{"product_id":"cell-biology-protocols-hardback-9780470847589","title":"Cell Biology Protocols (Hardback) 9780470847589","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eCell Biology Protocols\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eJ. Robin Harris (Edited by), R Harris (Author), John M. Graham (Edited by), David Rickwood (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780470847589, Wiley\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 27 January 2006\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e432 pages\u003cbr\u003e24.4 x 19.6 x 3 cm, 1.021 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\"A valuable possession for every cell biologist’s library.\" (\u003ci\u003eBSCB Newsletter\u003c\/i\u003e, September 2006)\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eAs a modern composite scientific discipline, Cell Biology has expanded and moved forward rapidly in recent years. Cell Biologists now require a wide range of techniques, including those of analytical biochemistry and microscopy in all its diverse forms. These are often used alongside the techniques of molecular biology and molecular genetics. This book contains numerous useful protocols, covering light and electron microscopy, cell culture, cell separation, subcellular fractionation, organelle and membrane isolation, and the use of in vitro reassembly systems in Cell Biology. Many of these protocols feature helpful notes and safety information for practical application. The format favours easy use at the bench with space for notes and important safety information. An appendix contains essential analytical information that will prove invaluable to those working on all aspects of cell biology.\u003cbr\u003e \u003cbr\u003e This book will be of interest to students and more experienced cell biologists, as well as molecular biologists and those working in genomics and proteomics who are looking for cellular techniques to validate their findings within intact cells.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePreface xi\u003c\/p\u003e \u003cp\u003eList of Contributors xiii\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Basic Light Microscopy 1\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eMinnie O’Farrell\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 1\u003c\/p\u003e \u003cp\u003eKey components of the compound microscope 2\u003c\/p\u003e \u003cp\u003eTechniques of microscopy 6\u003c\/p\u003e \u003cp\u003eProtocols\u003c\/p\u003e \u003cp\u003e1.1 Setting up the microscope for bright field microscopy 7\u003c\/p\u003e \u003cp\u003e1.2 Setting K¨ohler illumination 8\u003c\/p\u003e \u003cp\u003e1.3 Focusing procedure 9\u003c\/p\u003e \u003cp\u003e1.4 Setting up the microscope for phase contrast microscopy 11\u003c\/p\u003e \u003cp\u003e1.5 Setting up the microscope for epifluorescence 14\u003c\/p\u003e \u003cp\u003e1.6 Poly-L-lysine coating 18\u003c\/p\u003e \u003cp\u003eReferences 19\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Basic Electron Microscopy 21\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eJ. Robin Harris\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 21\u003c\/p\u003e \u003cp\u003eEM methods available 22\u003c\/p\u003e \u003cp\u003eProtocols\u003c\/p\u003e \u003cp\u003e2.1 Preparation of carbon-formvar, continuous carbon and holey carbon support films 25\u003c\/p\u003e \u003cp\u003e2.2 The ‘droplet’ negative staining procedure (using continuous carbon, formvar–carbon and holey carbon support films) 27\u003c\/p\u003e \u003cp\u003e2.3 Immunonegative staining 29\u003c\/p\u003e \u003cp\u003e2.4 The negative staining-carbon film technique: cell and organelle cleavage 31\u003c\/p\u003e \u003cp\u003e2.5 Preparation of unstained and negatively stained vitrified specimens 33\u003c\/p\u003e \u003cp\u003e2.6 