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- The different roles of mammalian egg zona pellucida (ZP) proteins ZP1-4 during oogenesis, fertilization, and early development, and<\/li>\n
- The role of the zona pellucida domain (ZPD), a long conserved sequence found in ZP1-4 and many other proteins, in normal and diseased states.<\/li>\n<\/ol>\n
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Research<\/p>\nFor all animals, maintenance of life and speciation depend on the process of fertilization. Fusion of eggs and sperm to form a zygote is the culmination of a complex series of interactions between two highly specialized gametes. In mammals, interactions between gametes begin when free-swimming sperm reach the site of ovulated eggs in the oviduct and then bind to the unfertilized egg\u2019s extracellular coat, the zona pellucida (ZP), surrounding the plasma membrane. Identification of the ZP around human eggs dates back nearly 200 years.<\/p>\n
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Paul M. Wassarman<\/strong>
Department of Cell, Developmental, and Regenerative Biology<\/strong>
Icahn School of Medicine at Mount Sinai
Annenberg 25-30B, Box 1020
1468 Madison Avenue
New York, NY 10029-6574
Office: (212) 241-8616\/8620
E-mail:\u00a0 paul.wassarman@mssm.edu<\/a><\/p>\n[\/et_pb_text][\/et_pb_column][\/et_pb_row][\/et_pb_section][et_pb_section fb_built=”1″ module_id=”projects” module_class=”projects-section” _builder_version=”3.22″ background_color=”#eaf2f7″][et_pb_row _builder_version=”3.25″][et_pb_column type=”4_4″ _builder_version=”3.25″ custom_padding=”|||” custom_padding__hover=”|||”][et_pb_text admin_label=”Current Projects” module_id=”projects” module_class=”projects-section” _builder_version=”3.27.4″]<\/p>\n
Current Projects<\/h4>\n
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<\/p>\nOur research has focused on mammalian egg and sperm surface components that account for species-restricted binding of sperm to eggs during fertilization. Among these components are proteins present in the ovulated egg\u2019s ZP. In mice the unfertilized egg\u2019s ZP consists of only three proteins called ZP1, ZP2, and ZP3. A fourth protein, ZP4, present in ZP of a number of other mammalian eggs, including human eggs, is very similar to ZP1. Over the years we were the first to (i) identify, name, and characterize ZP1-3; (ii) identify growing oocytes as the source of nascent ZP1-3; (iii) demonstrate that ZP2 and ZP3 are sperm receptors; (iv) demonstrate that ZP3 is an acrosome reaction- inducer; (v) determine the primary structure of ZP3; (vi) clone and characterize the gene encoding ZP3; (vii) identify cis-acting sequences and trans-acting factors that regulate ZP3 gene expression; and (viii) produce ZP3 heterozygous and homozygous null mice. While much of our research has been carried out with mice, ZP1-3 are present in the ZP of all mammalian eggs, including human eggs, and ZP1-3-like proteins are present as well in the extracellular coat of eggs from amphibians, birds, fish, and many invertebrates.<\/p>\n
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<\/p>\nSchematic representation of the organization of mouse zona pellucida (ZP) proteins mZP1\u20133 and human ZP protein hZP4. In each case, the polypeptide has a signal sequence at the N terminus; a ZP domain (ZPD) consisting of ZP-N and ZP-C subdomains and a linker region; a consensus furin cleavage site (CFCS); transmembrane domain (TMD); and cytoplasmic tail in the C-terminal propeptide (CTP). mZP1 and hZP4 also have a trefoil domain adjacent to the ZPD. mZP2 [713 amino acids (aa)] has three additional ZP-N subdomains, N1\u2013N3, between the N terminus of the polypeptide and the ZPD. mZP1 (623 aa) and hZP4 (540 aa) have one additional ZP-N subdomain, N1, between the N terminus of the polypeptide and the trefoil domain. mZP3 is the smallest of the three mouse ZP proteins (424 aa) and consists primarily of a ZPD. Notably, mZP1 and mZP2 have only three or four aa between the ZPD and the CFCS, whereas mZP3 has 47 aa, which include the sperm-combining site and represent a region of positive Darwinian selection during evolution.<\/p>\n
