of100 broods the average relatedness among full siblings expected 1 05 was 047 sem 002 The mean inbreeding coef cient of our population Fig calculated from the microsatellite data using Fstat V293 equals 0006 The observed level ofinbreeding was 33 two of 61 local recruits with known parents mated with close relatives 1 05 and 0125 Received 21 March accepted 25 Iuly 2003 doi101038natuie01959 1 lennionsM DampPetne MWhydofemalesmatemultipiyzAreviewofthegeneticbenentsotol Rev 75 21e64 2000 2 Tregenza T at Wedell N Genetic compatibility mate choice and patterns ofparentage invited review Mol Ecol 910134027 2000 3 Zeh l A ampZeh D w Reproductivemode and the geneticbenefits ofpo1yandry Anim Behav 61 10514063 2001 4 0rown l L Atheory ofmate choice based on heterozygosity Behav Ecol s EDeES 1997 5 Zeh l A ampZeh D w The evolution ofpoiyandry I intragenomic confiict and genetic incompatibility Pmc 12 Soc Lond B 263 17114717 1996 6 Tregenza T ampWedell N polyandrous females avoid costs of inbreeding Norm 415 7143 2002 7 Thornhill N w The Natural Hierovy ofInbveedmg and Duthveedmg Theoretical and Empincol Pcvspccrrvos Univ chicago press chicago 1993 8 Kempenaers 0 Adriaensen 0 van Noordwiik A l at Dhondt A A Genetic similarity inbreeding and hatchingfaiiure in blue tits are unhatched eggs infertile Pmc 12 Soc Lond B 263 179485 1996 9 Coltman D w 0owen w D ampanht l M 0irthweight andneonatai survival ofharbour sealpups arepositively correlated with geneticvariation measured bymicrosatellites Pmc 12 Soc Lond B 265 803e809 1998 lDA1nosW eral Theinfiuence ofparental relatedness on reproductive successpvoc 12 Soc Lond B268 20214027 2001 Hansson 0 0ensch s Hasselquist D arAkesson M Microsatellite diverSitypredlcts recruitment of sibling great reedwarbiers Pmc 12 Soc Lond B2681287e1291 2001 12 Hogiund 1 2t ol inbreeding depression and male tness in black grouse Pmc 12 Soc Lond B 269 711415 2002 13 Hansson 0 at Westerberg L On the correlation between heterozygosity and tness in natural populations Mol Ecol 11 24674474 2002 14 pusey A ampWolf M inbreeding avoidance in animals Trend Ecol Evol 11 201406 1996 15 petrie M at Kempenaers 0 Emi39aepaii39 paternity in birds explaining variation between species and populations Trends Ecol Evol 13 5258 1998 16 Blomqvist D eral Genetic similarity between mates and exii39aepaii39parentage in three species of shorebirds Norm 419 613e615 2002 17 Kempenaers 0 crol Einiaepaiipateinityiesults 39omfemalepieferenceforbighequalitymales inthe blue tit Norm 351494496 1992 18 Kempenaers 0 Verheyen G R at Dhondt A A Extrapaii paternity in the blue tit Farm cocvnlcm female choice male characteristics and offspring performance Behav Ecol s 481492 1997 19 Aparicio l M eordero p l at Veiga l p A test of the hypothesis ofmate choice based on heterozygomy in the spotless starling Anim Behav 6210014006 2001 20 Andersson s Ornborg l arAndersson M Ultraviolet sexual dimorphism and assortativemating in blue tits Pmc 12 Soc Lond B 265 445450 1998 Hunt 5 Cutl39iill i c 0ennett A T D at Grif ths R preferences for ultravioletpartners in the blue tit Anim Behav 5s 809e815 1999 sheldon 0 Andersson s Grif th s c Ornborg l at Senderka l Ultraviolet colour variation in uences blue tit sex ratios Norm 402 87Ae877 1999 Mitton l 0 schuster w s 0 eothran E G at De Eries l c Correlation between the individual heterozygomy ofparents and their offspring Home 71 59e63 1993 24 Stocldey p Seaile l 0 MacDonald D w at Jones c 5 Female multiple mating behaviour in the common shrew as a strategy to reduce inbreeding Pmc 12 Soc Lond B 2541734791993 Dawson D A Hanotte 0 Greig c Stewart 1 R K at Burke T polymorphic microsatellites inthe bluetit Farm cocvnlcm and their crossespeues utility in 20 songbirdfamrhes Mol Ecol 9 19414944 2000 0ensch 5 price T at iltohn l isolation and characterization ofmicrosatellite loci in a Phylloscopm warbler Mol Ecol 6 91e92 1997 Fridolfsson