Metal shadowing of biological specimens 35\u003c\/p\u003e \u003cp\u003e2.7 A routine schedule for tissue processing and resin embedding 37\u003c\/p\u003e \u003cp\u003e2.8 Agarose encapsulation for cell and organelle suspensions 39\u003c\/p\u003e \u003cp\u003e2.9 Routine staining of thin sections for electron microscopy 40\u003c\/p\u003e \u003cp\u003e2.10 Post-embedding indirect immunolabelling of thin sections 42\u003c\/p\u003e \u003cp\u003e2.11 Imaging the nuclear matrix and cytoskeleton by embedment-free electron microscopy 44\u003cbr\u003e\u003ci\u003eJeffrey A. Nickerson and Jean Underwood\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eReferences 50\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Cell Culture 51\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eAnne Wilson and John Graham\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eCells: isolation and analysis 51\u003cbr\u003e\u003ci\u003eAnne Wilson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eMechanical disaggregation of tissue 52\u003c\/p\u003e \u003cp\u003eProtocols\u003c\/p\u003e \u003cp\u003e3.1 Tissue disaggregation by mechanical mincing or chopping 54\u003c\/p\u003e \u003cp\u003e3.2 Tissue disaggregation by warm trypsinization 56\u003c\/p\u003e \u003cp\u003e3.3 Cold trypsinization 58\u003c\/p\u003e \u003cp\u003e3.4 Disaggregation using collagenase or dispase 60\u003cbr\u003e\u003ci\u003eAnne Wilson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.5 Recovery of cells from effusions 63\u003cbr\u003e\u003ci\u003eAnne Wilson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.6 Removal of red blood cells by snap lysis 64\u003c\/p\u003e \u003cp\u003e3.7 Removal of red blood cells and dead cells using isopycnic centrifugation 65\u003cbr\u003e\u003ci\u003eAnne Wilson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.8 Quantitation of cell counts and viability 67\u003cbr\u003e\u003ci\u003eAnne Wilson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.9 Recovery of cells from monolayer cultures 71\u003cbr\u003e\u003ci\u003eAnne Wilson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.10 Freezing cells 74\u003c\/p\u003e \u003cp\u003e3.11 Thawing cells 76\u003cbr\u003e\u003ci\u003eJohn Graham\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.12 Purification of human PBMCs on a density barrier 80\u003c\/p\u003e \u003cp\u003e3.13 Purification of human PBMCs using a mixer technique 82\u003c\/p\u003e \u003cp\u003e3.14 Purification of human PBMCs using a barrier flotation technique 83\u003c\/p\u003e \u003cp\u003eReferences 84\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Isolation and Functional Analysis of Organelles 87\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eJohn Graham\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 88\u003c\/p\u003e \u003cp\u003eHomogenization 88\u003c\/p\u003e \u003cp\u003eDifferential centrifugation 90\u003c\/p\u003e \u003cp\u003eDensity gradient centrifugation 91\u003c\/p\u003e \u003cp\u003eNuclei and nuclear components 92\u003c\/p\u003e \u003cp\u003eMitochondria 93\u003c\/p\u003e \u003cp\u003eLysosomes 94\u003c\/p\u003e \u003cp\u003ePeroxisomes 94\u003c\/p\u003e \u003cp\u003eRough and smooth endoplasmic reticulum (ER) 95\u003c\/p\u003e \u003cp\u003eGolgi membranes 96\u003c\/p\u003e \u003cp\u003ePlasma membrane 96\u003c\/p\u003e \u003cp\u003eChloroplasts 97\u003c\/p\u003e \u003cp\u003eProtocols\u003c\/p\u003e \u003cp\u003e4.1 Isolation of nuclei from mammalian liver in an iodixanol gradient (with notes on cultured cells) 98\u003c\/p\u003e \u003cp\u003e4.2 Isolation of metaphase chromosomes 100\u003c\/p\u003e \u003cp\u003e4.3 Isolation of the nuclear envelope 102\u003c\/p\u003e \u003cp\u003e4.4 Nuclear pore complex isolation 104\u003cbr\u003e\u003ci\u003eJ. Robin Harris\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.5 