Our studies revealed that ZP1-3 are synthesized, processed, and secreted by mouse oocytes, the precursors of eggs, during oogenesis. In mammals expression of single-copy genes encoding ZP1-3 is female specific. During growth of oocytes, nascent ZP1-3 are secreted, processed, and assemble using non-covalent interactions into an extensive network of interconnected fibrils that constitute the thick ZP matrix. The fibrils consist of ZP2-ZP3 dimers present every 140 \u00c5 or so along the fibrils, and the fibrils are interconnected by ZP1 and\/or ZP4. Free-swimming sperm recognize and bind to a specific region of ZP3, the sperm combining-site. Binding to ZP3 activates the signal transduction pathway of sperm that culminates in exocytosis, the acrosome reaction, that enables bound sperm to penetrate the ZP and reach the egg\u2019s plasma membrane. After undergoing the acrosome reaction, either spontaneously or due to binding to ZP3, acrosome-reacted sperm bind to ZP2. Therefore, ZP2 and ZP3 are structural proteins used to build a specialized extracellular matrix around eggs and are sperm receptors employed during fertilization. ZP3 is also an activator of signal transduction when acrosome-intact sperm bind to unfertilized eggs. Once eggs are fertilized by a single sperm ZP2 and ZP3 are modified and the structure of the ZP is altered such that additional free-swimming sperm can no longer bind to the ZP \u2013 part of the so-called block to polyspermy.<\/p>\n
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<\/p>\nSchematic representation of a general mechanism for assembly of nascent ZP proteins. In all ZPD precursor proteins (Precursor), the ZPD (ZP-N and ZP-C) is followed by a C-terminal propeptide (CTP) that contains a basic cleavage site, such as a consensus furin cleavage-site (CFCS), and external hydrophobic patch (EHP), and a transmembrane domain (TMD) anchor site. Precursors do not polymerize within the cell either as a result of direct interaction between the EHP and internal hydrophobic patch (IHP) or because they adopt a conformation dependent on the presence of both hydrophobic patches. C-terminal processing at the CFCS by a proprotein convertase (Cleaved at CFCS, X) leads to dissociation of mature proteins from the EHP and activation of the ZPD (Activation of ZPD) for assembly (Polymerization) into fibrils and matrix.<\/p>\n
All ZP proteins share a large region of polypeptide, approximately 270 amino acids in length, called the zona pellucida domain (ZPD). A ZPD has 8 conserved cysteine residues present as 4 intramolecular disulfides and arose more than 600 million years ago. A ZPD is also present in a wide variety of other proteins of diverse origins and functions. For example, ZPD-containing proteins are components of the mammalian egg, inner ear, nose, and kidney, as well as the Drosophila cuticle, wing epithelium, and mechanosensory organ. Our research strongly suggests that the ZPD is a conserved module used generally for polymerization of extracellular proteins. Since a ZPD is found in a number of proteins involved in human pathologies, including deafness, infertility, vascular and renal disease, and cancer, we are also interested in relationships between mutations in the ZPD and disease.<\/p>\n
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Publications<\/h4>\n
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Wassarman, P.M. and Litscher, E.S.:\u00a0 Zona pellucida proteins, fibrils, and matrix.\u00a0\u00a0Annual Review Biochemistry<\/em>\u00a089: 695-715 (2020).<\/p>\n