A 1c Gyilensten U 0 ampIalltobsson sMicrosatel1ite markers for paternity testing inthe willow warbler Phylloscopm ooclnlm high frequency of mraepair young in an island population Hcvcdtros 1261274321997 28 Iamieson A The effectiveness of using coedominant polymorphic allelic series for 1 checking 2 2 2 2 2 2 NATURE lVDL 425 l 15 OCTOBER 2003 lwwwnatuiecomnatuie 2003 Nature Publishing Group letters to nature pedigrees and 2 distinguishingfuliesib pairmembersAmm Genet 25 3744 1994 29 pemberton 1 M Coltman D w Coulson T N at slate 1 in Microsatellites Evolunon and Appltconoos eds Goldstein D 0 at schlotterer c 151464 oioford Univ press Oxford 1999 3a Turelli M at Ginzburg L R should individual tness increase with heterozygosity Generic 104 191e209 1983 Acknowledgements We thank D Blomqust S Grif th D Hasselquist L Keller M Milinski A Peters B Sheldon C Wedekind and D Zeh for comments on the manuscript K Cartel D Kaulfuss H Kunc K Peer A Posel and A Turk for help with eld and laboratory work 5 Andersson for computing the colour variables and H Winklei Konrad Lorenz institute for Comparative Ethology and RT Klumpp and A Folt Institute of Silvicultuie University of Agricultural Sciences Vienna for logistic support Competing interests statement The authors declare that they have no competing nancial interests Correspondence and requests for materials should be addressed to BK bkempenaeiseiloinitholmpgde RNA molecules stimulate prion protein conversion Nathan R Deleault Rall W Lucassen 8i Surachai Supattapone Department of Biochemistry 7200 Vail Building Dartmouth Medical School Hanover New Hampshire 03755 USA Much evidence supports the hypothesis that the infectious agents of prion diseases are devoid of nucleic acid and instead are composed of a speci c infectious protein i This protein PrPsc seems to be generated by template induced conformational change of a normally expressed glycoprotein PrPC refi 2 Although numerous studies have established the conversion of PrPC to PrPSC as the central pathogenic event of prion disease letters to nature RNase V which degrades only double stranded dsRNA rnol eculess or RNase H which speci cally cleaves RNADNA hybrids Fig lb rst and second panels Taken together these results suggest that single stranded ssRNA is required for PrPres ampli cati n in vino but that dsRNA and RNADNA hybrids are not Addition ofDNase or the restriction enzyme EcoRI did not decrease PrPres ampli cation showing that DNA is not required for the process Fig lb third and fourth panels Addition ofthe enzymes apyrase and heparinase 111 also had no effect on PrPres ampli ca tion suggesting that neither high energy nucleotides nor molecules containing heparan sulphate are required for PrPres ampli cation in vino Fig lb fth and sixth panels In control experiments we con rmed the degradation ofthe target molecules in each ofthese reaction mixtures by using appropriate analytical assays for these structures Supplementary Fig 52 To ensure that the commercial nuclease preparations we used were not contaminated with proteases we measured the levels of 1gtr1gtC and PrPres after overnight incubation with various nucleases These measurements con rmed that levels of 1gtr1gtC Fig 2a and input PrPres Fig 2b were both unperturbed by addition of enzymes that inhibited PrPres ampli cation As a control to con rm that abolition of PrPres ampli cation depends on the stimulatory activity of each inhibitory nuclease we 39 Enzyme M 30 M SC L mmm My RNIIe 91K DNualme 25K 31K MA 25K 51K Human 25K Miamama 39 57quot mm 25K 37K Bonmnm 25K I Enlyma M Sc M SC X mmm Mr 4 S7K mm 25K NmH 7 Iii s1K 9N9 25K s1K EwRI e39 25K a7K Amman 25K s1K Ha Iquot palms o st Figure I Enect oryanous enzymes on PrPres amplification lmmunoplots or PrPres amplification reactions Samples incluue mixtures or normal anu oiluteu scrapie prain nomopenate M oiluteu scrapie prain nomopenae control