新人必学：让卫新洗衣液成交量提高50%的销售步骤

「キッチン」についての感想文「キッチン」という本は今日本でかなり人気がある吉本バナナの処女作である。

彼女は１９８７年に書いた「キッチン」で第６回の「海燕」新人文学賞、１９８８年単行本「キッチン」で泉鏡花文学賞を受賞した。

「キッチン」は桜井美影の女の子の成長についての小説である。

吉本バナナの多くの小説の中で一番気に入るのは「キッチン」だ。

「キッチン」より親切、静かな気持ちをしみじみと感じることができて、そわそわとする現実から脱して命の珍しさをわかることができる。

これはたぶんこの短い小説がなぜ大勢のひとに好かれた理由かもしれないと思う。

「キッチン」は一人の女の子の成長することを描くことを通じて、作者は生命ということがこころを癒す過程であると言う見方を読者に伝えている。

主人公の桜井美影の運命は大変かわいそうだ。

文章の中でこのような述べるところがある：「私、桜井美影の両親は、そろって若死にしている。

そこで祖父母が私を育ててくれた。

中学校へ上がる頃、祖父が死んだ。

そして祖母と二人でずっとやってきたのだ。

先日、なんと祖母が死んでしまった。

びっくりした。

家族と言う、確かにあったものが年月の中でひとりひとり減っていって、自分がひとりここにいるのだと、ふと思い出すと目の前にあるものがすべて、うそに見えてくる。

生まれ育った部屋で、こんなに時間が過ぎて、私だけがいるなんて、驚きだ。

」親しい人がなくなったから桜井美影の心は寂しさと絶望にあふれていて、生活に対して彼女は自信がちっともなくなって、暗い闇に陥て未来にも迷っている。

その時、いつも祖母に世話になった田辺雄―と彼の変性した母に拾われて、この病的みたい少し変な家庭の中で、かえって彼女はだんだん家族みたい暖かいを感じられて、生きている光が見える。

田辺家の明るい台所からー歩―歩死亡の影に踏み出して、勇ましくなってしっかり人生を見直して社会人になっている。

文章のおわりのどおり書いた︰「もっともっと大きくなり、いろんなことがあって、何度も底まで沈み込む。

1あなたはすでに私一生、それがあなたの歓楽があります。

このもろい薄い杯児、あなたが后を绝たないはそれを放り出そ空があって、また、新規に命を绝がいっぱいだ。

この小さな苇笛、あなたを携えてそれを超えて、笛管山越谷で吹いた金ヒョンジュン・ヨンシンの音楽だ。

あなたの心の中では両手の不朽の通りを抚でのもとで、私の小さな心で、夜明け无辺至福の女の子の词调、音が避けられない。

あなたの漢方薬を赐だけに小さな手にかかっている。

時代がたって、君はまだ倾であるため、私の手にも残量のまちがいっぱいだ。

2私はあなたが命令したとき、私は歌の心で眼れようとしている、私は誇りウソップ見上げて君の顔に、涙が押し寄せて私の出そうになりますに浸っている。

私の生命の中ですべての凝渋さと葛藤が溶けた漆黒のような甘い柔の語呂合わせ——。

私の賛美歌1匹の喜びの小鸟、振翼を跳び越えて海が広がっている。

私はあなたを知って歓喜私の歌だ。

私は知っていたという理由だけで中国があってこそ、私はあなたの前にまで歩く。

私は私の歌の遠に伸ばして翼の梢に触れた君の足であっても、それは私(わたし)に触れそうに二の足を踏んでいた。

群がる歌唱中に酔い、忘れてた自分に、あなたの本は私の主、私はあなたは友达です。

3私はあなたを知って、私はどのように歌った主人をします!私はいつも不思議原文だった。

あなたの音楽の輝きが明るくなった世界。

あなたの音楽の息吹を徹底诸天だった。

あなたの音楽の聖泉駆け抜けてすべてさえぎるの岩、前を向いていった。

あなたが私の心を念願と合唱、もがいていることが出来ない声だった。

私が話すために言叶によってちゃいけない曲で、私の名前は出てこなかった。

ああ、あなたは私の心に変わっていたあなたの音楽ポータルサイトの捕虜をの垂れ幕がぼくの主です!4私の生命の生命を維持しなければ、私は永远に私の狂態を分かっていますから、あなたの命の摩抚接して私の脚。