Wassarman, P.M.:\u00a0\u00a0A Place in History: The Biography of John C. Kendrew.<\/em>\u00a0Oxford University Press, 368 pp. (2020).<\/p>\n
Litscher, E.S. and Wassarman, P.M.:\u00a0 Zona pellucida genes and proteins and human fertility.\u00a0 Trends Developmental Biology<\/em> 13: 21-33 (2020).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 Zona pellucida genes and proteins:\u00a0 Essential players in mammalian oogenesis and fertility.\u00a0\u00a0 Genes (Basel)<\/em> 12: 1-22 (2021).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 Female fertility and the zona pellucida.\u00a0 eLife<\/em> 11: e76106 (2022).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 Mammalian fertilization.\u00a0 In Brenner\u2019s Encyclopedia of Genetics<\/em>, 4th ed., in press (2023).<\/p>\n
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Plaza, S., Chanut-Delalande, H., Fernandes, I., Wassarman, P.M., and Payre, F.:\u00a0 From A to Z:\u00a0 Apical structures and zona pellucida-domain proteins.\u00a0 Trends Cell Biology <\/em>20: 524-532 (2010).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 Egg’s ZP3 structure speaks volumes.\u00a0 Cell <\/em>143: 337-338\u00a0 (2010).<\/p>\n
Wassarman, P.M. and Soriano, P.M. (Eds.):\u00a0 Guide to Techniques in Mouse Development, Part A, Mice, Embryos, and Cells.\u00a0 Methods in Enzymology<\/em> 476: 539 pp. (2010) .<\/p>\n
Wassarman, P.M. and Soriano, P.M. (Eds.):\u00a0 Guide to Techniques in Mouse Development, Part B, Mouse Molecular Genetics. \u00a0Methods in Enzymology<\/em> 477: 637 pp. (2010).<\/p>\n
Wassarman, P.M.:\u00a0 The sperm\u2019s sweet tooth.\u00a0 Science <\/em>233: 1708-1709 (2011).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 Influence of the zona pellucida of the mouse egg on folliculogenesis and fertility.\u00a0 International Journal Developmental Biology<\/em> 56: 833-839 (2012).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 Biogenesis of the mouse egg\u2019s extracellular coat, the zona pellucida.\u00a0 Current Topics in Developmental Biology <\/em>102: 243-266 (2013).<\/p>\n
Wassarman, P.M. (Ed.):\u00a0 Gametogenesis.\u00a0 Current Topics in Developmental Biology<\/em> 102: 434 pp. (2013).<\/p>\n
Wassarman, P.M.:\u00a0 Reproductive biology:\u00a0 Sperm protein finds its mate.\u00a0 Nature <\/em>508:\u00a0 466-467 (2014).<\/p>\n
Litscher, E.S. and Wassarman, P.M.:\u00a0 Evolution, structure, and synthesis of vertebrate egg-coat proteins.\u00a0 Trends in Developmental Biology <\/em>8: 65-76 (2014).<\/p>\n
Rosenwaks, Z. and Wassarman, P.M. (Eds.):\u00a0 Human Fertility: Methods and Protocols.\u00a0 Methods in Molecular Biology<\/em> 1154: 584 pp. (2014).<\/p>\n
Litscher, E.S. and Wassarman, P.M. (Eds.):\u00a0 A Guide to Zona Pellucida Domain Proteins.<\/em>\u00a0 John Wiley and Sons, 208 pp. (2015).<\/p>\n
Wassarman, P.M. (Ed.):\u00a0 Essays on Developmental Biology. Current Topics in Developmental Biology <\/em>Part A 116: 744 pp.; Part B 117: 710 pp. (2016).<\/p>\n
Wassarman P.M.:\u00a0 A personal perspective:\u00a0 My four encounters with John Kendrew.\u00a0 Journal Molecular Biology<\/em> 429: 2594-2600 (2017).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 The mouse egg\u2019s zona pellucida.\u00a0 Current Topics in Developmental Biology<\/em> 130: 331-356 (2018).<\/p>\n
Litscher, E.S. and Wassarman, P.M.: \u00a0The fish egg’s zona pellucida. \u00a0Current Topics in Developmental Biology<\/em> 130: 275-306 (2018).<\/p>\n
Litscher, E.S. and Wassarman, P.M. (Eds.):\u00a0 Extracellular Matrix and Egg Coats. <\/span>Current Topics in Developmental Biology<\/em> 130: 488 pp. (2018).<\/span><\/p>\n
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Wassarman, P.M., Jovine, L., and Litscher, E.S.:\u00a0 A profile of fertilization in mammals.\u00a0 Nature Cell Biology<\/em> 3: E59-E64 (2001).<\/p>\n
