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大眾汽車·奧迪汽車技術詳解及常見故障精析

為了解決EA888的問題，作者凌凱汽車技術編寫組 這樣論述：

本書主要內容為一汽大眾、奧迪汽車的發動機、底盤、變速器以及車身電氣等系統的新技術剖析、常見故障和技術通報。在各部分開篇介紹大眾、奧迪汽車各系統技術特點，如發動機部分先詳細介紹兩車系目前裝配的EA211系列（三缸、四缸1.0T、1.2T、1.4T、1.5L和1.6L）、EA888系列（1.8T、2.0T）、EA837系列（3.0TSI）、EA839系列（3.0TSI）發動機的機械結構、特殊結構，以及發動機的共性問題，再對各車型發動機常見故障案例分析、排除進行詳細介紹。底盤首先介紹大眾、奧迪汽車所有手動變速器、雙離合器變速器（前置前驅型DQ200、DQ250、DQ380、DQ500，橫置后驅型DL

382、DL501）等變速器異同點及特點，再對各車型變速器故障案例分析、排除方法進行詳細介紹。本書資料新（所選年款均為主流車型較新年款，正處於維修期或即將處於維修期，同時兼顧目前最新款）、內容全（涵蓋目前大眾全部發動機、變速器、底盤等資料）、維修參考價值高。 本書不僅適合廣大維修工閱讀使用，還適合各類汽車院校針對大眾車型培訓使用，同樣適用於汽車愛好者了解大眾汽車構造使用。

EA888進入發燒排行的影片

非接觸式量測於細胞膜量測通透性研究

為了解決EA888的問題，作者吳宗霖 這樣論述：

細胞膜對於水的通透性 (Cell-membrane permeability to water) 與細胞膜對於抗凍劑的通透性 (Cell-membrane permeability to cryoprotective agents) 是生物樣本進行最佳化冷凍保存 (Cryopreservation) 的關鍵資訊。此項研究開發了一種微渦流 (Mirco-vortex) 系統，利用微流體 (Microfluidics) 通道的擴展區域在低雷諾數下，被動形成的流體動力 (Hydrodynamic) 將感興趣的細胞捕獲並且維持在渦流中。被捕獲的細胞會保持懸浮狀態 (Suspension)，並隨著局部

渦流的流線移動，因此，細胞被捕獲在該系統中避免了物理接觸 (Physical contact) 的情況發生，進一步支持細胞膜通透性的理論中利用細胞體積的圖形計算球型體積時，將其假設為100% 球形並且求出細胞膜活性表面積。因此，透過高速攝影中的即時細胞辨識系統，細胞膜通透性可以通過影像可視化追蹤單顆細胞並且取得其二維圖形，透過架設瞬態的滲透性梯度 (Osmotic gradient) 在細胞內 (Intracellular) 與細胞外 (Extracellular) 環境，計算響應細胞體積變化。本研究以急性 T 細胞淋巴瘤細胞系 (Jurkat) 為模型，來檢查新採用的微渦流技術，結果表明其數

值略高於現有技術。我們的結果呈現高於使用基於物理接觸的細胞捕獲裝置，顯示基於非接觸式的量測顯著影響細胞膜通透性的活性表面積，提供一個提高對於細胞膜通透性量測準確性的新方法。

汽車發動機維修入門到精通全圖解

為了解決EA888的問題，作者於海東（主編） 這樣論述：

本書從發動機拆裝工具及發動機基本組成入手，再到發動機的基本保養、就車維修以及簡單器件更換，最后介紹發動機大修及各系統故障檢查及排除。發動機基本保養、就車維修以及簡單器件更換部分以目前市場上保有量較大的大眾EA888發動機為例，考慮到發動機大修方面初學人員可能沒有條件進行此發動機的拆裝，所以將配氣機構、曲柄連桿拆裝以及點火系統、燃油供給系統更換為更容易接觸到的國產自主車型發動機的相關部件。本書語言精練，以圖為主，內容豐富，實用性強，既可供初學汽車維修技術的人員使用，也可供廣大汽車愛好者、駕駛人員以及大中專院校有關專業的師生閱讀和參考。

探討在神經退化性疾病中調控核醣核酸結合蛋白MBNL2表現之機轉

為了解決EA888的問題，作者王李馨 這樣論述：

中文摘要 iAbstract iiContents iiiIntroduction 1Myotonic dystrophy type 1 (DM1) 1Cerebral involvement of adult-onset DM1 2Genetic basis of DM1 4Molecular mechanism in DM1 4Mouse models of DM1 with expression of CUG repeats 6RNA-binding protein: Muscleblind-like (MBNL) family

8MBNL1 and MBNL2 knockout mice 9Calcium-dependent cysteine protease: Calpain 11Calpain-1 and -2 11Calpain-1 and -2 deficient mice 12Calpain-1 and -2 in neurodegeneration 13Alzheimer’s disease (AD) 14Disease stages of AD 14Clinical presentations of AD 15Brain atrophy of AD