Preparation of nuclear matrix 106\u003c\/p\u003e \u003cp\u003e4.6 Preparation of nucleoli 107\u003c\/p\u003e \u003cp\u003e4.7 Isolation of a heavy mitochondrial fraction from rat liver by differential centrifugation 108\u003c\/p\u003e \u003cp\u003e4.8 Preparation of a light mitochondrial fraction from tissues and cultured cells 110\u003c\/p\u003e \u003cp\u003e4.9 Purification of yeast mitochondria in a discontinuous Nycodenz\u003csup\u003e®\u003c\/sup\u003e gradient 112\u003c\/p\u003e \u003cp\u003e4.10 Purification of mitochondria from mammalian liver or cultured cells in a median-loaded discontinuous Nycodenz\u003csup\u003e®\u003c\/sup\u003e gradient 114\u003c\/p\u003e \u003cp\u003e4.11 Succinate–INT reductase assay 116\u003c\/p\u003e \u003cp\u003e4.12 Isolation of lysosomes in a discontinuous Nycodenz\u003csup\u003e®\u003c\/sup\u003e gradient 117\u003c\/p\u003e \u003cp\u003e4.13 β-Galactosidase (spectrophotometric assay) 119\u003c\/p\u003e \u003cp\u003e4.14 β-Galactosidase (fluorometric assay) 120\u003c\/p\u003e \u003cp\u003e4.15 Isolation of mammalian peroxisomes in an iodixanol gradient 121\u003c\/p\u003e \u003cp\u003e4.16 Catalase assay 123\u003c\/p\u003e \u003cp\u003e4.17 Analysis of major organelles in a preformed iodixanol gradient 124\u003c\/p\u003e \u003cp\u003e4.18 Separation of smooth and rough ER in preformed sucrose gradients 127\u003c\/p\u003e \u003cp\u003e4.19 Separation of smooth and rough ER in a self-generated iodixanol gradient 129\u003c\/p\u003e \u003cp\u003e4.20 NADPH-cytochrome c reductase assay 131\u003c\/p\u003e \u003cp\u003e4.21 Glucose-6-phosphatase assay 132\u003c\/p\u003e \u003cp\u003e4.22 RNA analysis 133\u003c\/p\u003e \u003cp\u003e4.23 Isolation of Golgi membranes from liver 134\u003c\/p\u003e \u003cp\u003e4.24 Assay of UDP-galactose galactosyl transferase 136\u003c\/p\u003e \u003cp\u003e4.25 Purification of human erythrocyte ‘ghosts’ 137\u003c\/p\u003e \u003cp\u003e4.26 Isolation of plasma membrane sheets from rat liver 139\u003c\/p\u003e \u003cp\u003e4.27 Assay for 5’-nucleotidase 141\u003c\/p\u003e \u003cp\u003e4.28 Assay for alkaline phosphodiesterase 143\u003c\/p\u003e \u003cp\u003e4.29 Assay for ouabain-sensitive Na\u003csup\u003e+\u003c\/sup\u003e\/K\u003csup\u003e+\u003c\/sup\u003e-ATPase 144\u003c\/p\u003e \u003cp\u003e4.30 Isolation of chloroplasts from green leaves or pea seedlings 145\u003c\/p\u003e \u003cp\u003e4.31 Measurement of chloroplast chlorophyll 147\u003c\/p\u003e \u003cp\u003e4.32 Assessment of chloroplast integrity 148\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Fractionation of Subcellular Membranes in Studies on Membrane Trafficking and Cell Signalling 153\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eJohn Graham\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 154\u003c\/p\u003e \u003cp\u003eMethods available 154\u003c\/p\u003e \u003cp\u003ePlasma membrane domains 155\u003c\/p\u003e \u003cp\u003eAnalysis of membrane compartments in the endoplasmic reticulum–Golgi–plasma membrane pathway 156\u003c\/p\u003e \u003cp\u003eSeparation of membrane vesicles from cytosolic proteins 157\u003c\/p\u003e \u003cp\u003eEndocytosis 158\u003c\/p\u003e \u003cp\u003eProtocols\u003c\/p\u003e \u003cp\u003e5.1 Separation of basolateral and bile canalicular plasma membrane domains from mammalian liver in sucrose gradients 160\u003c\/p\u003e \u003cp\u003e5.2 Isolation of rat liver sinusoidal domain using antibody-bound beads 162\u003c\/p\u003e \u003cp\u003e5.3 Fractionation of apical and basolateral domains from Caco-2 cells in a sucrose gradient 163\u003c\/p\u003e \u003cp\u003e5.4 Fractionation of apical and basolateral domains from MDCK cells in an iodixanol gradient 165\u003c\/p\u003e \u003cp\u003e5.5 Isolation of lipid rafts 167\u003c\/p\u003e \u003cp\u003e5.6 Isolation of caveolae 