Qi, H., Williams, Z.,\u00a0 and Wassarman, P.M.:\u00a0 Secretion and assembly of zona pellucida glycoproteins by growing mouse oocytes microinjected with epitope-tagged cDNAs for mZP2 and mZP3.\u00a0 Molecular Biology Cell<\/em> 13:\u00a0 530-541 (2002).<\/p>\n
Jovine, L., Qi, H., Williams, Z., Litscher, E., and Wassarman, P.M.:\u00a0 The ZP domain is a conserved module for protein polymerization.\u00a0 Nature Cell Biology<\/em> 4:\u00a0 457-461 (2002).<\/p>\n
Wassarman, P.M. and Keller, G.M. (Eds.):\u00a0 Differentiation of Embryonic Stem Cells. Methods in Enzymology<\/em> 36: 535 pp. (2003) .<\/p>\n
Jovine, L., Qi, H., Williams, Z., Litscher, E.S., and Wassarman, P.M.:\u00a0 A duplicated motif controls assembly of zona pellucida domain proteins.\u00a0 Proceedings National Academy Sciences, USA<\/em>\u00a0 101: 5922-5927 (2004).<\/p>\n
Darie, C.C., Biniossek, M.L., Jovine, L., Litscher, E.S., and Wassarman, P.M.:\u00a0 Structural characterization of fish egg vitelline envelope proteins by mass spectrometry.\u00a0 Biochemistry <\/em>43: 7459-7478 (2004).<\/p>\n
Jovine, L., Darie, C.C., Litscher, E.S., and Wassarman, P.M.:\u00a0 Zona pellucida domain proteins.\u00a0 Annual Review Biochemistry<\/em> 74: 83-114 (2005).<\/p>\n
Williams, Z., Litscher, E.S., Jovine, L., and Wassarman, P.M.:\u00a0 Polypeptide encoded by mouse ZP3<\/em> exon-7 is necessary and sufficient for sperm binding in vitro<\/em>.\u00a0\u00a0 Journal Cellular Physiology <\/em>207: 30-39 (2006).<\/p>\n
Wassarman, P.M.:\u00a0 Fertilization:\u00a0 Welcome to the fold.\u00a0 Nature <\/em>456: 586-587 (2008).<\/p>\n
Wassarman, P.M.:\u00a0 Zona pellucida glycoproteins.\u00a0 Journal Biological Chemistry<\/em> 283: 24285-24289 (2008).<\/p>\n
Wassarman, P.M. and Litscher, E.S.:\u00a0 Mammalian fertilization is dependent on multiple membrane fusion events.\u00a0\u00a0 In, Cell Fusion: Methods and Protocols 475: 99-113, Methods in Molecular Biology <\/em>(2008).<\/p>\n
Wassarman, P.M. and Vacquier, V.D. (Eds.):\u00a0 Fertilization.\u00a0 International Journal Developmental Biology <\/em>52: 388 pp. (2008).<\/p>\n
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Lira, S.A., Kinloch, R.A., Mortillo, S., and Wassarman, P.M.: An upstream region of the mouse ZP3 gene directs expression of firefly luciferase specifically to growing oocytes in transgenic mice. Proceedings National Academy of Sciences, USA<\/em> 87: 7215-7219 (1990).<\/p>\n
Wassarman, P.M.: Profile of a mammalian sperm receptor. Development<\/em> 108: 1-19 (1990).<\/p>\n
Mortillo, S. and Wassarman, P.M.: Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments. Development <\/em> 113: 141-149 (1991).<\/p>\n
Wassarman, P.M. (Ed.): Elements of Mammalian Fertilization,<\/em> Vol. 1, Basic Concepts, Vol. 2, Practical Applications, 493 pp. (1991).<\/p>\n
Kinloch, R.A., Mortillo, S., Stewart, C.L., and Wassarman, P.M.: Embryonal carcinoma cells transfected with ZP3 genes differentially glycosylate similar polypeptides and secrete active mouse sperm receptor. Journal Cell Biology<\/em> 115: 655-664 (1991).<\/p>\n
Wassarman, P.M. and DePamphilis, M.L. (Eds.): Guide to Techniques in Mouse Development. Methods in Enzymology<\/em> 225: 1021 pp. (1993).<\/p>\n
Wassarman, P.M.: Towards molecular mechanisms for gamete adhesion and fusion during mammalian fertilization. Current Opinion Cell Biology<\/em> 7: 658-664 (1995).<\/p>\n
Litscher, E.S, Juntunen, K., Seppo, A., Niemal\u00e4, R., Penttil\u00e4, L., Renkonen, O., and Wassarman, P.M.: Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro. Biochemistry<\/em> 34: 4662-4669 (1995).<\/p>\n
Liu, C., Litscher, E.S., Mortillo, S., Sakai, Y., Kinloch, R.A., Stewart, C.L., and Wassarman, P.M.: Targeted disruption of the mZP3 gene results in production of eggs lacking a zona pellucida and infertility in female mice. Proceedings National Academy of Sciences, USA<\/em> 93: 5431-5436 (1996).<\/p>\n