私は永远は私の思想のうち屏除伪り、分かっていますからあなたがあの私の心の中で燃え上がる理性をもたせて真理のようだ。

Leading EdgeReviewMembrane BuddingJames H.Hurley,1,*Evzen Boura,1Lars-Anders Carlson,1and Bartosz Ro´_zycki21Laboratory of Molecular Biology2Laboratory of Chemical PhysicsNational Institute of Diabetes and Digestive and Kidney Diseases,National Institutes of Health,Bethesda,MD20892-0580,USA*Correspondence:hurley@DOI10.1016/j.cell.2010.11.030Membrane budding is a key step in vesicular transport,multivesicular body biogenesis,and envel-oped virus release.These events range from those that are primarily protein driven,such as the formation of coated vesicles,to those that are primarily lipid driven,such as microdomain-dependent biogenesis of multivesicular bodies.Other types of budding reside in the middle of this spectrum,including caveolae biogenesis,HIV-1budding,and ESCRT-catalyzed multivesicular body formation.Some of these latter events involve budding away from cytosol,and this unusual topology involves unique mechanisms.This Review discusses progress toward understanding the structural and energetic bases of these different membrane-budding paradigms.Eukaryotic cells are defined by their compartmentalization into membrane-delimited structures.The protein and lipid content of these membranes is maintained and regulated by a constant flux of vesicular trafficking.Each vesicular trafficking event involves the budding of a membrane vesicle from a donor membrane,typically followed by its regulated transport to,dock-ing to,and fusion with an acceptor membrane.Many viruses also have membrane envelopes and escape from host cells by membrane-budding events.Our laboratory has been characterizing the unusual membrane-budding reaction promoted by the ESCRTs,which has led us to take a fresh look at how membrane lipid properties might make protein-dependent,energetically expensive reac-tions easier.Several excellent reviews have covered the way proteins induce curvature in biological membranes(Farsad and De Camilli,2003;McMahon and Gallop,2005;Voeltz and Prinz, 2007)and the physical principles of membrane curvature (Zimmerberg and Kozlov,2006).This Review will take a different viewpoint and consider the comparative roles of proteins and lipids in select examples of vesicular budding events(Figure1) to discuss similarities and differences in budding events in synthetic versus cellular contexts,the potential roles of proteins in orchestrating lipid phase changes,and the roles of lipids in recruiting and regulating proteins.We also examine the implica-tions of the above for cell physiology.This article is not intended as a comprehensive review of all cellular budding events.Rather, we consider emerging mechanistic thinking in multivesicular body formation and virus budding,placing these in the context of the classical mechanisms underlying budding of coated vesicles.Energetics of Vesicle BuddingThe formation of spherical vesicles from aflat membrane of typical biological composition and no intrinsic propensity to curve entails a membrane-bending free energy(Helfrich,1973), D G=8pk 250–600k B T,given k 10–25k B T,where k B T is thermal energy(Bloom et al.,1991).This is important for biology because events that require thermal energy of this magnitude (that is,of 100k B T or greater)do not occur spontaneously. Biophysical studies of membrane budding,which offer the promise of accounting for energetics,are typically carried out in vesicles that are much larger than their counterparts in biolog-ical systems.Fortunately,the energetic cost of bud formation is to afirst approximation independent of the size of the bud. In pure lipid mixtures used in biophysical studies,vesicles are microns in size,spreading the energetic cost over 106or more lipid molecules.In cells,however,membrane buds have a diameter of 20–100nm,thus involving as few as103–104lipid molecules.This poses the question,how do a modest number of protein-lipid interactions create the free energy that is needed for budding,or alternatively,how do lipids themselves contribute to lowering the energy barrier?Coated Vesicle BuddingClathrinThe dominant mechanism of membrane budding into the cytosol and the paradigm for protein-directed budding is the formation of coated vesicles(Figures1F and1G and Figure2).Clathrin-coated vesicles(CCVs)are typically60–100nm in diameter (Bonifacino and Lippincott-Schwartz,2003;Brodsky et al., 2001).Clathrin can form baskets in vitro that resemble the CCVs in the absence of membranes,and the basket structure has been characterized in molecular detail(Fotin et al.,2004). Clathrin itself binds neither membranes nor cargo but relies on adaptors for this function.Among the most comprehensively studied is adaptor protein complex2(AP-2complex)(Robinson and Bonifacino,2001),which functions in clathrin-mediated endocytosis at the plasma membrane.The AP-2adaptor complex opens up in the presence of cargo and the lipid phos-phatidylinositol(4,5)-bisphosphate(PI(4,5)P2)to form aflat plat-form capable of binding multiple PI(4,5)P2and cargo molecules (Jackson et al.,2010).The established role for PI(4,5)P2in this Cell143,December10,2010ª2010Elsevier Inc.875pathway is to recruit AP-2and other proteins to the site of budding.A role for PI(4,5)P 2clustering into microdomains has been suggested on theoretical grounds (Liu et al.,2006)but has yet to be directly visualized.Clathrin is absolutely required for the budding of AP-2-and cargo-rich plasma membrane domains,which remain flat in its absence (Hinrichsen et al.,2006).However,clathrin monomers are flexible,which gives clathrin the ability to form different types of lattices and to adapt to various cargoes (Ehrlich et al.,2004).Given the flexibility of clathrin monomers,the energy of clathrin polymerization has been proposed on theoretical grounds to be insufficient on its own to bend the membrane into a bud (Nos-sal,2001).However,this concept has yet to be confirmed exper-imentally and is not universally accepted.Cholesterol is important for clathrin-mediated endocytosis by many (though not all)accounts (Rodal et al.,1999;Subtil et al.,1999),although it is less sensitive to cholesterol depletion than most coat-independent budding pathways (Sandvig et al.,2008).Clathrin,cargo adaptors,and PI(4,5)P 2are necessary but not sufficient on their own to induce membrane curvature.The essential early endocytic factor epsin wedges its amphi-pathic helix a 0into the membrane upon PI(4,5)P 2binding,promoting positive curvature (Ford et al.,2002).The cargo-binding muniscin proteins FCHo1/2(Syp1in yeast)contain BAR domains that promote positive curvature very early in endo-cytosis (Henne et al.,2010;Reider et al.,2009;Stimpson et al.,2009;Traub and Wendland,2010).In principle,the reagents and concepts would appear to be in place to reconstitute clathrin-dependent membrane budding.Reconstitution of clathrin-mediated endocytosis using synthetic lipids and purified proteins would be an important step in determining whether clathrin,AP-2,one or more amphipathic helix and/or BARdomain proteins,and PI(4,5)P 2constitute the minimum require-ments for membrane bud formation in this pathway.The scission of the clathrin-coated bud to form a detached vesicle is a complex process in its own right,and the reader is referred to recent reviews (Pucadyil and Schmid,2009).Finally,following scission,the clathrin coat is removed by the ATP-dependent action of the molecular chaperone Hsc70and its cofactor auxillin (Eisenberg and Greene,2007).It is only following nucleotide hydrolysis that the energetic cost of clathrin-induced membrane deformation is finally paid,making the full reaction cycle—from flat membrane to uncoated vesicle—thermody-namically irreversible.COP I and COP IIVesicles carrying cargo from the endoplasmic reticulum (ER)to the Golgi are coated by the COP II complex,which,like clathrin,can form membrane-free baskets in vitro with vesicle-like dimen-sions (Stagg et al.,2006).COP II vesicles have a preferred size,but as with clathrin,the flexibility of the COP II subunits allows formation of expanded lattices that can accommodate large cargoes such as procollagen and large lipoprotein particles known as chylomicrons (Stagg et al.,2008).COP II vesicle budding has been reconstituted in vitro from purified proteins and synthetic lipids (Lee et al.,2005;Matsuoka et al.,1998).A membrane consisting only of synthetic unsatu-rated phospholipids was capable of supporting budding (Matsuoka et al.,1998).COP II consists of the Sec23/24sub-complex,which binds lipids and cargo via a gently curved face (Bi et al.,2002),the Sec13/31subcomplex,which forms an outer cage around the vesicle,and the membrane-bending GTPase Sar1.The Sec23/24and Sec13/31subcomplexes in combina-tion are sufficient to form buds,with Sar1strictly required only for the scission of the buds.GTP hydrolysis by Sar1providesFigure 1.Proteins and Lipid Microdomains in Membrane Budding(A)Budding of phase-separated lipid microdomains from GUVs (giant unilamellar vesicles)composed of synthetic lipids is an example of membrane budding in the absence of any proteins.Reproduced by permission from Baumgart et al.(2003).(B)Shiga toxin (black dots)acts from outside the plasma membrane to induce membrane buds and is an example of a protein triggering budding events that areprimarily driven by lipid microdomains.Image reproduced by permission from Macmillan Publishers Ltd:Nature,Ro¨mer et al.(2007),copyright 2007.(C)Budding by caveolae represents a hybrid between a membrane microdomain and protein coat-driven mechanisms.Reproduced by permission from Mac-millan Publishers Ltd:Nat.Rev.Mol.Cell.Biol.,Parton and Simons (2007),copyright 2007.(D)ESCRT-I and -II induce buds in synthetic GUVs.Reproduced by permission from Wollert and Hurley (2010).Proteins organize these structures but do not form a coat,suggesting a possible role for microdomains.(E)HIV-1buds visualized by electron tomography (Carlson et al.,2008).The bud is organized by the HIV-1capsid protein,heavily enriched in raft lipids,and cleaved by ESCRT proteins.(F)Deep etch visualization of clathrin-coated pits (image courtesy of J.Heuser).Clathrin assembles into baskets in the absence of membranes but is thought to be too flexible to deform membranes on its own.For this,clathrin needs help from other membrane-deforming proteins and possibly from lipids.(G)The COP II cage is an example of a protein structure that can form in the absence of lipids and can impose its shape on any simple bilayer-forming lipid mixture.Reproduced by permission from Russell and Stagg (2010).876Cell 143,December 10,2010ª2010Elsevier Inc.energy input into the system,making the overall process (which culminates in the uncoating of cargo-loaded vesicles)thermody-namically irreversible.COP I-coated vesicles are responsible for retrograde traffic from the Golgi to the ER,and this reaction has also been recon-stituted from purified proteins and synthetic lipids.The budding reaction requires the coatomer complex,GTP-bound Arf1,and protein cargo tails tethered to the membrane but has no special lipid requirements (Bremser et al.,1999).Budding occurs even from vesicles composed of the pure synthetic phospholipid DOPC doped with small amounts of a lipopeptide cargo.Recently,a composite crystallographic structure of cage-form-ing components of coatomer consisting of the a ,b 0,and 3subunits has been determined and shown to resemble the cla-thrin triskelion (Lee and Goldberg,2010).In sum,COP I and COP II provide some of the purest examples of protein-directed membrane budding,in which the protein coat imposes its shape upon the membrane with minimal dependence on its lipid composition.Membrane Microdomains and BuddingLipid Phase Separation as a Budding MechanismIn contrast to the protein-dominated paradigm of coated vesicle budding,phase separation in simple lipid mixtures can drive budding on a micron scale in synthetic model membranes,in the absence of proteins (Baumgart et al.,2003)(Figure 1A and Figure 3).Membrane bilayers can adopt either a solid or a liquidphase,with the translational and conformational order of the lipid chains depending on their composition and the temperature.The liquid phase is the more relevant to biology and can be subdi-vided into liquid disordered (L d )and liquid ordered (L o )phases.Lipids in the L d phase have higher conformational freedom and diffusion coefficients than in the L o phase.At biological temper-atures,the L d and L o phases can coexist in membranes of mixedcomposition (Elson et al.,2010;Garcı´a-Sa ´ez and Schwille,2010).In general,phospholipids with unsaturated chains prefer the L d phase,whereas cholesterol,sphingolipids,and phospholipids with saturated chains prefer the L o phase (Lingwood and Simons,2010).Typically,the energetic cost for contact betweendissimilar lipids is small, 0.5k B T (Garcı´a-Sa ´ez and Schwille,2010),but becomes significant when summed over many lipids.The higher acyl chain order in the L o phase results intheirFigure 3.Membrane Microdomains and Budding(A)Coexistence of phases in model membranes visualized by atomic force microscopy in a supported bilayer (a membrane bilayer adsorbed onto a solid support,usually glass).Reproduced with permission from Chiantia et al.(2006).(B)Phase transitions in a single-lipid membrane analyzed by molecular dynamics simulations.Reproduced with permission from Heller et al.(1993).Copyright 1993American Chemical Society.(C)Schematic model of a raft-type membrane microdomain,including a model of a myristoylated ESCRT-III subunit Vps20as an example of protein that might anchor torafts.Figure 2.Coated Vesicle Budding(A)Structure of a clathrin basket from cytoelectron microscopy;reproduced by permission from Macmillan Publishers Ltd:Nature,Fotin et al.(2004),copy-right 2004.(B)COP II vesicles produced from purified components;reproduced by permission from Lee et al.(2005).(C)Structural parallels between clathrin,COP I,and COP II.Adapted from Lee and Goldberg (2010).Cell 143,December 10,2010ª2010Elsevier Inc.877elongation to their maximum extent,hence L o membrane domains are thicker than L d domains.The height mismatch at the phase boundary is energetically unfavorable because it forces the polar headgroup region of the L d domain into contact with the hydrophobic portion of the L o domain.The free energy cost per unit length is known as the line tension and has units of force.In order to minimize the free energy associated with line tension,membrane domains will coalesce with one another into circular zones.When circular domains reach a critical size at which the line tension energy term exceeds the Helfrich (curva-ture-dependent)energy of membrane deformation,the membrane will deform out of plane in order to minimize the zone of contact (Lipowsky,1992).If the line tension is high enough,the neck connecting the membrane bud can be severed,leading to the formation of detached vesicles.In addi-tion to line tension effects,membrane microdomain formation can bend membranes by concentrating lipids with distinct intrinsic curvatures,and the contents of such microdomains can not only drive budding but dictate its direction (Bacia et al.,2005).The complex lipid mixture of the plasma membrane supports phase separation in micron-sized domains when reconstituted in giant unilamellar vesicles (Baumgart et al.,2007).However,in living cells,membrane microdomains are heterogeneous,highly dynamic nanoscale structures (Hancock,2006;Lingwood and Simons,2010;Pike,2006).In the most up-to-date biophys-ical view,these nanoscale structures likely correspond to critical fluctuations (Veatch et al.,2007).Although the concepts of the L o and L d phases are oversimplifications of the variety of dynamic membrane substructures that exist in cells (Lingwood and Simons,2010),they will be used in this Review because they are useful intuitive handles,deeply ingrained in the literature,and helpful in relating model membrane studies to biology.Most,but not all,of the membrane microdomains impli-cated in cellular budding are the sterol-and sphingolipid-richdomains known as ‘‘rafts.’’Why don’t rafts and other microdo-mains coalesce on the micron scale in living cells,as they do in model membranes?The answer is not known,but the action of the cytoskeleton and membrane traffic,and the large fraction of protein in cellular membranes,are usually invoked.Indeed,it is to be expected that cells would have mechanisms to block the unchecked growth of microdomains,as the ensuing spontaneous vesiculation of cell membranes would be disas-trous.Soluble and lumenally anchored cargoes,viruses,and toxins are selectively transported in vesicular carriers even though they have no direct communication with the cytosol to signal their packaging and sorting.In some cases,transmembrane-sorting receptors serve as adaptors to link cargo to conventional cytosolic coat complexes.In other cases,membrane rafts make the link.Simian virus 40(SV40)and cholera toxin enter cells by binding to multiple molecules of the ganglioside GM1(Damm et al.,2005;Kirkham et al.,2005),a raft-favoring lipid.The cholera toxin B subunit (Merritt et al.,1994)and the SV40VP1protein (Neu et al.,2008)both bind to GM1as pentamers.Cholera toxin pentamer binds GM1(Figure 4)and thus induces formation of an L o microdomain in model membranes (Hammond et al.,2005)and in turn leads to budding (Bacia et al.,2005;Ewers et al.,2010).Shiga toxin B subunit binds the glycolipid Gb3and appears to operate by a similar paradigm.In this case tubular vesicles are formed,and lipid compression favoring negative curvature is thought to be the driving force (Ro¨mer et al.,2007).In each of these examples,it is clear that clustering of lipids leads to important changes in membrane structure that contribute to budding.The proposed physical mechanisms remain speculative,however.Revealing these mechanisms remains a profound challenge to experimen-talists and thus is an area that will benefit from increasing sophisticated computer simulations of membrane dynamics on realistictimescales.Figure 4.Protein Structures that Cluster Raft Lipids(A)Simian virus 40VP1pentamer bound to the membrane via the headgroup of the ganglioside GM1(Neu et al.,2008).(B)Cholera toxin B subunit pentamer bound to GM1(Merritt et al.,1994).(C)Composite model of the myristoylated HIV-1matrix domain trimer bound to PI(4,5)P 2(Hill et al.,1996;Saad et al.,2006,2008).In each case,lipid tails are modeled.Images were generated with VMD 1.8.6.878Cell 143,December 10,2010ª2010Elsevier Inc.CaveolaeCaveolae(‘‘little caves’’)areflask-shaped60–80nm invagina-tions of the plasma membrane that consist of raft lipids,caveo-lins1–3,and the caveolin-associated cavins1–4(Hansen and Nichols,2010).Caveolins are structurally analogous to the retic-ulons and DP1/Yop1proteins that maintain the curvature of ER membrane tubules(Hu et al.,2008;Shibata et al.,2009)and to another plasma membrane raft protein,flotillin(Bauer and Pelk-mans,2006).Caveolins are pentahelical proteins,with two of the helices inserting deeply into the membrane,almost but not completely spanning the bilayer.The other three helices are amphipathic and are thought to wedge themselves into the inter-facial region of the membrane(Parton et al.,2006).Caveolae contain a consistent number of caveolin molecules, 144,which suggests the formation of a highly organized coat(Pelkmans and Zerial,2005).Posttranslational modification of caveolins is important to their function.Palmitoylation at multiple residues promotes their constitutive association with cholesterol and other raft lipids. Caveolins also undergo phosphoregulation by multiple protein kinases(Pelkmans and Zerial,2005).For instance,when caveo-lin-1is phosphorylated at serine80,which adjoins one of the predicted interfacial a helices,its ability to induce curvature is turned off.Although the energetic book-keeping of caveolin-induced curvature has not been worked out,it is likely to differ greatly from that of conventional coated vesicles.Insertion of caveolin into the membrane presumably shifts the intrinsic curvature of the membrane such that the positively curved bud is the low-energy state and theflat caveolin microdomain is the high-energy state.Thus,once the caveolin microdomain is formed,energy input is probably needed toflatten the membrane rather than to curve it.ATP hydrolysis by protein kinases that phosphorylate caveolin might provide the thermo-dynamic driving force for membraneflattening.Dephosphoryla-tion by protein phosphatases would,in this speculative scheme, allow the membrane to spring back to its low-energy state. Cavins are soluble proteins rich in predicted coiled-coil struc-ture and basic residues but otherwise structurally uncharacter-ized.They seem to be important for caveolar structure,but the precise role of these recently discovered factors in structuring the caveolar coat is not clear.Given that caveolae have a consis-tent amount of caveolin protomers,they could be viewed as highly organized assemblies whose specialized structure and distinct curvature are caveolin driven but lipid stabilized.Alternatively,if viewed from the standpoint of their lipid content,caveolae could be viewed as specialized,morphologically distinct membrane microdomains,whose formation is driven by lipids but stabilized by caveolin(Parton and Simons,2007).The hybrid nature of caveolae,seemingly at once both coated vesicle and membrane microdomain,makes them a particularly fascinating example of the interplay between proteins and lipids in membrane budding. Tetraspanin-Enriched MicrodomainsTetraspanin-enriched microdomains(TEMs),which are abun-dant in exosomes and in the intralumenal vesicles of immune cell multivesicular bodies,are another potential example of a membrane microdomain involved in budding(Pols and Klum-perman,2009).Tetraspanins are a family of at least32proteins in mammals and are defined by the presence of four transmem-brane-spanning a helices(Hemler,2005).Tetraspanins have two extracellular domains;the second,EC2,is the larger of the two. The structure of the EC2region of CD81has been determined, revealing an extensive dimerization interface(Kitadokoro et al., 2001).The minimal functional tetraspanin oligomer is probably a homodimer.These proteins are multiply palmitoylated on their short intracellular loop and N-and C-terminal extensions,and these palmitoylations are central to their ability to form TEMs. Tetraspanins bind to a wide range of potential cargo proteins (Hemler,2005),potentially coupling them to TEMs and thereby to microdomain-mediated budding.More extensive mechanistic analysis of the budding mechanism responsible for TEM traffic will be eagerly awaited.Multivesicular BodiesThe sorting of unneeded,damaged,or dangerous plasma membrane proteins to the lysosome for degradation is carried out by endosomes(Sorkin and von Zastrow,2009).This pathway also is central to the biogenesis of the lysosome(or yeast vacuole),as it carries newly synthesized lysosomal enzymes from the trans-Golgi to their destination.In the metazoa,the endosomal pathways have many additional roles,with the most pertinent to this Review being the biogenesis of lyso-some-related organelles(Raposo and Marks,2007)and exosomes.Multivesicular bodies(MVBs,also known as multive-sicular endosomes)are key intermediates in endolysosomal transport(Figure5;Gruenberg and Stenmark,2004;Piper and Katzmann,2007).MVBs are formed by the invagination and scission of buds from the limiting membrane of the endosome into the lumen.MVB biogenesis is the main physiological example of membrane budding away from the cytosol. ESCRTs and Multivesicular BodiesYeast(Saccharomyces cerevisiae)has a single MVB pathway that drives the internalization of ubiquitinated transmembrane proteins into the lumens of early endosomes(Piper and Katz-mann,2007).The pathway is initiated by the presence of the lipid phosphatidylinositol3-phosphate(PI(3)P)and membrane-teth-ered ubiquitin moieties on the endosome surface.PI(3)P is synthesized by the class III PI3-kinase Vps34,an enzyme essen-tial for the progression of the endolysosomal pathway.PI(3)P is the defining marker of early endosomes,autophagosomes, and,in mammalian cells,phagosomes.PI(3)P signals are recog-nized by FYVE and PX domain-containing proteins(Misra et al., 2001).In the MVB pathway,the key FYVE domain protein is a subunit of the ESCRT-0complex.ESCRT-0containsfive ubiquitin-binding domains(UBDs)(Ren and Hurley,2010)and clusters ubiquitinated cargo in vitro(Wollert and Hurley,2010). Recruitment of ESCRT-0to the early endosomal membrane initiates the recruitment of the ESCRT-I,-II,and–III complexes (Saksena et al.,2007;Williams and Urbe´,2007).Based on in vitro reconstitution,ESCRT-I and-II drive membrane budding, whereas ESCRT-III cleaves the bud necks to form intralumenal vesicles(Hurley and Hanson,2010;Wollert and Hurley,2010; Wollert et al.,2009).In vitro ESCRT budding reactions have been carried out with a mixture of saturated and unsaturated phospholipids and cholesterol(Wollert and Hurley,2010),but the precise lipid requirements for the reaction have yet to be analyzed in detail.Cell143,December10,2010ª2010Elsevier Inc.879Strikingly,ESCRT-I,-II,and -III all localize to the bud neck (Wollert and Hurley,2010).ESCRT-III subunits assemble into tubular structures in vitro and when overexpressed (Bajorek et al.,2009;Hanson et al.,2008;Lata et al.,2008).The ESCRT-III proteins coat the interior of lipid tubes created in vitro (Lata et al.,2008)and have diameters of 40–50nm for lipid-free tubes,and 100nm for lipid-coated tubes.These tubes exceed the narrowest dimensions of bud necks in cells,based on just a few observations that suggest a size closer to 20nm (Murk et al.,2003).However,the tubes taper to a dome at their ends (Fabrikant et al.,2009),which may repre-sent the tubes’most important functional feature.Lipid tube extrusion by ESCRT-III seems to have no special lipid require-ments,as it can be supported in vitro by a simple mixture of the unsaturated phospholipids SOPC and DOPS (Lata et al.,2008).Indeed,whereas most ESCRTs are unique to the eukarya,ESCRT-III is conserved in a subset of Archaea,where it functionsin the membrane abscission step of cell division (Linda˚s et al.,2008;Samson et al.,2008).Thus the Archaeal ESCRT-III ortho-logs can presumably function in membrane scission with Archaeal lipids,which are radically different from eukaryotic lipids and rich in rigid,bilayer-spanning tetraether linkages (Koga and Morii,2005).It is thought on theoretical grounds that membrane tubes are induced by the binding of the curved ESCRT-III polymer to the membrane (Lenz et al.,2009).ESCRT-III polymerization governs the late stage of neck devel-opment leading to scission,but it is not likely to be the main factor in the initial budding event.The initial formation of the bud is driven by the assembly of ESCRT-I and -II with one another and with the endosome membrane (Wollert and Hurley,2010).The structure of this assembly is unknown,and the nature of the assembly is a pressing question in the fiposite structures of the ESCRT-I and -II complexes have been devel-oped on the basis of crystal structures of the separate compo-nents together with hydrodynamic information of thecompleteFigure 5.Multivesicular Bodies Bud via Diverse Mechanisms(A)Multivesicular bodies (MVBs)form from late en-dosomes in animal cells.Their formation is depen-dent on both ESCRT complexes and the unusual lipid lysobisphosphatidic acid (LBPA).(B)The conserved ESCRT-dependent MVB biogenesis pathway from early endosomes in yeast and animal cells.PI(3)P has been directly visualized in these MVBs.Cholesterol has been visualized in MVBs from animal cells,but it has not been directly confirmed whether these are ESCRT dependent or not.(C)Specialized formation of MVBs containing polymerized Pmel17.(D)Ceramide-dependent MVBs bud from raft-like and tetraspanin-enriched microdomains in animal cells.complexes in solution (Im and Hurley,2008;Kostelansky et al.,2007).These structures show that multiple membrane and ESCRT-III attachment sites are sepa-rated by rigid spacers of up to 18nm across,suggesting a mechanism toinduce or at least stabilize formation of a membrane neck of roughly those dimensions.Subsequent recruitment and poly-merization of ESCRT-III into spiral domes (Fabrikant et al.,2009)would then narrow and sever the neck in the current model (Hurley and Hanson,2010).The observation that the ESCRT complexes localize to the bud neck explains how they bud membranes away from the cytosol without themselves being consumed in the bud.This mechanism stands in sharp contrast to the familiar budding of coated vesi-cles toward cytosol,described above.The thermodynamic driving force for the pathway is the coupling of ESCRT-III solubi-lization and recycling to ATP hydrolysis by the dodecameric AAA ATPase Vps4(Babst et al.,1998;Wollert et al.,2009).Although the overall thermodynamic driving force is clear,the energetic trajectory of neck-directed bud formation is currently unknown.Theoretical analysis of the membrane mechanics of this process is urgently needed,as is a better understanding of the roles of lipids.All four ESCRT complexes are conserved between yeast and metazoa.In its broad outlines,the ESCRT-dependent conver-sion of early endosomes into MVBs is the same in yeast and metazoa (Raiborg and Stenmark,2009).Intralumenal vesicles in mammalian cells are highly enriched in cholesterol and tetra-spanins (Mo¨bius et al.,2003;van der Goot and Gruenberg,2006).However,at least some of the cholesterol-and tetraspa-nin-rich intralumenal vesicles in mammalian cells are part of process that is distinct from the ESCRT pathway (Simons and Raposo,2009).Raft markers such as long-chain sphingomyelins transit through MVBs (Koivusalo et al.,2007).Consistent with a possible ESCRT-sterol connection,defects in ESCRT function block endosomal cholesterol transport in mammalian cells (Bishop and Woodman,2000;Peck et al.,2004).In yeast,ergos-terol and,more speculatively,Sna3(Piper and Katzmann,2007)might replace the roles of cholesterol and tetraspanins in micro-domain formation.Given that ESCRTs bud membranes without880Cell 143,December 10,2010ª2010Elsevier Inc.。