Sc anu mixtures or normal anu oiluteu scrapie prain nomopenae incupateuvyitn yarious enzymes in a oilution series The values or x manuracturers Llul ror enzymes are DNase rree RNase n5 RNaseA 0005 RNaseTl an micrococcal nuclease 0005 penzonase RNase Vl e um RNase H l RNase free DNase e l Econ nepannase lll 0025 5 e l apyrase 7 ul 118 o 2003 NaturePublishing Group added benzonase micrococcal nuclease and RNase A to PrPres ampli cation reactions in enzymatically inactive states Bothbenzo nase and micrococcal nuclease require divalent cations for enzy matic activity so we inactivatedthese nucleases by addition ofS mM EDTA The active site ofRNase A contains a critical histidine residue that can be covalently modi ed by diethyl pyrocarbonate DEPC Therefore we pre treated RNase Awith DEPC to inhibit its RNase activity and removed excess DEPC by dialysis Our results show that none of the three nucleases inhibits PrPres ampli cation in their inactive states supporting the hypothesis that intact RNA molecules stimulate this process Fig 2c To test whether inhibition of PrPres ampli cation might be mediated by end products ofRNase digestion we measured directly the effect ofcyclic 2 3 guanidine monophosphate GMP and 3 cytidine monophosphate CMP on PrPres ampli cation Neither of these nucleotides inhibited PrPres ampli cation in vino at concentrations up to lmM Fig 2d Our control experiments rule out the possibility that contaminating proteases steric hin drance or digestion end products account for the inhibition of I EmaUpllmul D 25 5 Tahlproi 39lmg 501mm 501mm 501mm 501mm A4 WWI PIP u 39 Mr a7K animus 25K s1K W ee 25K a1K Rugu lt 425K ll Nuclmiaam MScMSclm i m 37K menu39saw e v25K 87K s GMP oquot 25K Figure 2 Nucleases oo not cause proteolytic steric or enu prouuct innipition or PrPres amplincation a Enect or DNase rree RNase on PIPE leyels Sunuaru amplincation mixtureswere incupateuoyernipntvyitn RNase Serial oilutionsor eacn sample are snown n Effectof nucleaseson PrPres leyels Samplesor oiluteu scrapie prain nomopenate were treateuvyitn specineu nucleases at concentrations oesipnateu x in Flg l o Effect or inactiyateu nucleases on PrPres amplincation Samples incluue mixtures or normal anu oiluteu scrapie bralll nomopenae M and oiluteu scrapie prain liomopenate control 64 a Effect or nucleotiues on PrPres amplincation NATURE l V0 Azsl is OCTOBER 2005 l wwwnaturz amnaturz FrFres ampli cation by speci c nudeases Taken together these experiments indicate that RNA is required for FrFres ampli cation in who We next sought to determine whether a preparation of isolated RNA molecules could reconstitute the ability of nuclease treated normal brain homogenate to amplify PrPres Remarkably total RNA isolated from hamster brain successfully reconstituted the ability of benzonase pre treated brain homogenate to amplify PrPres in a dose dependent manner Fig 3a By contrastpuri ed heparan sulphate proteoglycan HSPG failed to reconstitute PrPres ampli cation Fig 3a Otherpolyanions such as ssDNA Fig 3b polyadenylic acid heparan sulphate pentosan sulphate and poly glutamic acid data not shown also failed to stimulate PrPres ampli cation In this and other reconstitution experiments benzo nase treated control lanes have a greater level of PrPres ampli ca tion than the diluted scrapie brain homogenate control samples indicating that the benzonase pre treatment reactions were incom plete Empirically we found that it was necessary to perform benzonase pre treatment reactions at 4 C to avoid denaturing FrFC before the addition ofpolyanions To estimate the molecular size of the RNA species capable of reconstituting PrPres ampli cation we fractionated our prep aration of total hamster brain RNA by ultra ltration through a lter with a relative molecular mass cutoff of approximately 100000 M 100K Using agarose gel electrophoresis we detected all ofthe ribosomal RNA bands in the