170\u003c\/p\u003e \u003cp\u003e5.7 Analysis of Golgi and ER subfractions from cultured cells using discontinuous sucrose–D\u003csub\u003e2\u003c\/sub\u003eO density gradients 172\u003c\/p\u003e \u003cp\u003e5.8 Analysis of Golgi, ER, ERGIC and other membrane compartments from cultured cells using continuous iodixanol density gradients 174\u003c\/p\u003e \u003cp\u003e5.9 Analysis of Golgi, ER, TGN and other membrane compartments in sedimentation velocity iodixanol density gradients (continuous or discontinuous) 177\u003c\/p\u003e \u003cp\u003e5.10 SDS–PAGE of membrane proteins 180\u003c\/p\u003e \u003cp\u003e5.11 Semi-dry blotting 182\u003c\/p\u003e \u003cp\u003e5.12 Detection of blotted proteins by enhanced chemiluminescence (ECL) 183\u003c\/p\u003e \u003cp\u003e5.13 Separation of membranes and cytosolic fractions from (a) mammalian cells and (b) bacteria 185\u003c\/p\u003e \u003cp\u003e5.14 Analysis of early and recycling endosomes in preformed iodixanol gradients; endocytosis of transferrin in transfected MDCK cells 188\u003c\/p\u003e \u003cp\u003e5.15 Analysis of clathrin-coated vesicle processing in self-generated iodixanol gradients; endocytosis of asialoglycoprotein by rat liver 191\u003c\/p\u003e \u003cp\u003e5.16 Polysucrose–Nycodenz\u003csup\u003e®\u003c\/sup\u003e gradients for the analysis of dense endosome–lysosome events in mammalian liver 194\u003c\/p\u003e \u003cp\u003eReferences 196\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 \u003ci\u003eIn Vitro \u003c\/i\u003eTechniques 201\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eEdited by J. Robin Harris\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 203\u003c\/p\u003e \u003cp\u003eProtocols\u003c\/p\u003e \u003cp\u003e\u003cb\u003eNuclear components\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e6.1 Nucleosome assembly coupled to DNA repair synthesis using a human cell free system 204\u003cbr\u003e\u003ci\u003eGenevi\u003c\/i\u003e\u003ci\u003eève Almouzni and Doris Kirschner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.2 Single labelling of nascent DNA with halogenated thymidine analogues 210\u003cbr\u003e\u003ci\u003eDaniela Dimitrova\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.3 Double labelling of DNA with different halogenated thymidine analogues 214\u003c\/p\u003e \u003cp\u003e6.4 Simultaneous immunostaining of proteins and halogen-dU-substituted DNA 217\u003c\/p\u003e \u003cp\u003e6.5 Uncovering the nuclear matrix in cultured cells 220\u003cbr\u003e\u003ci\u003eJeffrey A. Nickerson, Jean Underwood and Stefan Wagner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.6 Nuclear matrix–lamin interactions: \u003ci\u003ein vitro \u003c\/i\u003eblot overlay assay 228\u003cbr\u003e\u003ci\u003eBarbara Korbei and Roland Foisner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.7 Nuclear matrix–lamin interactions: \u003ci\u003ein vitro \u003c\/i\u003enuclear reassembly assay 230\u003c\/p\u003e \u003cp\u003e6.8 Preparation of \u003ci\u003eXenopus laevis \u003c\/i\u003eegg extracts and immunodepletion 234\u003cbr\u003e\u003ci\u003eTobias C. Walther\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.9 Nuclear assembly \u003ci\u003ein vitro \u003c\/i\u003eand immunofluorescence 237\u003cbr\u003e\u003ci\u003eMartin Hetzer\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.10 Nucleocytoplasmic transport measurements using isolated \u003ci\u003eXenopus \u003c\/i\u003eoocyte nuclei 240\u003cbr\u003e\u003ci\u003eReiner Peters\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.11 Transport measurements in microarrays of nuclear envelope patches by optical single transporter recording 244\u003cbr\u003e\u003ci\u003eReiner Peters\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eCells and membrane systems\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e6.12 