50音图教材平假名あ(a) い(i) う(u) え(e) お(o)片假名ア(a) イ(i) ウ(u) エ(e) オ(o)あいさつ【挨拶】打招呼(1)アメリカ【U.S.A】美国(0)いんさつ【印刷】印刷(0)インストール【Installation】安装(4)うれしい【嬉しい】高兴(3)ウイスキー【Whiskey】威士忌酒(2)えいが【映画】电影(0)(1)エラー【Error】错误(1)おなか【お腹】肚子(0)オレンジ【Orange】桔子(2)平假名か(ka) き(ki) く(ku) け(ke) こ(ko)片假名カ(ka) キ(ki) ク(ku) ケ(ke) コ(ko)かわいい【可愛い】可爱(3)カーテン【Curtain】窗帘(1)きおく【記憶]】记忆(0)キーワード【Keyword】关键词(3)くうき【空気】空气、气氛(1)クール【Cool】酷(1)けんこう【健康】健康(0)ケーキ【Cake】蛋糕(1)こども【子供】小孩(0)コーヒー【Coffee】咖啡(3)平假名さ(sa) し(xi) す(su) せ(se) そ(so) 片假名サ(sa) シ(xi) ス(su) セ(se) ソ(so)さいきん【最近】最近(0)サッカー【Soccer】足球(1)しごと【仕事】工作(0)シーズン【Season】季节(1)すし【寿司】寿司(1)(2)スーツ【Suit】西服(1)せいと【生徒】学生(1)セール【Sale】促销(1)そうぞう【想像】想像(0)ソックス【Socks】袜子(1)平假名た(ta) ち(chi) つ(tsu) て(te) と(to) 片假名タ(ta) チ(chi) ツ(tsu) テ(te) ト(to)たいふう【台風】台风(3)タイプ【Type】型(1)ちきゅう【地球】地球(0)チーズ【Cheese】奶酪(1)つくえ【机】书桌(0)ツール【Tool】工具(0) (1)ていし【停止】停止(0)テーブル【Table】饭桌(0)ともだち【友達】朋友(0)トイレ【Toilet】厕所(1)平假名な(na) に(ni) ぬ(nu) ね(ne) の(no) 片假名ナ(na) ニ(ni) ヌ(nu) ネ(ne) ノ(no)なまえ【名前】名字(0)ナース【Nurse】护士(1)にんげん【人間】人(0)ニーズ【Needs】需要(1)ぬくもり【温もり】温暖(0) (4)ヌードル【Noodle】面条(1)ねがい【願い】愿望(2)ネーム【Name】姓名(0)(1)のうぜい【納税】纳税(0)ノート【Note】笔记本(1)平假名は(ha) ひ(hi) ふ(fu) へ(he) ほ(ho) 片假名ハ(ha) ヒ(hi) フ(fu) ヘ(he) ホ(ho)はかせ【博士】博士 (1)ハート【Heart】心 (0) (1)ひみつ【秘密】秘密 (0)ヒーロー【Hero】英雄 (1)ふかのう【不可能】不可能 (2)フォーラム【Forum】论坛 (1)へいき【平気】没事很冷静 (0)ヘルパー【Helper】助手 (1)ほめる【褒める】称赞、夸奖 (2)ホット【Hot】热 (1)平假名ま(ma) み(mi) む(mu) め(me) も(mo) 片假名マ(ma) ミ(mi) ム(mu) メ(me) モ(mo)まほう【魔法】台风 (0)マイク【Mic】麦克 (1)みらい【未来】未来 (1)ミラー【Mirror】镜子 (1)むすめ【娘】女儿、女孩 (3)ムード【Mood】气氛 (1)めし【飯】饭 (2)メール【mail】电子邮件 (0) (1)もも【桃】桃子 (0)モンスター【Monster】怪兽 (1)平假名や(ya) ゆ(yu) よ(yo)片假名ヤ(ya) ユ(yu) ヨ(yo)やくそく【約束】约定 (0)ヤンキー【Yankee】洋气的年轻人美国人 (1)ゆめ【夢】梦、梦想 (2)ユーザー【User】用户 (0)(1)よる【夜】夜晚 (1)ヨーグルト【Yogurt】酸奶 (3)平假名ら(ra) り(ri) る(ru) れ(re) ろ(ro)片假名ラ(ra) リ(ri) ル(ru) レ(re) ロ(ro)らいねん【来年】来年 (0)ランチ【Lunch】午餐 (1)りかい【理解】理解 (1)リボン【Ribbon】发带 (1)るいけい【累計】累计 (0)ルーキー【Rookie】新手 (1)れきし【歴史】历史 (0)レモン【Lemon】柠檬 (1)ろうじん【老人】老人 (0)ロウソク【蠟燭】蜡烛 (3)(4)平假名わ(wa) を(wo/o)ん(n)片假名ワ(wa) ヲ(wo/o)ン(n)わしょく【和食】日本料理 (0)ワイン【Wine】红酒 (1)ぼうしをかぶる【帽子を被る】把帽子戴上浊音：平假名が(ga) ぎ(gi) ぐ(gu) げ(ge) ご(go)片假名ガ(ga) ギ(gi) グ(gu) ゲ(ge) ゴ(go)がいこく【外国】外国 (0)ガール【Girl】女孩子 (1)ぎもん【疑問】疑问 (0)ギター【Guitar】吉他 (1)ぐうぜん【偶然】偶然 (0)グラス【Glass】玻璃杯 (1)げんきん【現金】现金 (3)ゲーム【Game】游戏 (1)ごうかく【合格】合格 (0)ゴリラ【Gorilla】大猩猩 (1)平假名ざ(za) じ(zi/ji) ず(zu) ぜ(ze) ぞ(zo)片假名ザ(za) ジ(zi/ji) ズ(zu) ゼ(ze) ゾ(zo)ざいじゅう【在住】在居 (0)ザーサイ【搾菜】榨菜 (0)じかん【時間】时间 (0)ジーンズ【Jeans】牛仔裤 (1)ずめん【図面】图纸 (0)ズボン【(法)Jupon】裤子 (1)(2)ぜいかん【税関】海关 (0)ゼリー【Jelly】冻胶、果冻 (1)ぞうすい【雑炊】稀粥 (0)ゾーン【Zone】区域 (1)平假名だ(da) ぢ(di/ji) づ(du/zu) で(de) ど(do) 片假名ダ(da) ヂ(di/ji) ヅ(du/zu) デ(de) ド(do)だいじょうぶ【大丈夫】没问题 (3)ダーツ【Darts】镖 (1)はなぢ【鼻血】鼻血 (0)いいづらい【言い辛い】很难开口 (4)でんごん【伝言】口信 (0)デート【Date】约会 (1)どうい【同意】同意 (0)ドア【Door】门 (1)平假名ば(ba) び(bi) ぶ(bu) べ(be) ぼbo)片假名バ(ba) ビ(bi) ブ(bu) ベ(be) ボ(bo)ばか【馬鹿】傻子 (1)バイキング【Viking】自助餐 (1)びんぼう【貧乏】贫穷 (1)ビール【Beer】啤酒 (1)ぶどう【葡萄】葡萄 (0)ブーム【Boom】热潮、流行 (1)べんきょう【勉強】学习 (0)ベル【Bell】铃 (1)ぼうえき【貿易】贸易 (0)ボス【Boss】老板、老大 (1)平假名ぱ(pa) ぴ(pi) ぷ(pu) ぺ(pe) ぽ(po)片假名パ(pa) ピ(pi) プ(pu) ペ(pe) ポ(po)ぱちんこ【Pachinko】日本赌博机；弹弓 (0)パパ【Papa】爸爸 (1)ぴかぴか【Pikapika】闪闪、光亮 (0)(1)(2)ピアノ【Piano】钢琴 (0)ぷうたろう【風太郎】无业游民 (0)プライド【Pride】自尊 (0)ぺちゃんこ【Pechanko】压扁、扁扁的 (0)(2) ペキン【Beijing】北京 (1)ぽかぽか【Pokapoka】暖暖的 (1)ポリシー【Policy】政策 (1)平假名きゃ(kya) きゅ(kyu) きょ(kyo)片假名キャ(kya) キュ(kyu) キョ(kyo)きゃく【客】客人 (0)キャラクター【Character】人物 (2)(1)きゅうか【休暇】休假 (0)キュート【Cute】可爱 (1)きょう【今日】今天 (1)キョンシー【Jiangshi】僵尸 (1)平假名しゃ(sya) しゅ(syu) しょ(syo)片假名シャ(sya) シュ(syu) ショ(syo)しゃかいじん【社会人】社会人 (2)シャーペン【Sharp+Pencil】自动铅笔 (0)しゅうちゃく【執着】执着 (0)シュレッダー【Shredder】切书机 (2)しょうかい【紹介】介绍 (0)ショールーム【Showroom】商品陈列室 (3)平假名ちゃ(cya) ちゅ(cyu) ちょ(cyo)片假名チャ(cya) チュ(cyu) チョ(cyo)ちゃいろ【茶色】茶色 (0)チャイナ【China】中国 (1)ちゅうごく【中国】中国 (1)チューナー【Tuner】调谐器 (0)(1)ちょうせい【調整】调整 (0)チョイス【Choice】选择 (1)平假名にゃ(nya) にゅ(nyu) にょ(nyo)片假名ニャ(nya) ニュ(nyu) ニョ(nyo)こんにゃく【蒟蒻】鬼芋 (3)(4)ニャーニャー【Nya-nya-】猫的哭叫声 (1)にゅうせき【入籍】入籍 (0)ニュース【News】新闻 (1)にょうぼう【女房】妻子 (1)ニョロニョロ【Nyoronyoro】弯曲的 (1)平假名ひゃ(hya) ひゅ(hyu) ひょ(hyo)片假名ヒャ(hya) ヒュ(hyu) ヒョ(hyo)ひゃっかてん【百貨店】百货店 (3)(0)ヒャヒャヒャ【Hyahyahya】奸笑声 (1)ひゅうが【日向】地名 (1)ヒューストン【Houston】休斯敦 (1)ひょうか【評価】评价 (1)ヒョウ【豹】豹 (1)平假名みゃ(mya) みゅ(myu) みょ(myo)片假名ミャ(mya) ミュ(myu) ミョ(myo)みゃく【脈】脉 (2)ミャンマー【Myanmar】缅甸 (1)ミュージック【Music】乐曲、音乐 (1)ミュージカル【Musical】音乐剧；歌舞剧 (1)みょうじ【名字】姓名 (1)みょうにち【明日】明天、明日 (1)平假名りゃ(rya) りゅ(ryu) りょ(ryo)片假名リャ(rya) リュ(ryu) リョ(ryo)りゃくご【略語】省略语 (0)りゃくず【略図】省略图 (0)りゅうこう【流行】流行 (0)リュック【Rucksack】背包 (1)りょうり【料理】料理 (1)りょうど【領土】领土 (1)平假名ぎゃ(gya) ぎゅ(gyu) ぎょ(gyo)片假名ギャ(gya) ギュ(gyu) ギョ(gyo)ぎゃく【逆】反 (0)ギャンブル【Gamble】赌博 (1)ぎゅうどん【牛丼】牛肉饭 (0)ギュッと【Gyutto】紧紧的 (0)(1)ぎょうむ【業務】业务 (1)ギョーザ【Jiaozi】饺子 (0)平假名じゃ(jya) じゅ(jyu) じょ(jyo)片假名ジャ(jya) ジュ(jyu) ジョ(jyo)じゃま【邪魔】障碍、碍事 (0)ジャガー【Jaguar】美洲豹 (1)じゅうぶん【十分】十分 (3)ジュース【Juice】果汁、饮料 (1)じょうだん【冗談】玩笑 (3)ジョーク【Joke】玩笑 (1)平假名びゃ(bya) びゅ(byu) びょ(byo)片假名ビャ(bya) ビュ(byu) ビョ(byo)びゃくや【白夜】白夜 (1)さんびゃく【三百】三百 (1)ビュアー【Viewer】观看者看片机 (1) ビューティー【Beauty】美 (1)びょうき【病気】病 (0)びょうどう【平等】平等 (0)平假名ぴゃ(pya) ぴゅ(pyu) ぴょ(pyo)片假名ピャ(pya) ピュ(pyu) ピョ(pyo)ろっぴゃく【六百】六百 (0)(3)はっぴゃく【八百】八百 (0)(3)ピューマ【Puma】彪马、美洲狮 (1) ピュア【Pure】纯洁 (1)はっぴょう【発表】发表 (0)ピョンヤン【平壌】平壤 (1)。