Wassarman, P.M.: Mammalian fertilization: Molecular aspects of gamete adhesion, exocytosis, and fusion. Cell <\/em> 96: 175-183 (1999).<\/p>\n
Wassarman, P.M. and Wolffe, A.P. (Eds.): Chromatin. Methods in Enzymology<\/em> 304: 815 pp. (1999).<\/p>\n
Litscher, E.S., Qi, H., and Wassarman, P.M.: Mouse zona pellucida glycoproteins mZP2 and mZP3 undergo carboxy-terminal proteolytic processing in growing oocytes. Biochemistry<\/em> 38: 12280-12287 (1999).<\/p>\n
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DePamphilis, M.L. and Wassarman, P.M.: Eukaryotic chromosome replication: A close-up of the replication fork. Annual Review Biochemistry<\/em> 49: 627-666 (1980).<\/p>\n
Shelton, E.R., Wassarman, P.M., and DePamphilis, M.L.: Structure, spacing and phasing of nucleosomes on isolated forms of mature simian virus 40 chromosomes. Journal<\/em> Biological Chemistry<\/em> 255: 771-782 (1980).<\/p>\n
Bleil, J.D. and Wassarman, P.M.: Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte’s zona pellucida. Developmental Biology<\/em> 76: 185-202 (1980).<\/p>\n
Bleil, J.D. and Wassarman, P.M.: Synthesis of zona pellucida proteins by denuded and follicle-enclosed mouse oocytes during culture in vitro. Proceedings National Academy<\/em> of Sciences, USA<\/em> 77: 1029-1033 (1980).<\/p>\n
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Bleil, J.D. and Wassarman, P.M.: Mammalian sperm-egg interaction: Identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell <\/em> 20: 873-882 (1980).<\/p>\n
Herman, T.M., DePamphilis, M.L., and Wassarman, P.M.: Structure of chromatin at DNA replication forks: Location of the first nucleosomes on newly synthesized Simian virus 40 DNA. Biochemistry<\/em> 20: 621-630 (1981).<\/p>\n
Greve, J.M., Salzmann, G.S., Roller, R.J., and Wassarman, P.M.: Biosynthesis of the major zona pellucida glycoprotein secreted by oocytes during mammalian oogenesis. Cell <\/em> 31: 749-759 (1982).<\/p>\n
DePamphilis, M.L. and Wassarman, P.M.: The organization and replication of Papovavirus DNA and chromatin. In, The Organization and Replication of Viral DNA,<\/em> (A.S. Kaplan, ed.), pp. 37-114 (1982).<\/p>\n
Salzmann, G.S., Greve, J.M., Roller, R.J., and Wassarman, P.M.: Biosynthesis of the sperm receptor during oogenesis in the mouse. EMBO Journal<\/em> 2: 1451-1456 (1983).<\/p>\n
Cusick, M.E., DePamphilis, M.L., and Wassarman, P.M.: Dispersive segregation of nucleosomes during replication of simian virus 40 chromosomes. Journal Molecular Biology <\/em> 178: 249-261 (1984).<\/p>\n
Greve, J.M. and Wassarman, P.M.: Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat. Journal Molecular Biology<\/em> 181: 253-264 (1985).<\/p>\n
Florman, H.M. and Wassarman, P.M.: O-Linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity. Cell <\/em> 41: 313-324 (1985).<\/p>\n
Wassarman, P.M., Bleil, J.D., Florman, H.M., Greve, J.M. et al.: The mouse egg’s sperm receptor: What is it and how does it work? In, Molecular Biology of Development, Cold Spring Harbor Symposium Quantitative Biology<\/em> 50: 11-18 (1985).<\/p>\n
Bleil, J.D. and Wassarman, P.M.: Autoradiographic visualization of the mouse egg’s sperm receptor bound to sperm. Journal Cell Biology<\/em> 102: 1363-1371 (1986).<\/p>\n
Wassarman, P.M.: The biology and chemistry of fertilization. Science<\/em> 235: 553-560 (1987).<\/p>\n
Chalifour, L.E., Wirak, D.O., Hansen, U., Wassarman, P.M., and DePamphilis, M.L.: Cis- and trans-acting sequences required for the expression of Simian virus 40 genes in mouse oocytes. Genes and Development<\/em> 1: 1096-1106 (1987).<\/p>\n
Wassarman, P.M.: Early events in mammalian fertilization. Annual Review Cell Biology<\/em> 3: 109-142 (1987).<\/p>\n
Bleil, J.D., Greve, J.M., and Wassarman, P.M.: Identification of a secondary sperm receptor in the mouse egg zona pellucida: Role in maintenance of binding of acrosome-reacted sperm to eggs. Developmental Biology<\/em> 128: 376-385 (1988).<\/p>\n