Cell permeabilization with Streptolysin O 248\u003cbr\u003e\u003ci\u003eIvan Walev\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.13 Nanocapsules: a new vehicle for intracellular delivery of drugs 250\u003cbr\u003e\u003ci\u003eAnton I. P. M. de Kroon, Rutger W. H. M. Staffhorst, Ben de Kruijff and Koert N. J.Burger\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.14 A rapid screen for determination of the protective role of antioxidant proteins in yeast 255\u003cbr\u003e\u003ci\u003eLuis Eduardo Soares Netto\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.15 \u003ci\u003eIn vitro \u003c\/i\u003eassessment of neuronal apoptosis 259\u003cbr\u003e\u003ci\u003eEric Bertrand\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.16 The mitochondrial permeability transition: PT and Δѱm loss determined in cells or isolated mitochondria with confocal laser imaging 265\u003cbr\u003e\u003ci\u003eJudie B. Alimonti and Arnold H. Greenberg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.17 The mitochondrial permeability transition: measuring PT and Δѱm loss in isolated mitochondria with Rh123 in a fluorometer 268\u003cbr\u003e\u003ci\u003eJudie B. Alimonti and Arnold H. Greenberg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.18 The mitochondrial permeability transition: measuring PT and Δѱm loss in cells and isolated mitochondria on the FACS 270\u003cbr\u003e\u003ci\u003eJudie B. Alimonti and Arnold H. Greenberg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.19 Measuring cytochrome \u003ci\u003ec \u003c\/i\u003erelease in isolated mitochondria by Western blot analysis 271\u003cbr\u003e\u003ci\u003eJudie B. Alimonti and Arnold H. Greenberg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.20 Protein import into isolated mitochondria 272\u003cbr\u003e\u003ci\u003eJudie B. Alimonti and Arnold H. Greenberg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.21 Formation of ternary SNARE complexes \u003ci\u003ein vitro \u003c\/i\u003e274\u003cbr\u003e\u003ci\u003eJinnan Xiao, Anuradha Pradhan and Yuechueng Liu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.22 \u003ci\u003eIn vitro \u003c\/i\u003ereconstitution of liver endoplasmic reticulum 277\u003cbr\u003e\u003ci\u003eJacques Paiement and Robin Young\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.23 Asymmetric incorporation of glycolipids into membranes and detection of lipid flip-flop movement 280\u003cbr\u003e\u003ci\u003eFélix M. Go\u003c\/i\u003e\u003ci\u003eñi, Ana-Victoria Villar, F.-Xabier Contreras and Alicia Alonso\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.24 Purification of clathrin-coated vesicles from rat brains 286\u003cbr\u003e\u003ci\u003eBrian J. Peter and Ian G. Mills\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.25 Reconstitution of endocytic intermediates on a lipid monolayer 288\u003cbr\u003e\u003ci\u003eBrian J. Peter and Matthew K. Higgins\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.26 Golgi membrane tubule formation 293\u003cbr\u003e\u003ci\u003eWilliam J. Brown, K. Chambers and A. Doody\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.27 Tight junction assembly 296\u003cbr\u003e\u003ci\u003eC. Yan Cheng and Dolores D. Mruk\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.28 Reconstitution of the major light-harvesting chlorophyll \u003ci\u003ea\u003c\/i\u003e\/\u003ci\u003eb \u003c\/i\u003ecomplex into liposomes 300\u003cbr\u003e\u003ci\u003eChunhong Yang, Helmut Kirchhoff, Winfried Haase, Stephanie Boggasch and Harald Paulsen\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.29 Reconstitution of photosystem 2 into liposomes 305\u003cbr\u003e\u003ci\u003eJulie Benesova, Sven-T. Liffers and Matthias Rögner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.30 Golgi–vimentin interaction \u003ci\u003ein