2010年黑龙江省成人本科毕业生申请学士学位（150分钟100分）注：答案写在答题纸上，写在试卷上无效。

试卷一I．文字（共20题，10分，考试时间10分钟）一、次の文のの漢字の最も適切な読み方をそれぞれ選択肢ABCDの中から一つ選び、解答用紙にその符号に印をつけなさい。

(0.5×10=5点)1. 一度食べてみましたが、刺身はあまりおいしくなかった。

A さしみB おすしC てんぷらD さらだ2．毎日は大学院生の入学試験の準備で忙しい。

A じゅんびB じゅんぴC しゅんびD しゅんぴ3．古いカーテンの生地を利用し、工夫をして子供の服を作った。

A こうじょうB くうきC くふうD くうこう4. 時間を無駄にしたくないから、飛行機に乗ることにした。

A むちゃB むだC ぶじD むた5．息子は最近ゲームに熱中していて、ちっとも勉強しない。

AねじゆうBねつじゆうCねっちゆDねっちゅう6．彼は一人で細かい作業をしている。

AふかいBこまかいCみじかいDあたたかい7．2008年8月８日、北京で29回のオリンピックが行われました。

AおそわれましたBいわれましたCおこなわれましたDかわれました8．朝4時に起きるのは無理ですよ。

A しじB よんじC よじD くじ9．観光客が訪れるような都市にはたいてい両替所がある。

A おくれるB わかれるC おとずれるD はなれる10．長崎では８日、63回目の原爆の日を迎えた。

A かんがえたB まちがえた Cむかえた D こたえた二、次の文の＿＿＿＿の言葉は、どのような漢字を書きますか。

その漢字をABCDの中から一つ選び、解答用紙にその符号に印をつけなさい。

(0.5×10=5点)11.日本の会社では男性と女性はきゅうりょうが違うそうです。

A 給料B 両側C 性質D 性格12.張さんはいつもせいけつな感じがしています。

A 綺麗B 整然C 清潔D 簡潔13.りっぱな通訳になるつもりで、毎日頑張っています。

TITLE : オフィスラブ――甘い誘惑講談社電子文庫オフィスラブ――甘い誘惑阿部牧郎著目次§１オフィスラブ講座§２オフィスラブ――甘い誘惑First Night 聖夜の仔猫Second Night 二人だけの忘年会Third Night 二人だけの晴着Last Night 成人式――パエリアの日オフィスラブ――甘い誘惑§１オフィスラブ講座Lesson１サラリーマンにとってオフィスは花園である週に一、二度、私は大阪北新地（きたしんち）の酒場街へ出向く。