retentate and all of the transfer RNA in the ltrate data not shown Using these samples we discovered that the lter retentate was capable of reconstituting PrPres ampli cation to a level slightly lower than unfractionated total brain RNA By contrast the ltrate was not able to reconstitute PrPres ampli cation Fig 3c These data indicate that most of the reconstitution activity is conferred by RNA molecules gt100K in size gt300 nucleotides There is currently a need to develop more sensitive diagnostic tests for prion disease this might be achieved by increasing the ef ciency ofFrFres ampli cation techniques We therefore investi gated whether addition of total hamster brain RNA could increase the ef ciency of FrFres ampli cation in vino in brain samples not Elnqus RNA HSFG man M Sc M 5 0122550 0 122550 lapelmaul 37K ocC 25KW3 b surname M Sc M Sc cm HNA DNA Mv 37K 25K G muG M 59 M 539 CM T F R R 37K 39 quot 25K Figure 3 Reconstitution of FrFres ampllncatlon mtn RNA lmmlllloblots 0f FrFres ampllncatlon reactlons Samples lncluge mlxtures of normal and glluteg scraple braln nomogenate M and glluteg scraple braln nomogenae control 34 lnglcateg samples were pre treateg mtn benzonase before reconstltutlon assaysas gescnbeg ln Netnogs a Reconstltutlon wtn total namster braln RNA or HSPG b Reconstltutlon wtn 05 mg ml total namster braln RNA or 05 mg ml ranoom syntnetlc 23 base DNA ollgonucleotldec Reconstltutlon mtn 05mg ml mtal T nltrate F retentate Rang 50ln tonnamlge retentate R samples from RNA tractlonateg by ultraflltratloll NATURE l V0 425 l 16 OCTOEER 2003 l w natuxt remnature 2003 NatureFuhlishirrg Group letters to nature pre treated with nuclease We mixed a more dilute homogenate of prion infected brain 002 wv with 5 wv normal brain homogenate overnight without sonication and measured PrPres ampli cation Our results show that addition of totalhamster brain RNA to this mixture of intact brain homogenates signi cantly stimulates PrPres ampli cation over baseline Fig 4a As a control we con rmed that addition ofRNA did not alter the level ofinput FrFres or FrFC in these samples Supplementary Fig 53 Densito metric measurements indicate that FrFres in 002 wV prion infected brain homogenate samples is ampli ed about sixfold after overnight incubation similar to the PrPres ampli cation level previously reported for 01 wV prion infected brain homogen ate3 By contrast FrFres in samples ampli ed with RNA is ampli ed about 24 fold indicating that addition of RNA increases the ef ciency ofin vim FrFres ampli cation about fourfold Addition of RNA also increased the ef ciency of FrFres ampli cation of sonicated protein misfolding cyclic ampli cation PMCA reac tions Supplementary Fig 54 To assess the speci city ofRNA mediated stimulation of FrFres ampli cation we isolated total RNA from several sources including Escherichia coli Succhmomyces cerevisiue Cuenorhubditis eleguns Dmsophilu melexogmm and mouse and hamster brain Agarose gel electrophoresis analysis ofthese preparations revealed the expected band patterns for each species and con rmed that each preparation I so Sc M M M RNA w 737K quot quot 725K 47 4719 e RNA Sam M M f gm 787K Experimn v 7st 737K Expninnmz 725K Figure AStlmulatlon 0f PlPrFs ampllncatlon wtn RNA a lmmunoblotof FrFres ampllncatlon reactlons Samples lncluge mlxturesot 5 wv normal and 002sn wv scraple braln nomogenate M and glluteg scraple braln nomogenate control 34 lnglcateg samples contalneg 05 mg ml total namster braln RNA b Agarose gel electropnoresls of total RNA prepared from Varlolls specles o lmmlllloblot 0f specles speclnc stlmlllatlorl 0f FrFres ampllncatlon wtn RNA Total RNA 05 mg ml prepared from Varlolls specles was added to FrFres ampllncatlon reactlons 119 letters to nature contained high quality non degraded RNA Fig 4b Furthermore each of these preparations was substantially free from contaminants as judged by optical