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    1. Naturvetenskap och teknik
    2. Matematik och naturvetenskap
    3. Biologi
    4. Biokemi

    Guide to Zona Pellucida Domain Proteins

    AvEveline S. Litscher,Paul M. Wassarman

    Inbunden, Engelska, 2015

    Del i serien Wiley Series in Protein and Peptide Science

    1 992 kr

    Beställningsvara. Skickas inom 5-8 vardagar. Fri frakt över 249 kr.

    Beskrivning

    This book provides a coherent, clear, and uniform presentation of structural, genetic, molecular, and biochemical information available for the zona pellucida domain protein family, which impact pathologies such as infertility, deafness, and cancer. Furthermore it: Details information about the structure and function of the ZP domain in ZPDC-proteinsProvides illustrations of the organization of ZPDC-proteins, the genes that encode the proteins, and examples of mutations in the ZP domain that cause diseasesSpeculates as to the evolution of the ZP domain and potential therapeutics for diseases stemming from ZP domain mutationsAddresses mammalian and non-mammalian systems

    Produktinformation

    • Utgivningsdatum:2015-08-04
    • Mått:160 x 241 x 16 mm
    • Vikt:413 g
    • Format:Inbunden
    • Språk:Engelska
    • Serie:Wiley Series in Protein and Peptide Science
    • Antal sidor:200
    • Förlag:John Wiley & Sons Inc
    • ISBN:9780470528112

    Utforska kategorier

    • Biokemi inom Naturvetenskap och teknik

    Mer om författaren

    Eveline S. Litscher, Ph.D., is Assistant Professor in the Department of Developmental and Regenerative Biology at the Icahn School of Medicine at Mount Sinai in New York City. Previously a Swiss National Science Foundation post-doctoral fellow in the Department of Cell and Developmental Biology at the Roche Institute of Molecular Biology, she has more than 20 years of research experience working on extracellular coat proteins of mammalian and non-mammalian eggs, and  has published more than 45 primary papers and reviews. Paul M. Wassarman, Ph.D., is Professor in the Department of Developmental and Regenerative Biology at the Icahn School of Medicine at Mount Sinai in New York City. Previously a faculty member in the Department of Biological Chemistry at Harvard Medical School and in the Department of Cell and Developmental Biology at the Roche Institute of Molecular Biology, he has more than 35 years of research experience working on extracellular coat proteins of mammalian and non-mammalian eggs, and has published more than 220 primary papers and reviews.

    Innehållsförteckning

    • List of Tables xiIntroduction to the Wiley Series on Protein and Peptide Science xiiiPreface xvAcknowledgments xviiList of Abbreviations xixPart A Zona Pellucida Domain Proteins 1A.1 Nature of the Zona Pellucida Domain 1A.2 Mouse ZP Proteins 2A.3 Synthesis, Secretion, and Assembly of ZP Proteins 7A.4 Structure of the ZPD 13A.5 Evolution of ZPD Proteins 18Part B Mammalian Zona Pellucida Proteins 21B.1 Introduction 21B.2 Monotremes 22B.3 Marsupials 24B.4 Placental Mammals 25B.4.a Mouse 26B.4.b Rat 26B.4.c Hamster 28B.4.d Rabbit 30B.4.e Cow 32B.4.f Pig 33B.4.g Dog 35B.4.h Monkey 36B.4.i Chimpanzee 38B.4.j Human 40B.5 Mammalian ZP Proteins as Antifertility Vaccines 45B.6 Summary Tables 48Part C Mammalian Zona Pellucida Domain Proteins 53C.1 Betaglycan/TGFβ]Receptor Type III 53C.2 CUB and Zona Pellucida]like Domain 1 (CUZD]1) Proteins 55C.2.a UTCZP/Itmap-1 55C.2.b UO-44/ERG-1 56C.3 Deleted in Malignant Brain Tumor 1 (DMBT1) Proteins 58C.3.a CRP-Ductin 58C.3.b DMBT1 60C.3.c Ebnerin 62C.3.d Hensin 63C.3.e Vomeroglandin 65C.4 Endoglin/CD]105 66C.5 Liver]Specific ZPD]Containing Protein (LZP) 68C.6 Oocyte]Secreted Protein 1 (Oosp1) 69C.7 Pancreatic Zymogen Granule Protein (GP]2) 70C.8 Placenta]Specific 1 (Plac1) 71C.9 Tectorin]α and ]β 72C.10 Uromodulin/Tamm–Horsfall Protein 78C.11 Uromodulin]like Proteins 81C.12 Summary Tables 84Part D Non]mammalian Zona Pellucida Domain Proteins 87D.1 Jellyfish (Aurelia aurita) 87D.1.a Mesoglein 87D.2 Sea Urchins (Strongylocentrotus purpuratus) 90D.2.a Oit-3 90D.2.b UO-44 90D.3 Nematodes (Caenorhabditis elegans) 91D.3.a Cuticlins 91D.3.b DYF-7 93D.3.c RAM-5 94D.4 Mollusks (Haliotis rufescens) 96D.4.a Vitelline envelope ZPs 96D.5 Fruit Flies (Drosophila melanogaster) 101D.5.a Dusky (dy), dusky-like (dyl), and miniature (m) 102D.5.b Dumpy (dp) 104D.5.c NompA (nompA) 105D.5.d Papillote (pot) and piopio (pio) 107D.5.e Quasimodo (qsm) 109D.5.f Shavenbaby target genes (cyr, dyl, m, mey, neo, nyo, tyn, and zye) 109D.6 Tunicates: Vitelline Coat Proteins and Oikosins 113D.6.a Ciona: CiVC-16, -20, -182-1, -569 114D.6.b Halocynthia: HrVC-120, HaVC-130 115D.6.c Oikopleura: oikosins 117D.7 Fish: Vitelline Envelope Proteins 118D.7.a Salmonidae 119D.7.b Cyprinidae 121D.7.c Sparidae 122D.7.d Adrianichthyidae 124D.7.e Cynoglossidae 125D.8 Amphibians: Vitelline Envelope Proteins 127D.8.a Xenopus laevis 127D.8.b Bufo arenarum 130D.9 Reptiles: Predicted ZPD Proteins 133D.9.a Anolis carolinensis 133D.9.b Chelonia mydas 135D.9.c Ophiophagus hannah 136D.10 Birds: Vitelline Envelope Proteins 138D.10.a Chicken vitelline envelope proteins 140D.10.b Quail vitelline envelope proteins 143D.11 Summary Tables 145Part E Appendix 149E.1 Sources of Sequence Information 149E.2 Site(s) of ZP Protein Synthesis 154E.3 Characteristics of Mammalian and Non-Mammalian ZPD Proteins 155E.4 Comparison of Vertebrate ZP Proteins and Human ZP1–4 159E.5 Sequence Alignments of ZPDs with 11 Cys Residues 161E.5A Positions of Cys Residues of ZPDs with 11 Cys Residues 162E.5B Positions of Cys Residues of Drosophila ZPDs with 11 Cys Residues 165Index 167