もう二十年来の習慣である。

酒場から酒場へ移動する途中、通りをぶらつく大勢の人々とすれちがう。

おどろくほど人通りが多い。

私の若いころ、北新地は高級クラブ、高級料亭が軒（のき）なみで、足をふみいれるのさえ恐れ多かったものだった。

いまはラウンジバー、カラオケバーが増えた。

手軽なスナックバーが数多くある。

偉い人だけでなく、若いサラリーマンも大勢出入りしている。

時代は変った。

人通りのなかにギャルがたくさんいる。

ふつうの会社のＯＬである。

男性社員とグループで飲みにきた子がほとんどである。

ほんの十年まえは、夜、北新地で見かける女性は九十九パーセントが酒場のホステスだった。

通りを歩く女性にかぎっての話だが、いまはＯＬのほうがはるかに多い。

しかも美人の率が高いのである。

すれちがう瞬間、ふっと足をとめて眺めたくなる女性の圧倒的多数がふつうの女の子なのだ。

酒場へ入って、なかで働く女性を見てがっかりすることがある。

この程度の女を相手になんで高価（たか）い酒を飲まなくてはならないのかという気になる。

夜の世界へ入ってくる女性が尐くなって、業界全体がレベルダウンしたことははっきりしている。

だが、私のような書斎労働者は、一般社会のふつうの女の子に接するチャンスがまったくない。

酒場のホステス以外、ゆっくりことばをかわせる女性がいないのである。

やむをえず酒場でおろかな時間をすごす。

あア a ---あ：来源“安”，ア：来源“阿”左侧部分。

记忆方式：阿安来了-----“安”对应“あ”，“了”这里对应“ア”いイ i ---い：来源“以”，イ：来源“伊”左侧部分。

记忆方式：以理服人-----“以”对应“い”，“人”对应“イ”うウ u ---う：来源“宇”，ウ：来源“宇”上半部分。

记忆方式：屋顶看宇宙-----“宇”对应“ウ”えエ e ---え：来源“衣”，エ：来源“江”右侧部位记忆方式：爱上元首工作-----“元”对应“え”，“工”对应“エ”おオ o ---お：来源“於”，オ：来源“於”左侧部分记忆方式：奥运求才----“求”对应“お”，“才”对应“オ”かカ ka ---か：来源“加”，カ：来源“加”左侧部分记忆方式：卡车加力-----“加”对应“か”，力对应“カ”きキ ki ---き：来源“几”，キ：来源“几”记忆方式：kim丰衣足食-----“丰”对应“き”“キ”くク ku ---く：来源“久”，ク：来源“久”左侧部分记忆方式：哭了很久-----哭的读音嘴唇就是く的样子，“久”对应“ク”けケ ke ---け：来源“计”，ケ：来源“介”记忆方式：凯恩计划介入-----“计”对应“け”，“介”对应“ケ”こコ ko ---こ：来源“己”，コ：来源“已”上半部分记忆方式：靠自己-----“己”对应“こ”“コ”さサ sa ---さ：来源“左”，サ：来源“散”左上角记忆方式：撒腿就跑-----“撒”对应“サ”，跑的样子就是象“さ”しシ si/shi ---し：来源“之”，シ：来源“之”记忆方式：洗毛笔-----“洗”对应“シ”，毛笔的形状就象“し”すス su ---す：来源“寸”，ス：来源“须”繁体右下角记忆方式：束起胡须-----“束”对应“す”，“须”对应“ス”せセ se ---せ：来源“世”，セ：来源“世”记忆方式：赛车世界-----“世”对应“せ”“セ”そソ so ---そ：来源“曾”，ソ：来源“曾”记忆方式：扫荡3关-----“3”对应“そ”，“关”对应“ソ”たタ ta ---た：来源“太”，タ：来源“多”记忆方式：他太多变-----“多”对应“タ”ちチ chi ---ち:来源“知”，チ：来源“千”记忆方式：千年古器-----“千”以及“千”开始的发音对应“チ”，“古”对应了“ち”つツ tsu ---つ：来源“川”，ツ：来源“川”记忆方式：刺激的川菜-----“川”对应“ツ”てテ te ---て：来源“天”，テ：来源“天”记忆方式：台币7元-----“7”对应“て”，“元”对应“テ”とト to ---と：来源“止”，ト：来源“止”记忆方式：偷上萝卜-----“上”对应“と”，“卜”对应“ト”なナ na ---な：来源“奈”，ナ：来源“奈”左上角记忆方式：那般奈何-----“奈”对应“ナ”にニ ni ---に：来源“仁”，ニ：来源“二”记忆方式：泥仁-----“仁”对应“に”“ニ”ぬヌ nu ---ぬ：来源“奴”，ヌ：来源“奴”右侧部分记忆方式：奴才又来了-----“奴”对应“ぬ”，“又”对应“ヌ”ねネ ne ---ね：来源“祢”，ネ：来源“祢”记忆方式：内衣扔了-----“衣”对应“ネ”，“扔”对应“ね”のノ no ---の：来源“乃”，ノ：来源“乃”记忆方式：挠四下痒痒-----“四”对应“の”，痒痒棒对应“ノ”はハ ha ---は：来源“波”，ハ：来源“八”记忆方式：哈利波特和八哥-----“波”对应“は”，“八”对应“ハ”ひヒ hi ---ひ：来源“比”，ヒ：来源“比”右侧部分记忆方式：黑夜比武-----“比”对应“ヒ”ふフ fu ---ふ：来源“不”，フ：来源“不”左上部分记忆方式：服不服小子-----“不”对应“フ”，“小”对应“ふ”へヘ he ---へ：来源“部”，ヘ：来源“部”右侧部分变形记忆方式：海角7号----“7”对应“へ”ほホ ho ---ほ：来源“保”，ホ：来源“保”右下部分记忆方式：好好环保-----“保”对应“木”まマ ma ---ま：来源“末”，マ：来源“末”记忆方式：抹布坏了-----“抹”对应“ま”，“了”在这里对应“マ”みミ mi ---み：来源“美”，ミ：来源“三”记忆方式：米有三升-----“三”对应“ミ”，“升”对应“み”むム mu ---む：来源“武”，ム：来源“牟”上半部分记忆方式：母犬上台-----“犬”可以对应“む”，“台”的上面对应“ム”めメ me ---め：来源“女”，メ：来源“女”记忆方式：麦女士错了-----“女”对应“め”，错了对应“メ”もモ mo ---も：来源“毛”，モ：来源“毛”记忆方式：毛毛雨-----“毛”对应“も”“モ”やヤ ya ---や：来源“也”，ヤ：来源“也”记忆方式：亚军也好-----“也”对应“や”“ヤ”ゆユ yu ---ゆ：来源“由”，ユ：来源“由”右侧部分记忆方式：由2姐（尤二姐）-----“2”对应“ユ”よヨ yo ---よ：来源“与”，ヨ：来源“与”下半部分记忆方式：钥匙与锁-----钥匙的形状对应“よ”，“与”对应“ヨ”らラ ra ---ら：来源“良”，ラ：来源“良”右上部分记忆方式：辣椒5文钱-----5对应“ら”，“文”对应“ラ”りリ ri ---り：来源“利”，リ：来源“利”右边部分记忆方式：利剑-----“利”对应“り”“リ”るル ru ---る：来源“留”，ル：来源“流”右下部分记忆方式：陆家3儿-----“3”对应“る”，“儿”对应“ル”れレ re ---れ：来源“礼”，レ：来源“礼”右侧部分记忆方式：来送礼-----“礼”对应“れ”“レ”ろロ ro ---ろ：来源“吕”，ロ：来源“吕”上半部分记忆方式：老3口-----“3”对应“ろ”，“口”对应“ロ”わワ wa ---わ：来源“和”，ワ：来源“和”右上部分记忆方式：娃娃打它-----“打”对应“わ”，“它”上部对应“ワ”をヲ o/wo ---を：来源“远”，ヲ：来源“乎”记忆方式：澳洲大于cuba（古巴）-----大于C对应“を”，大于对应“ヲ”んン n ---ん：来源“无”，ン：来源“尔”记忆方式：嗯有二人-----“人”对应“ん”，“二”对应“ン”。