spectroscopy AzgoAzgo gt 19 where A indicates absorbance and subscript numbers indicate wavelength Notably among the six preparations of RNA tested only hamster and mouse brain RNA could stimulate PrPres ampli cation in vitrc Fig 4c This apparent species speci city cannot be attributed to tissue speci city because total hamster liver RNA also stimulated PrPres ampli cation data not shown This argues that mice and hamsters express speci c RNA molecules required for PrPres ampli cation Additional experiments show that the RNA stimu lation activity within the Trizol extracted hamster brain RNA preparation was irreversibly destroyed by glyoxylation but not by deproteination heating to 60 C or transient exposure to 50 formamide for 1h Supplementary Fig SS If PrPres ampli cation studies accurately model PrPS C formation in viva the results presented here represent a signi cant advance in our understanding of the mechanism of prion conversion Pre viously it has been shown that puri ed PrPC can be converted into protease resistant PrPres in vitrc in the absence of cellular cofactors7 However the fact that a 50 fold molar excess of puri ed PrPres is required to drive conversion of puri ed PrPC suggests that ef cient PrPres formation may depend on the presence of cellular factors other than PrPC ref 8 On the basis ofthe results presented here we propose the hypothesis that speci c RNA molecules are cellular cofactors for PrPS C formation Consistent with our hypothesis that speci c RNA converting factors stimulate PrPS C formation nucleic acids bind avidly to and promote conformation al change of recombinant PrP refs 9 14 However it is important to note that full length refolded recombinant PrP lacking post translational modi cations cannot undergo stoichiometric conver sion to PrPres Supplementary Fig 56 and therefore the results of biophysical studies using recombinant PrP cannot be directly related to the results described here It has been proposed that PrPS C molecules might bind to speci c host RNA molecules to generate strain diversity Whether the RNA converting factors we describe are also involved in generating strain diversity remains to be determined Finally it is important to emphasize that the existence of RNA converting factors is fully consistent with the protein only hypothesis proposed previously because the nucleic acids we describe are host encoded and not contained within the infectious agent D Methods Animal and reagent sources Speci ccpathogencfree female golden Syrian hamsters at 3 weeks old were purchased from Charles River Laboratories Apyrase DEPC cyclic 239339cGMP S39cCMP heparinase III heparan sulphate proteoglycan M gt200Kpo1yadeny1ic acid M 2007200010 and polyglutamic acid M 5m100K were obtained from Sigma RNasecfree DNase micrococcal nuclease RNase A and DNasecfree RNase were obtained from Roche RNase T1 was obtained from Epicentre recombinant benzonase nuclease was purchased from Novagen EcoRI was obtained from Gibco BRL and RNase H and RNase V were obtained from Ambion In vitro PrPres amplification Irt vim PrPres ampli catioif and PMCA were performed as previously described except that normal brain homogenates were prepared with EDTAcfree complete protease inhibitors Roche to facilitate experiments involving metalcdependent enzymes Two millimolar MgCl was added to reactions with benzonase and 2 mM CaCl was added to reactions with micrococcal nuclease and apyrase All ampli cation and control reactions were performed at 37 C for 1611 For PrPres detection protease digestion was performed with 50 pg ml proteinase K for 1h at 37 C and immunoblotting was performed with 314 monoclonal antibody Signet For PrPC detection samples were not subjected to proteinase K digestion before immunoblotting All protein electrophoresis experiments shown were performed on 12 SDS polyacrylamide gels and reference M for such experiments are shown Nuclease