vitro \u003c\/i\u003eand \u003ci\u003ein vivo \u003c\/i\u003e307\u003cbr\u003e\u003ci\u003eYa-sheng Gao and Elizabeth Sztul\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eCytoskeletal and fibrillar systems\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e6.31 Microtubule peroxisome interaction 313\u003cbr\u003e\u003ci\u003eMeinolf Thiemann and H. Dariush Fahimi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.32 Detection of cytomatrix proteins by immunogold embedment-free electron microscopy 317\u003cbr\u003e\u003ci\u003eRobert Gniadecki and Barbara Gajkowska\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.33 Tubulin assembly induced by taxol and other microtubule assembly promoters 326\u003cbr\u003e\u003ci\u003eSusan L. Bane\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.34 Vimentin production, purification, assembly and study by EPR 331\u003cbr\u003e\u003ci\u003eJohn F. Hess, John C. Voss and Paul G. FitzGerald\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.35 Neurofilament assembly 337\u003cbr\u003e\u003ci\u003eShin-ichi Hisanaga and Takahiro Sasaki\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.36 α-Synuclein fibril formation induced by tubulin 342\u003cbr\u003e\u003ci\u003eKenji Uéda and Shin-ichi Hisanaga\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.37 Amyloid-β fibril formation \u003ci\u003ein vitro \u003c\/i\u003e345\u003cbr\u003e\u003ci\u003eJ. Robin Harris\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.38 Soluble Aβ\u003csub\u003e1–42\u003c\/sub\u003e peptide induces tau hyperphosphorylation \u003ci\u003ein vitro \u003c\/i\u003e348\u003cbr\u003e\u003ci\u003eTerrence Town and Jun Tan\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.39 Anti-sense peptides 353\u003cbr\u003e\u003ci\u003eNathaniel G. N. Milton\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.40 Interactions between amyloid-β and enzymes 359\u003cbr\u003e\u003ci\u003eNathaniel G. N. Milton\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.41 Amyloid-β phosphorylation 364\u003cbr\u003e\u003ci\u003eNathaniel G. N. Milton\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.42 Smitin–myosin II coassembly arrays \u003ci\u003ein vitro \u003c\/i\u003e369\u003cbr\u003e\u003ci\u003eRichard Chi and Thomas C. S. Keller III\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.43 Assembly\/disassembly of myosin filaments in the presence of EF-hand calcium-binding protein S100A4 \u003ci\u003ein vitro \u003c\/i\u003e372\u003cbr\u003e\u003ci\u003eMarina Kriajevska, Igor Bronstein and Eugene Lukanidin\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.44 Collagen fibril assembly \u003ci\u003ein vitro \u003c\/i\u003e375\u003cbr\u003e\u003ci\u003eDavid F. Holmes and Karl E. Kadler\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Selected Reference Data for Cell and Molecular Biology 379\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eDavid Rickwood\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eChemical safety information 379\u003c\/p\u003e \u003cp\u003eCentrifugation data 386\u003c\/p\u003e \u003cp\u003eRadioisotope data 388\u003c\/p\u003e \u003cp\u003eIndex 391\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Biology, life sciences [\u003ca title=\"See our other books on Biology, life sciences\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biology,%20life%20sciences%20%5BPS%5D%22\"\u003ePS\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Wiley","offers":[{"title":"Brand New","offer_id":52278036463896,"sku":"9780470847589","price":122.99,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/files\/9780470847589.jpg?v=1781457073","url":"https:\/\/freshlyprintedbooks.co.uk\/products\/cell-biology-protocols-hardback-9780470847589","provider":"Freshly Printed Books","version":"1.0","type":"link"}