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辣là藏cáng 粉fěn挂guà 搬bān某mǒu 涮shuàn 穷qióng 任rèn 谢xiè秋qiū断duàn 童tóng 女nǚ略lüè 卷juàn 涛tāo 邹zōu麻má日rì朱zhū苗miáo 低dī宣xuān 泼pō涩sè 卫wèi 白bái 册cè牛niú 雁yàn 垮kuǎ陪péi 波bō姚yáo 管guǎn 兄xiōng 喊hǎn 击jī郑zhèng 淌tǎng 袄ǎo 平píng 乃nǎi 石shí饶ráo 善shàn 冲chōng娘niáng 点diǎn 怪guài 哑yǎ掉diào 屉tì否fǒu 滚gǔn 薛xuē武wǔ仇chóu 爱ài 纺fǎng 拼pīn叶yè 举jǔ矿kuàng 鹅é 容róng 晕yùn 块kuài 荫yìn 群qún 称chēng 贰èr 苏sū怀huái 决jué 翁wēng 辞cí御yù 座zuò 旬xún 亮liàng 灰huī索suǒ秧yāng扔rēng 子zǐ尊zūn黄huáng 蹭cèng 舜shùn测试题-10读单音节字词100个麻má 辈bèi 特tè 废fèi 办bàn 否fǒu 盼pàn 奔bēn黑hēi 绑bǎng 敢gǎn 嫩nèn 瞪dèng 批pī灭miè 撇piē扁biǎn 渺miǎo 致zhì屏píng 免miǎn 品pǐn 炕kàng 恨hèn 斋zhāi赦shè 丢diū挑tiāo 劣liè 热rè 妞niū炒chǎo 则zé 擦cā复fù 愁chóu 烧shāo 灾zāi 次cì撒sā佛fó 酿niàng 邻lín 加jiā骑qí饶ráo 衬chèn 宁níng 下xià 赛sài 草cǎo 乘chéng 而ér 哀āi生shēng 让ràng 搜sōu 案àn 亲qīn 呕ǒu 浆jiāng 古gǔ挂guà 推tuī段duàn 挎kuà 国guó 姓xìng 吨dūn 铸zhù 怀huái 穷qióng 吞tūn 栋dòng 款kuǎn 悔huǐ刷shuā滚gǔn 拽zhuài 作zuò 踹chuài 拢lǒng 框kuàng 女nǚ军jūn 嘴zuǐ涮shuàn 红hóng 略lüè 穗suì撞zhuàng 锯jù 存cún 躯qū捐juān 瘸qué 穴xué 全quán 殉xùn 熊xióng测试题-11读单音节字词100个捐juān 缴jiǎo 琴qín 揣chuǎi 哪nǎ稻dào 增zēng 怀huái 阔kuò 甲jiǎ江jiāng 留liú 壮zhuàng 训xùn 湾wān 疼téng 花huā嫩nèn 舜shùn 光guāng 藏cáng 杯bēi星xīng 水shuǐ特tè 惊jīng 首shǒu 绿lǜ铅qiān 立lì串chuàn 捏niē入rù 表biǎo 色sè 乡xiāng唤huàn 扫sǎo 铐kào 锌xīn铁tiě日rì取qǔ浓nóng 军jūn笨bèn 三sān 面miàn 瞎xiā阅yuè 孩hái 勇yǒng 绝jué梦mèng 放fàng 冰bīng 孔kǒng 腮sāi浙zhè 温wēn求qiú 槛jiàn 牛niú 恰qià 擦cā法fǎ毒dú 锐ruì专zhuān 耍shuǎ飘piāo 外wài 穷qióng 费fèi 村cūn 否fǒu 拼pīn揭jiē略lüè刮guā共gòng 怪guài测试题-12读单音节字词100个掐qiā乐lè 您nín 掀xiān擦cā丈zhàng 清qīng 埋mái 损sǔn 丁dīng 暖nuǎn 对duì促cù 铜tóng 任rèn 卡qiǎ古gǔ揭jiē丸wán 吞tūn 抓zhuā修xiū荡dàng 旺wàng 摔shuāi畏wèi 脸liǎn 热rè 把bǎ耗hào 平píng 筛shāi 亏kuī否fǒu 瓦wǎ棍gùn 松sōng 匀yún 女nǚ用yòng 喜xǐ说shuō揣chuǎi 咱zán 佛fó 此cǐ勋xūn 院yuàn 子zǐ钻zuān 牙yá 民mín 饭fàn 北běi何hé 凋diāo坡pō观guān 骗piàn 荒huāng烤kǎo 赔péi 级jí贪tān抢qiǎng 风fēng 理lǐ缤bīn能néng 锅guō邻lín 口kǒu 而ér 翁wēng 掠lüè 羊yáng 思sī全quán 捏niē灾zāi 穷qióng 体tǐ针zhēn 描miáo 月yuè 容róng 参cān 歪wāi 续xù 贴tiē搜sōu 场cháng 拨bō是shì支zhī窗chuāng 目mù 耻chǐ掘jué 熬āo测试题-13读单音节字词100个摆bǎi 判pàn 门mén 钉dīng 肥féi 赴fù 舔tiǎn 妞niū尼ní否fǒu 冒mào 军jūn 穷qióng 吃chī蝻nǎn 逮dài 溶róng 葱cōng 曾zēng 枕zhěn 字zì苏sū软ruǎn 淌tǎng 横héng 用yòng 石shí善shàn 此cǐ薄báo 骗piàn 能néng 懂dǒng 屯tún 段duàn 女nǚ嗑kē塔tǎ致zhì吵chǎo 纫rèn 坡pō病bìng 脑nǎo 乱luàn 国guó垮kuǎ翁wēng垒lěi 邻lín 铐kào 画huà 拐guǎi 狂kuáng 鬼guǐ略lüè 选xuǎn 绿lǜ红hóng 悔huǐ叫jiào 掐qiā嗅xiù野yě王wáng 袄ǎo 册cè 扎zā而ér 几jī肖xiāo妾qiè 僵jiāng 朱zhū伪wěi揣chuǎi 双shuāng越yuè 霞xiá 顺shùn 琴qín 襄xiāng 闯chuǎng 邢xíng 撒sā却què 熏xūn 具jù 群qún 鳃sāi 雁yàn 权quán 四sì长cháng 邹zōu 晌shǎng 豁huò熟shú跌diē轴zhóu测试题-14读单音节字词100个拔bá 涩sè 日rì发fā次cì铐kào 二èr 海hǎi 黑hēi早zǎo 怎zěn 透tòu 烂làn 就jiù 恨hèn 唱chàng 风fēng成chéng 俩liǎng 票piào 拣jiǎn 午wǔ您nín 末mò 枪qiāng 平píng 数shù 翁wēng 多duō块kuài 推tuī弯wān 准zhǔn 猜cāi 慌huāng 懂dǒng 女nǚ矮ǎi 快kuài 圆yuán 穷qióng 舍shè 似sì非fēi操cāo 仇chóu 版bǎn 粉fěn 劣liè 苗miáo 人rén 溜liū棉mián 拼pīn家jiā习xí国guó 娘niáng 俯fǔ瓜guā播bō晴qíng 左zuǒ观guān吞tūn 庄zhuāng 容róng 旅lǚ具jù 寻xún 涌yǒng 鹤hè 石shí逮dài 宣xuān 脑nǎo 残cán 偶ǒu 判pàn 枕zhěn 蚌bàng 膛táng 响xiǎng 尼ní叶yè 夸kuā药yào 舔tiǎn 秦qín 杨yáng 苏sū索suǒ揣chuǎi 委wěi涮shuàn 润rùn 旺wàng 农nóng 薛xuē群qún测试题-15读单音节字词100个惹rě渠qú 准zhǔn 丢diū尽jìn 雄xióng 染rǎn 杂zá 捐juān 名míng 鲜xiān 弱ruò 钻zuān肥féi 某mǒu 遍biàn 罩zhào 沏qī甲jiǎ吓xià 妾qiè 邹zōu判pàn 瞟piǎo 沓tà 北běi坡pō冒mào 对duì风fēng 捌bā俯fǔ跎tuó 惯guàn 俩liǎng 炕kàng 怎zěn 苔tái 铙náo 逆nì铁tiě来lái 夸kuā横héng 奴nú 刷shuā久jiǔ别bié 黑hēi 顶dǐng 沈shěn 嘭pēng藕ǒu 拈niān 槛jiàn 偿cháng 您nín 歌gē尺chǐ烂làn 猜cāi 券quàn 晃huǎng 瓜guā溜liū桨jiǎng 蹭cèng 疮chuāng鹤hè 晕yùn 姚yáo 踹chuài 舜shùn 逮dài 根gēn 孔kǒng 坏huài 而ér 涮shuàn 梯tī浙zhè 蚌bàng 苏sū雪xuě穷qióng 司sī苗miáo 粉fěn 翁wēng 略lüè 笋sǔn 贫pín 脆cuì寻xún 铝lǚ撒sā菌jūn 从cóng 晌shǎng 卫wèi测试题-16读单音节字词100个诈zhà 惹rě而ér 紫zǐ迟chí碑bēi 拆chā i 冒mào 否fǒu 南nán 粉fěn裆dāng耕gēng 起qǐ俩liǎng 丢diū表biǎo 变biàn 瞥pi ē拼pīn酿niàng 平píng 扑pū挎kuà 播bō阔kuò 乖guāi退tuì断duàn 抡lūn 光guāng弄nòng 翁wēng举jǔ略lüè 泉quán 均jūn 穷qióng 扎zā涩sè 司sī使shǐ筛shāi废fèi 找zhǎo 偶ǒu 山shān恨hèn 扛káng 仍réng 习xí加jiā灭miè 跳tiào 牛niú 甜tián 民mín 亮liàng 鸣míng 促cù 抓zhuā佛fó 若ruò甩shuǎi 绘huì卵luǎn 纯chún 矿kuàng 红hóng 岸àn 决jué 癣xuǎn 熏xūn 雄xióng 损sǔn 采cǎi 赠zèng 忍rěn 盎àng 簪zān 疫yì截jié 邀yāo 雁yàn 荫yìn 仰yǎng 顶dǐng 蒜suàn 村cūn 壮zhuàng 荣róng 御yù 远yuǎn 躯qū恩ēn 擦cā袄ǎo 勇yǒng 恽yùn 学xué测试题-17读单音节字词100个多duō她tā碑bēi判pàn 某mǒu 胞bāo肯kěn 膘biāo 童tóng 扇shàn 表biǎo 言yán 恩ēn 层céng 润rùn 坏huài 磅bàng 贫pín 索suǒ肉ròu 涌yǒng 绝jué 共gòng 女nǚ乱luàn 浮fú 面miàn 增zēng 瞎xiā接jiē元yuán 区qū略lüè 钻zuān 平píng 摸mō方fāng 敌dí苔tái 聂niè 淡dàn 废fèi 贰èr 涩sè 采cǎi 朱zhū净jìng 丢diū腻nì懒lǎn 虐nüè 穷qióng 旬xún 捆kǔn 隋suí花huā瓷cí野yě网wǎng 册cè 软ruǎn 冲chōng宣xuān均jūn 舜shùn 秦qín 灵líng 更gēng漱shù 谢xiè 涮shuàn 亏kuī俩liǎng 欢huān 杂zá 酱jiàng 铐kào 枕zhěn 尾wěi 窄zhǎi 损sǔn 瓦wǎ疮chuāng迁qiān勺sháo 安ān坐zuò 氧yǎng 拆chāi 邹zōu 邀yāo 撒sā牛niú 怪guài 催cuī郑zhèng 鹤hè 池chí给gěi 装zhuāng测试题-18读单音节字词100个矮ǎi 翁wēng色sè 词cí秒miǎo 咱zán 世shì齿chǐ拽zhuài 敲qiāo 絮xù 久jiǔ恒héng 垮kuǎ柑gān辣là 艇tǐng 饶ráo 贴tiē都dū移yí岸àn 草cǎo 滋zī若ruò 谁shuí叉chā枕zhěn 讯xùn 囚qiú 军jūn 逛guàng 开kāi给gěi抡lūn酿niàng 贴tiē肉ròu 潘pān莽mǎng 浮fú 靶bǎ庞páng 粉fěn段duàn 唐táng 旅lǚ牛niú 质zhì抠kōu伪wěi 枷jiā劝quàn 乡xiāng 唇chún 少shǎo 贼zéi 存cún 桑sāng姚yáo 我wǒ渊yuān 野yě司sī佐zuǒ褥rù 爽shuǎng 穿chuān 助zhù 卸xiè 寝qǐn 计jì掰bāi 您nín 坑kēng 俩liǎng 褪tùn 掂diān扉fēi 惹rě观guān 迸bèng 决jué 掩yǎn 舜shùn 喝hē外wài 穷qióng 样yàng 戎róng 濒bīn 闯chuǎng 踝huái 涌yǒng 划huá 凭píng 钟zhōng 人rén 虐nüè 丸wán测试题-19读单音节字词100个扒bā拜bài 迥jiǒng 憋biē田tián 咯kǎ晕yùn 废fèi 如rú 涡wō佘shé 扮bàn 罩zhào 胸xiōng量liáng 脱tuō流liú 鲜xiān 垧shǎng 驭yù 望wàng 菠bō砂shā掘jué 许xǔ块kuài 矜jīn 笋sǔn 曾zēng踹chuài 软ruǎn 佣yōng董dǒng 酿niàng 反fǎn 海hǎi 稚zhì铝lǚ慌huāng卷juàn 青qīng 所suǒ滑huá 省shěng 死sǐ围wéi 扭niǔ跨kuà 寻xún 阵zhèn 菌jūn 尿niào 棕zōng 堆duī槽cáo 鹌ān侧cè 碎suì欺qī淤yū窜cuàn 拐guǎi 疮chuāng 槛jiàn 盖gài 贼zéi 婆pó 提tí二èr 刨páo 灌guàn 铲chǎn 吓xià 苗miáo 轨guǐ掐qiā讽fěng恩ēn 灭miè 鱿yóu 脏zàng 肉ròu 粉fěn 茉mò 您nín 尺chǐ贫pín 劝quàn 莽m ǎng 略lüè 蹲dūn 猿yuán 共gòng 吐tǔ谋móu 饼bǐng 盘pán 狂kuáng 蔫niān 使shǐ测试题-20读单音节字词100个白bái 美měi份fèn 丢diū舔tiǎn 潘pān 跨kuà 豁huò 壮zhuàng 冤yuān啪pā胞bāo 否fǒu 浪làng 秦qín 揣chuǎi 顺shùn 翁wēng 酸suān玉yù 沓tà 类lèi 槛jiàn 悄qiǎo 芯xīn 触chù 刷shuā女nǚ颊jiá 润rùn 鹤hè 之zhī回huí静jìng 矩jǔ夏xià 肉ròu 吃chī日rì愁chóu 撇piē苗miáo 盯dīng挪nuó 龟guī捆kǔn 慌huāng 全quán 蔓màn 铁tiě炸zhà 石shí摸mō桃táo 妞niū晾liàng 贼zéi 亏kuī扎zā而ér 攒zǎn 扇shàn 蜂fēng 剃tì增zēng 阳yáng 外wài 均jūn 母mǔ平píng 地dì略lüè 瓷cí寺sì纫rèn 腌yān坡pō遍biàn 襄xiāng 癣xuǎn 才cái 奔bēn 藏cáng 腮sāi扇shàn 穷qióng 区qū洞dòng 槽cáo 涩sè 迥jiǒng 层céng 让ràng 虐nüè 浮fú 弄nòng 荀xún 辙zhé 增zēng 共gòng测试题-21读单音节字词100个铡zhá白bái 杀shā鹤hè痣zhì舌shé逮dài 若ruò池chí筛shāi 得dé字zì给gěi二èr 鳃sāi棉mián宰zǎi 拣jiǎn 凹āo 淋lín 槽cáo品pǐn 朝zhāo腔qiāng挠náo 巷xiàng 泡pào 柄bǐng 藕ǒu 另lìng邹zōu氢qīng轴zhóu 腹fù岸àn 努nǔ榄lǎn 筑zhù瘫tān哭kū判pàn粗cū忍rěn 藏cáng 午wǔ缸gāng震zhèn 纺fǎng 挂guà忙máng耍shuǎ憎zēng 祸huò乘chéng 索suǒ正zhèng踹chuài 缝féng 坏huài梦mèng隋suí戏xì褪tùn 溺n ì霞xiá款kuǎn 颊jiá环huán 掖yè蒜suàn 谢xiè弯wān 爹diē舜shùn飘piāo 损sǔn 表biǎo 闯chuǎng 修xiū撞zhuàng 玖jiǔ童tóng 约yuē胸xiōng 劝quàn 孔kǒng 徐xú绒róng俊jùn 翁wēng 略lüè宋sòng 群qún掘jué总zǒng 荀xún穷qióng 旅lǚ婶shěn卷juàn测试题-22读单音节字词100个偶ǒu 铡zhá 红hóng 我wǒ姨yí秋qiū次cì剜wān 逮dài 平píng 翁wēng 挠náo 氧yǎng 食shí判pàn 镖biāo 佣yōng 涩sè 糖táng 野yě敏mǐn 痣zhì丢diū遍biàn 捐juān 而ér 仍réng 接jiē水shuǐ日rì音yīn 劣liè奖jiǎng 花huā邹zōu 源yuán 兄xiōng 咱zán 润rùn 发fā旬xún 线xiàn 扯c hě拐guǎi 虐nüè 品pǐn 爱ài 尚shàng 约yuē劝quàn 梦mèng 留liú共gòng 撕sī否fǒu/pǐ案àn 框kuàng 旅lǚ搓cuō瘫tān 踹chuài 蛙wā踩cǎi 纫rèn 怀huái 襄xiāng 瓜guā俩liǎng 主zhǔ撒sā/sǎ鸣míng 准zhǔn 击jī穿chuān 嘣bēng 迟chí肥féi 均jūn窜cuàn 混hùn 销xiāo 偏piān 苔tái 醉zuì你nǐ擂léi 阔kuò 缺quē克kè 胞bāo 裆dāng 女nǚ苏sū子zǐ氢qīng 申shēn 门mén 光guāng 掐qiā度dù测试题-23读单音节字词100个背bèi 群qún 丢dūi挺tǐng 女nǚ捐juān 雄xíong 晕yūn 