inactivation Micrococcal nuclease and benronase were inhibited with 5 mM EDTA RNase A 50 ug was incubated with 1 DEPC in 100 til at 25 c for 2 h After incubation the reaction was dialysed twice against ll 10 mM Tris pH 72 at 4 c using a Pierce 3500 MW SlidecAcLyzer 720 2003 Nature Publishing Group minidialyis unit to remove free DEPC Control samples containing active RNase Awere dialysed in parallel Protein recovery gt90 was con rmed by BCA assay Pierce Active and inactivated nucleases were added to ampli cation reactions at concentrations designated 26 in Fig 1 No enzyme control samples were processed in parallel Reconstitution assays Nuclease digestion before reconstitution was performed by incubating a batch of normal brain homogenate 10 wv with benzonase nal concentration of25 Upl and 2 mM Mgcl2 for 15h at 4 C in the absence ofdetergents Benzonase was then inactivated by the addition of 5 mM EDTA before reconstitution with RNA or other polyanions Preparation and measurement of RNA RNA was isolated from animals lt5 min after death using rotorcstator homogenization extraction with Trizol reagent Invitrogen for 5 min at 25 C and isopropanol precipitation according to manufacturers instructions using RNasecfree reagents containers and equipment For yeast cell walls were disrupted during extraction as previously described using Trizol in place ofphenol All RNA solutions were alcohol precipitated washed and resuspended in RNasecfree water before use The concentration and purity of each solution was determined by spectroscopic measurement of absorbance at MA 260280 nm and con rmed by electrophoresis on 1 agarose gels stained with ethidium bromide RNA size fractionation Total hamster brain RNA 04 mg was diluted into 08 ml RNasecfree water loaded in 021111 batches onto four separate Schleicher and Schuell Centrex UFc05 100K cutoff ultra ltration devices and centrifuged for 15 min at 3000g The devices were then washed with an equal volume of water The ltrates were pooled and retentate fractions collected by brie y centrifuging the ultra ltration devices upside down into new microcmtrifuge tub es Parallel samples of denatured retentate were prepared in 50 formamide to disrupt all intra and intermolecular interactions Reverse transcriptase polymerase chain reaction RTePCR was performed using the One Step RNA PCR kit AMV from TakaralFisher following the manufacturers instructions using the PrPcspeci c primers S39cCGAACC TTGGCTACTGGCTGCTGcS and 5 cGCTTGATGGTGATATTGACGCAGTGS and the following parameters reverse transcription at 50 C for 15 min heat inactivation of reversetranscriptase at 94 C for 2 min gtlt25 PCR cycles 94 C for 30 s 55 c for 30 s 72 c for 90 5 Products were run on a 1 agarose gel and stained with ethidium bromide Received 4 Iuly accepted 31 Iuly 2003 doi101038nature01979 1 Prusmer s 9 Novel proteinaceous infectious particles cause scrapie Setoaco 216 1357144 1982 2 Prusmel s 13 ed Paaa Biology and Disoaxos Cold spring Harbor Laboratory Press Cold spring Harbor NewYork 1999 3 Lucassen R Nishina K at supattapone s la Vina amplification ofpmteasecreSlstant prion protein requires free sulfhydryl groups Biacliomtsrry 42 412774135 2003 4 Sabono G R Permanne e at Soto C sensitive detection ofpathological prion protein by cyclic amplification ofprotein misfolding Norms 411 8107813 2001 s Lockard R E at Kumar A Mapping tRNA structure in solution using doublecstrandcspecl c ribonucleasev1 from cobra venom NacloicAcirls Ros 9 512575140 1981 5 Banks G R A ribonuclease H from Usnlaga mayae Properties mode of action and substrate specificity ofthe enzyme Em I Biacliom 47499507 1974 7 Kocisko D A oral Cellfreefonnation ofpmteasecteSlstalAtpnonpmteln Name 370471474 1994 s CaugheyBHonuhlMDelnau11aa R at Raymond G 1 Assays ofpmteasecteSlstantprionpmtem and its formation Morliaas Eazymal 309122133
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