15Two pathological hallmarks of AD 16The aims of the study 20Materials and methods 211. Animals 212. Primary hippocampal neuron culture, drug treatment, virus infection and transfection 213. Cell culture and transient transfection 234. Total protein extraction and sub

cellular fractionation 245. Immunoprecipitation (IP) 256. Immunoblotting analysis 257. RNA preparation, RT-PCR and splicing analysis 268. Immunofluorescence staining and immunohistochemistry 279. Quantification of fluorescent images of brain sections 2910. Quantif

ication of fluorescent images of neurons 3011. Antibodies 3012. Plasmids 3113. Statistical analysis 31Results 331. Characterize the role of MBNL2 in neuronal maturation1.1. MBNL2 is expressed postnatally and increased as neuronal maturation 331.2. MBNL2 expression

is required for promoting adult pattern of RNA processingand neuronal differentiation 342. Determine how neurodegenerative conditions reduce MBNL2 expression2.1. Glutamate-induced excitotoxicity reduces MBNL2 protein expression viaNMDAR activation 352.2. NMDAR-mediated Calpain-2 acti

vation causes MBNL2 protein degradation 362.3. Calcium-dependent nuclear translocation of CAPN2 is associated with reducedMBNL2 expression 382.4. Dysregulated calcium homeostasis reduces MBNL2 expression 392.5. Enhanced nuclear translocation of CAPN2 occurs in the EpA960/CamKII-Cre

brain 402.6. Enhanced nuclear translocation of CAPN2 in neurodegeneration recapitulates thefetal developmental pattern 413. Explore the possibility of the reduced MBNL2 expression associated re-induced fetalpattern of RNA processing as a common feature among neurodegenerative disorders3.

1. Enhanced nuclear translocation of CAPN2, reduced MBNL2 expression and associated aberrant MBNL2-regulated alternative splicing in the degenerative brains of AD 41Discussion 44Perspective 48References 49List of figuresFigure 1. MBNL2 is expressed postnatally and increased with bra

in maturation 64Figure 2. MBNL2 is expressed in the more differentiated cells during hippocampusmaturation 65Figure 3. MBNL2 is expressed ubiquitously in the adult mouse brain 66Figure 4. MBNL2 is expressed in the neurons, oligodendrocytes and astrocytes 67Figure 5. The knockdown

efficiency of MBNL2 shRNAs in cultured neurons 68Figure 6. The alternative splicing and polyadenylation of MBNL2 targets show a fetal to adult transition during neuronal differentiation 70Figure 7. MBNL2 depletion disrupts the developmental RNA processing transition in cultured neurons

71Figure 8. MBNL2 depletion impairs dendrite maturation in cultured neurons 72Figure 9. Glutamate treatment induces excitotoxicity in mature cultured neurons showing condensed nucleus 74Figure 10. Glutamate-induced excitotoxicity reduces MBNL2 protein level in mature cultured neurons 75

Figure 11. Glutamate reduces MBNL2 level via NMDAR activation in cultured neurons 77Figure 12. NMDAR-mediated MBNL2 reduction is calcium dependent 78Figure 13. The alternative splicing and polyadenylation of MBNL2 targets are disrupted in neurons treated with glutamate or NMDA 79Figure 14.

MBNL2 mRNA level is unchanged in cultured neurons treated with glutamate or NMDA 81Figure 15. MBNL2 protein is stable in the neurons 82Figure 16. NMDAR signaling-mediated MBNL2 reduction requires calpain activity incultured neurons 83Figure 17. Protein expression of CAPN1 and CAPN2 are alte

red in NMDA-treatedneurons 84Figure 18. MBNL2 binds to both CAPN1 and CAPN22 in HEK293 cells 85Figure 19. Knockdown efficiency of CAPN1 or CAPN2 shRNAs in neurons 86Figure 20. NMDAR-mediated calpain-2 activation causes MBNL2 degradation inneurons 87Figure 21. Depletion of CAPN2 preserves

MBNL2-regulated alternative splicing andpolyadenylation in neurons upon NMDA treatment 88Figure 22. CAPN2 is predominantly expressed in the cytoplasm of mature neurons 90Figure 23. NMDA treatment induces the nuclear translocation of CAPN2 in neurons 91Figure 24. NMDAR-mediated MBNL2 reduct

ion requires calpain-2 expression in thenucleus and cytoplasm of neurons 92Figure 25. NMDA-induced nuclear translocation of CAPN2 requires calcium 93Figure 26. Nuclear translocation of CAPN2 involves in MBNL2 degradation 94Figure 27. Dysregulated calcium homeostasis induces the nuclear tran

slocation of CAPN2 and reduced MBNL2 expression in neurons 95Figure 28. CAPN2 depletion preserves MBNL2 expression in the neurons with dysregulated calcium homeostasis 96Figure 29. Effect of CAPN2 depletion on the RNA processing pattern of MBNL2 targets in A23187-treated neurons 97Figure 30

. CAPN2 nuclear translocation is occurred in the EpA960/CaMKII-Cre mouse brains 98Figure 31. Nuclear-to-cytoplasmic distribution of CAPN2 during neuronal differentiation 99Figure 32. Nuclear translocation of CAPN2 occurs in the APP/PS1 and THY-Tau22brains 100Figure 33. Reduced MBNL2 express

ion in the APP/PS1 and THY-Tau22 brains 101Figure 34. Aberrant MBNL2-regulated alternative splicing in the APP/PS1 and THY-Tau22 brains 102