闯chǚa ng 拽zhuāi夸kuā 枪qiāng 却què 醋cù 晌shǎng 遭zāo 嘎gǎ稚zhì邢xíng 逆nì帘lía n 航háng 灰hūi实shí标biāo 聘pìng 而ér 妇fù 沫mò 绿lǜ涌yǒng 邹zōu 暗àn 踹chuài 人rén 贼zéi 雌cí鹅é 摊tān 沓tà 槛lán 犁lí球qùi 酿niàng 信xìng 书shū天tiān 哼hēng 杂zá 灭miè 替tì抓zhuā猿yuán 寡guǎ筒tǒng 昏hūn 翁wēng荒huāng 绝jué润rùn 隋suí坐zuò 篡cuàn 趁chèn 钩gōu 诱yòu 逮dǎi 饶ráo 散sǎn 栋dòng 发fā惹rě 开kāi 夹jiā 凋diāo 赛sài 煤méi 污wū 爱ài 关guān 尊zūn 选xuǎn 捶chuí说shuō 卸xiè 坡pō 往wǎng 剖pōu 尿niào 俩liǎng 闷mèn 蚌bàng 叩kòu 方fāng 郁yù 胞bāo 滥làn 琼qióng 军jūn 棚péng测试题-24读单音节字词100个茶chá 惹rě窒zhì拜bài 肋lèi 否fǒu 略lüè 返fǎn 群qún 焚fén 绑bǎng 蒸zhēng 屉tì颊jiá 灭miè 镖biāo丢diū电diàn 濒bīn 酿niàng 铃líng 毒dú 瓜guā拔bá 拽zhuài 刽guì短duǎn 穗suì尊zūn 幢chuáng 弓gōng 女nǚ穷qióng 虐nüè 捐juān 雌cí俊jùn 凶xiōng 窘jiǒng 沙shā择zé 日rì牌pái 黑hēi 苟gǒu 涵hán 根gēn 旁páng 乘chéng 忆yì掐qiā掖yè 瞟piǎo 有yǒu 甜tián 贫pín 良liáng 颈j ǐng 凸tū垮kuǎ叵pǒ踹chuài 傀kuǐ湍tuān 闻wén 疮chuāng红hóng 旅lǚ权quán 啊ā恻cè 买mǎi 嘈cáo 抠kōu 栈zhàn 啃kěn 仿fǎng 圣shèng 辖xiá 苗miáo 演yǎn 泯mǐn 湘xiāng澡zǎo 努nǔ划huá 锁suǒ暖nuǎn 双shuāng 松sōng 余yú悬xuán 紫zǐ傲ào 悔huǐ二èr 训xùn 粤yuè饶ráo 青qīng测试题-25读单音节字词100个胞bāo 雄xióng 潘pān撒sā奔bēn 二èr 掖yè 克kè 伐fá 音yīn沓tà羊yáng 剜wān 非fēi 她tā鹤hè 质zhì叉chā逮dài 枚méi 槛jiàn 扯chě雌cí坡pō佟tóng 矿kuàng 绿lǜ关guān 决jué 犬quǎn 熏xūn 软ruǎn 谁shuí揣chuǎi 啄zhuó 捆kǔn 拐guǎi 负fù慌huāng 拼pīn量liáng 孔kǒng 挑tiāo 敌dí谋móu 苔tái 申shēn 增zēng 耍shuǎ处chǔ薛xuē红hóng 卷juàn 略lüè 举jǔ褪tùn 佳jiā选xuǎn 住zhù 蛋dàn 抓zhuā邹zōu天tiān跌diē撇piē凑còu 鸟niǎo 农nóng 钙gài 镖biāo 梯tī宁níng 习xí尚shàng 绷bēng 摔shuāi 穷qióng 军jūn 寺sì怎zěn 瞒mán 绑bǎng 折zhē纫rèn 尼ní听tīng 混hùn 腮sāi 槽cáo 葬zàng 池chí掐qiā膻shān 轴zhóu 鬼guǐ流liú 念niàn 丢diū捆kǔn 漱shù测试题-26读单音节字词100个碑bēi 蚌bàng 别bié 镖biāo 扁biǎn 潘pān膀bǎng 披pī偏piān 品pǐn 迷mí灭miè 秒miǎo 免miǎn 名míng 费fèi 坟fén 防fáng 蜂fēng 达dá 逮dài 吊diào 丢diū吨dūn 塌tā瘫tān 铁tiě跎tuó 童tóng 您nín 宁níng 奴nú 农nóng 虐nüè 俩liǎng 亮liàng 领lǐng 卵luǎn 略lüè 给gěi 刮guā馆guǎn 广guǎng 课kè 开kāi 槛jiàn 垮kuǎ快kuài 耗hào 花huā坏huài 晃huǎng 斤jīn 奖jiǎng 决jué 卷juàn 俊jùn 球qiú 蛆qū尖jiān 群qún 穷qióng 修xiū徐xú 癣xuǎn 旬xún 雄xióng 志zhì绉zhòu 枕zhěn 浊zhuó 池chí仇chóu 踹chuài 吹chuī社shè 沈shěn 闩shuān 舜shùn 惹rě揉róu 乳rǔ弱ruò 子zǐ灶zào 增zēng 醉zuì财cái 操cāo 蹭cèng 催cuī色sè 苏sū孙sūn宋sòng 压yā养yǎng 旺wàng 御yù 涌yǒng测试题-27读单音节字词100个菌jūn 觉jué 铝lǚ气qì暂zàn 免miǎn 穴xué 抡lūn 熔róng 否fǒu 翁wēng 赠zèng 捅tǒng 塘táng 捏niē杠gàng 刁diāo挪nuó谱pǔ冒mào 肺fèi 放fàng 友yǒu 此cǐ勒lè 胸xiōng 娘niáng 催cuī牵qiān 哑yǎ枣zǎo 掌zhǎng 洞dòng 太tài 格gé 邪xié 蝉chán 兵bīng 刷shuā佛fó 摔shuāi圈quān窗chuāng吹chuī癣xuǎn 穷qióng 碑bēi 许xǔ透tòu 嘣bēng 岛dǎo 行xíng 化huà 镖biāo 国guó马mǎ册cè 黄huáng 判pàn 啪pā暖nuǎn 抨pēng糙cāo 假jiǎ换huàn 隋suí纫rèn 俩liǎng 揣chuǎi 名míng 邹zōu 解jiě宽kuān 讲jiǎng 朱zhū桥qiáo 里lǐ孙sūn染rǎn 沓tà 软ruǎn 靠kào 司sī砍kǎn 砣tuó 给gěi 郓yùn 浊zhuó 浙zhè 舜shùn 漱shù 荫yìn 逮dài 粟sù 痣zhì枕zhěn 裨bì临lín 牛niú 闩shuān测试题-28读单音节字词100个挨āi岸àn 恩ēn 压yā秧yāng 挽wǎn 往wǎng 于yú 员yuán 恽yùn 把bǎ猫māo 百bǎi 眯mī胞bāo免miǎn 邦bāng 泯mǐn 柄bǐng 啪pā泊bó 漂piāo 菲fēi 聘pìn 否f ǒu 颇pō焚fén 烽fēng 二èr 梯tī跌diē舔tiǎn 凋diāo帖tiè 丢diū太tài 堆duī嫩nèn 您nín 凉liáng 牛niú脸liǎn 狞níng 聊liáo 块kuài 劣liè 沽gū肋lè i 跨kuà 瑰guī扛káng 翁wēng 渴kě即jí恰qià 吓xià 指zhǐ扯chě识shí惹rě琥hǔ奖jiǎng 泅qiú 醒xǐng 栈zhàn 揣chuǎi 售shòu 扔rēng 划huá 绝jué 渠qú 薛xuē抓zhuā喘chuǎn 晌shǎng 若ruò 券quàn 淮huái 俊jùn 琼qióng 凶xiōng 椎zhuī冲chōng 霜shuāng 润rùn 紫zǐ洒sǎ此cǐ贼zéi 凑còu 腮sāi舱cāng 缩suō灶zào 颂sòng 粗cū嘴zuǐ更gēng 寸cùn 杆gān/gǎn测试题-29读单音节字词100个播bō们mén 挑tiāo 量liáng 合hé 秦qín 宣xuān揣chuǎi 软ruǎn 涩sè 面miàn 憋biē黑hēi 砣tuó 司sī乱luàn 蛆qū凶xiōng 床chuáng 润rùn 损sǔn 裆dāng 扁biǎn 肥féi 褪tùn 高gāo很hěn 权quán 褶zhě扒bā泼pō否fǒu 蝻nǎn 耕gēng 慌huāng 群qún 痣zhì笙shēng 宰zǎi 宋sòng 鲵ní纺fǎng 广guǎng 排pái 枕zhěn 贰èr 钻zuān 救jiù 穷qióng 榻tà 嘭pēng 纽niǔ邹zōu 铐kào 金jīn 彼bǐ刺cì捉zhuō刷shuā幼yòu 虐nüè 看kàn 瞟piǎo 得dé 霞xiá 讲jiǎng 甩shuǎi 促cù 腌yān 追zhuī栓shuān应yīng 剧jù平píng 到dào 跨kuà 栋dòng 俩liǎng 催cuī相xiāng卖mài 跌diē列liè 阔kuò 掘jué 冥míng 池chí顺shùn 翁wēng 存cún 题tí某mǒu 块kuài 临lín 蝉chán 啮niè 徐xú 乳rǔ撒sā恽yùn测试题-30读单音节字词100个碑bēi 潘pān 发fā逮dài 蹄tí您nín 槛jiàn 该gāi 克kè 行xíng 就jiù掐qiā萧xiāo 折zhē处chǔ申shēn 日rì邹zōu 擦cā色sè 癌ái 撒sā藏cáng 紫zǐ纫rèn 漱shù 揣chu ǎi 赵zhào 镶xiāng求qiú 浸jìn 鹤hè 铐kào 刮guā俩liǎng 挪nuó 舔tiǎn 岛d ǎo 废fèi 酶méi 匹pǐ蚌bàng 篇piān谋móu 粉fěn 等děng图tú 农nóng 辆liàng 滚gǔn 亏kuī划huá 讲jiǎng 轻qīng 宣xuān 郑zhèng 疮chuāng 耍shuǎ若ruò 怎zěn窜cuàn 寺sì欧ōu散sàn 曾zēng 润rùn 浊zhuó 旬xún 权quán 剧jù 怀huái 逛guàng 乱luàn 女nǚ褪tùn 拢lǒng 丢diū灭miè 品pǐn 别bié 凭píng 绿lǜ免miǎn 定dìng 童tóng 虐nüè 晕yùn 略lüè 绝jué 群qún 雄xióng 用yòng 镖biāo 免miǎn 卷juàn 穷qióng 鸣míng 晃huǎng 损sǔn 转zhuǎn测试题-31读单音节字词100个宣xuān 女nǚ绝jué 浙zhè 区qū寻xú n 沈shěn 刮guā颊jiá 幢chuáng 懂dǒng 作zuò 解jiě镖biāo 絮xù 抽chōu 匹pǐ由yóu 电diàn 盯dīng 锁suǒ蹭cèng 纺fǎng 舱cāng 尺chǐ副fù 吴wú 脑nǎo 邹zōu 克kè 相xiāng涩sè 军jūn 雄xióng 拐guǎi 而ér 略lüè 抓zhuā回huí字zì潘pān踹chuài 胞bāo逮dài 姚yáo 宵xiāo 赵zhào 铡zhá 榻tà 撒sā纫rèn 存cún 扎zā流liú 灭miè 您nín 穷qióng 头tóu 费fèi 扔rēng 行xíng 篇piān 俩liǎng 滚gǔn 煤méi 奖jiǎng 岁suì歌gē绕rào 海hǎi 奴nú 水shuǐ广guǎng 葱cōng 券quàn 奔bēn封fēng 凸tū两liǎng 容róng 品pǐn 憋biē免miǎn 勤qín 利lì囊náng 啪pā患huàn 阔kuò 沤òu 财cái 拨bō纯chún 鸣míng 裆dāng 槛jiàn 扇shàn 屉tì餐cān 钻zuān测试题-32读单音节字词100个怨yuàn 短duǎn 仍réng 黑hēi 坐zuò 捐juān 怀huái 否fǒu 钢gāng 付fù 瘸qué 枕zhěn 而ér 邹zōu 聘pìn 耍shuǎ蚌bàng 揣chuǎi 爷yé 拢lǒng 碑bēi 愁chóu 酿niàng 垮kuǎ灭miè 瓶píng 开kāi 处chǔ饶ráo 恩ēn 末mò 滚gǔn 鸣míng 萧xiāo 紫zǐ铐kào 晕yùn 彼bǐ润rùn 佟tóng 剜wān 秒miǎo 痣zhì穷qióng 丢diū赛sài 举jǔ停tíng 肉ròu 催cuī凡fán 弩nǔ膻shān 贷dài 挡dǎng 铡zhá 翁wēng扁biǎn 虐nüè 习xí乱luàn 坡pō体tǐ从cóng 霜shuāng 略lüè 笋sǔn 秦qín 凹āo 褪tùn 量liáng 甲jiǎ篇piān 捺nà 甩shuǎi 湖hú 睁zhēng旬xún 闷mèn 久jiǔ挠náo 酸suān 妾qiè 光guāng 隋suí许xǔ俏qiào 搓cuō克kè 舔tiǎn 食shí窗chuāng 俩liǎng 雄xióng 刺cì君jūn 肥féi 鹤hè 饮yǐn 瞥piē测试题-33读单音节字词100个发fā卡qiǎ值zhí大dà 喝hē侧cè 而ér 含hán 是shì紫zǐ车chē埋mái 彩cǎi 非fēi 袍páo 寺sì抽chōu北běi赛sài 饶ráo 奏zòu 艘sōu 稿gǎo 难nán 暂zàn 真zhēn 残cán 闪shǎn 葬zàng 常cháng 根gēn 草cǎo 正zhèng 忍rěn 航háng 披pī逢féng 蜜mì起qǐ漂piāo灭miè誊téng 俩liǎng 丢diū名míng 修xiū聂niè 也yě掂diān 假ji ǎ印yìn 福fú 新xīn表biǎo 胡hú 酿niàng 瓜guā九jiǔ熟shú舵duò 潦lǎo 抓zhuā怀huái 怪guài 挖wā艇tǐng 扁biǎn 块kuài 船chuán 税shuì团tuán 拨bō奖jiǎng 纯chún 锐ruì坡pō妥tuǒ岁suì狂kuáng 酸suān准zhǔn 同tóng 翁wēng 困kùn 捐juān 广guǎng 浪làng 拢lǒng 徐xú 圈quān 撞zhuàng 女nǚ觉jué 熏xūn 群qún 动dòng 铝lǚ兄xiōng 略lüè 穷qióng测试题-34读单音节字词100个洗xǐ蝻nǎn 都dū熟shú 卡qiǎ瘫tān肥féi 碑bēi 没méi 蚌bàng 瞟piǎo 鹤hè 称chēng 褶zhě溜liū掐qiā沓tà 此cǐ国guó 划huá组zǔ俊jùn 群qún 童tóng 分fēn 命mìng 摸mō论lùn 偶ǒu 许xǔ秦qín 减jiǎn 鳃sāi 饿è 啪pā福fú 挑tiāo 困kùn 冤yuān罪zuì株zhū洗xǐ早zǎo 菜cài 饶ráo 隋suí环huán 捐juān 穴xué 陆lù 铐kào 紫zǐ而ér 扔rēng耍shuǎ蛆qū熊xióng 病bìng 皮pí多duō量liáng 妾qiè 燃rán 邹zōu 此cǐ央yāng蒜suàn 给gěi 纺fǎng 慌huāng 穷qióng 俊jùn 葱cōng常cháng 摔shuāi 翁wēng狂kuáng 蹦bèng 蒙mēng 略lüè 谁shuí置zhì涩sè偶ǒu 正zhèng 嫁jià 踹chuài 铁tiě暖nuǎn 坡pō怪guài 吃chī建jiàn 肥féi 下xià 斤jīn广guǎng 习xí纫rèn 纽niǔ测试题-35读单音节字词100个嘎gā拍pāi舟zhōu纲gāng 押yā帘lián 柠níng 拽zhuài 慌huāng 泉quán 洒sǎ开kāi 揉róu 昂áng 别bié 件jiàn 迎yíng 揣chuǎi 脓nóng 群qún 吓xià 债zhài 产chǎn 檬méng 跌diē宾bīn 铺pū锐ruì综zōng迅xùn 扯chě柴chái 删shān 风fēng 夜yè 心xīn属shǔ最zuì从cóng 源yuán 舍shè 赔péi 嫩nèn 坑kēng 条tiáo 饮yǐn 塑sù 断duàn 女nǚ窘jiǒng 恶è 费fèi 狠hěn 笔bǐ脚jiǎo 亮liàng 垮kuǎ暖nuǎn 绿lǜ琼qióng 池chí给gěi怎zěn 坯pī要yào 象xiàng 画huà 窜cuàn 虐nüè 凶xiōng 狮shī贸mào 方fāng邸dǐ牛niú 洋yáng 博bó 顿dùn 掠lüè 思sī烤kǎo 浪làng 下xià 六liù 艇tǐng 某mǒu 托tuō润rùn 匡kuāng 缺quē捐juān 俩liǎng 您nín 惨cǎn 肯kěn 筒tǒng 肿zhǒng 疼téng 平píng 仍réng测试题-36读单音节字词100个胞bāo 浊zhuó 沓tà 揣chuǎi 蚌bàng 逮dài 鹤hè 槛jiàn 碑bēi邹zōu 铐kào 纽niǔ偶ǒu 勺sháo 潘pān 俏qiào 纫rèn 涩sè 晌shǎng 拈niān克kè 虐nüè 瞟piǎo 秦qín 润rùn 挠náo 嘭pēng 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16610.16638/ki.1671-7988.2020.12.051WorldSID 50th假人整体式和分体式胸部垫片的比对分析朱晓勇，陈亚依，丁冉冉，周鹏（中汽研汽车检验中心（宁波）有限公司，浙江 宁波 315336）摘 要：为深入了解WorldSID 50th 假人整体式和分体式胸部垫片结构性能的差异，在相同冲击工况下分别对配备两种垫片的WorldSID 50th 假人的胸部和腹部进行冲击，分析假人各部位的响应特性。

结果表明：在相同冲击条件下，配备分体式垫片的假人所受到的冲击力较小，所产生的胸腹部位移较大，使假人的受力响应更集中于受力的区域附近，力及加速度的传递方面会有所削弱，但总体的差异不大。

此研究中针对WorldSID 50th 假人整体式和分体式垫片在相同冲击工况下的研究和分析，为后期WorldSID 50th 假人胸部垫片的改良和选择提供了基础，具有一定的指导意义。

关键词：汽车安全；WorldSID 50th；假人标定；胸部垫片中图分类号：U467 文献标识码：A 文章编号：1671-7988(2020)12-166-04Comparative Analysis of Split and 1-Piece Thorax Pad of WorldSID 50th DummyZhu Xiaoyong, Chen Yayi, Ding Ranran, Zhou Peng( CA TARC Automotive Test Center (Ningbo) Co., Ltd., Zhejiang Ningbo 315336 )Abstract: In order to deeply understand the difference of structural performance between 1-piece pad and split pad of the WorldSID 50th dummy, the thorax of the WorldSID 50th dummy equipped with two kinds of pads were impacted respectively under the same impact condition, and the response characteristics of various parts of the dummy were analyzed. The results show that under the same impact condition, the dummy equipped with 1-piecepad receives less impact force and produces larger thorax and abdomendisplacement, which makes the stress response of the dummy more concentrated in the vicinity of the stress area and weakens the transmission of force and acceleration, but the overall difference is not big. The research and analysis of the 1-piece pad and split pad of the WorldSID 50th dummy under the same impact conditions provide a basis for the laterimprovement and selection of it, and have some guiding significance. Keywords: Car Safety; WorldSID 50th ; Dummy Calibration; Thorax Pad CLC NO.: U467 Document Code: A Article ID: 1671-7988(2020)12-166-04前言1 研究背景介绍1.1 WorldSID 50th假人的研究意义在碰撞试验中，碰撞假人是一件重要且易损的工具。