Kinloch, R.A., Roller, R.J., Fimiani, C.M., Wassarman, D.A., and Wassarman, P.M.: Primary structure of the mouse sperm receptor’s polypeptide chain determined by genomic cloning. Proceedings National Academy of Sciences, USA<\/em> 85: 6409-6413 (1988).<\/p>\n
Wassarman, P.M.: Zona pellucida glycoproteins. Annual Review Biochemistry<\/em> 57: 415-442 (1988).<\/p>\n
Wassarman, P.M.: Fertilization in mammals. Scientific American<\/em> 255: 78-84 (December, 1988).<\/p>\n
Wassarman, P.M. and Kornberg, R.D. (Eds.): Nucleosomes. Methods in Enzymology<\/em> 170: 683 pp. (1989).<\/p>\n
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Wassarman, P.M. and Lentz, P.J.: The interaction of tetraiodofluorescein with dogfish muscle lactate dehydrogenase: A chemical and X-ray crystallographic investigation. Journal Molecular Biology<\/em> 60: 509-523 (1971).<\/p>\n
Wassarman, P.M. and Burgner, J.W.: Kinetics of unfolding of dogfish muscle lactate dehydrogenase in the presence of guanidine hydrochloride. Journal Molecular Biology<\/em> 67: 537-542 (1972).<\/p>\n
Wassarman, P.M., Hollinger, T.G., and Smith, L.D.: RNA polymerases in the germinal vesicle contents of Rana pipiens<\/em> oocytes. Nature <\/em>240: 208-210 (1972).<\/p>\n
Sorensen, R.A. and Wassarman, P.M.: Relationship between growth and meiotic maturation of the mouse oocyte. Developmental Biology<\/em> 50: 531-536 (1976).<\/p>\n
Wassarman, P.M. and Letourneau, G.E.: RNA synthesis in fully grown mouse oocytes. Nature<\/em> 261: 73-74 (1976).<\/p>\n
Wassarman, P.M., Josefowicz, W.J., and Letourneau, G.E.: Meiotic maturation of mouse oocytes in vitro: Inhibition of maturation at specific stages of nuclear progression. Journal Cell Science<\/em> 22: 531-545 (1976).<\/p>\n
Schultz, R.M. and Wassarman, P.M.: Specific changes in the pattern of protein synthesis during meiotic maturation of the mammalian oocyte in vitro. Proceedings National Academy of Sciences, USA<\/em> 74: 538-542 (1977).<\/p>\n
Wassarman, P.M., Ukena, T.E., Josefowicz, W.J., and Karnovsky, M.J.: Asymmetrical distribution of microvilli in cytochalasin B induced pseudo-cleavage of mouse oocytes. Nature <\/em> 265: 742-744 (1977).<\/p>\n
Schultz, R.M., LaMarca, M.J., and Wassarman, P.M.: Absolute rates of protein synthesis during meiotic maturation of mouse oocytes in vitro. Proceedings National<\/em> Academy of Sciences, USA<\/em> 75: 4160- 4164 (1978).<\/p>\n
Shelton, E.R., Wassarman, P.M., and DePamphilis, M.L.: The structure of Simian virus 40 chromosomes in nuclei from infected monkey cells. Journal Molecular Biology<\/em> 125: 491-510 (1978).<\/p>\n
[\/et_pb_accordion_item][\/et_pb_accordion][et_pb_button button_url=”http:\/\/www.ncbi.nlm.nih.gov\/sites\/myncbi\/james.bieker.1\/bibliography\/40735946\/public\/?sort=date&direction=descending” button_text=”PubMed” disabled_on=”on|on|on” _builder_version=”3.19.10″ custom_button=”on” button_text_size=”14″ button_text_color=”#ffffff” button_bg_color=”#00aeef” button_border_width=”0″ button_border_radius=”2″ button_font=”Open Sans||||||||” button_use_icon=”off” background_layout=”dark” disabled=”on”][\/et_pb_button][et_pb_divider divider_style=”dotted” divider_position=”center” divider_weight=”0.5″ disabled_on=”on|on|on” _builder_version=”3.19.10″ height=”25px” disabled=”on”][\/et_pb_divider][et_pb_text disabled_on=”on|on|on” admin_label=”reviews” _builder_version=”3.27.4″ disabled=”on”]<\/p>\n
Selected Reviews<\/h4>\n
M.N. Gnanapragasam\u00a0Orchestration of late events in erythropoiesis by KLF1\/EKLF, Current Opinion in Hematology<\/em>, 24<\/u>, 183-190 (2017).<\/p>\n
Perkins, X. Xu, D.R. Higgs, G.P. Patrinos, L. Arnaud and S. Philipsen, \u201cKru\u0308ppeling\u201d erythropoiesis: an unexpected broad spectrum of human red blood cell disorders due to KLF1 <\/em>variants, Blood<\/em>, 127<\/u>, 1856-1862 (2016).<\/p>\n
Manwani KLF1: when less is more, Blood<\/em>, 124<\/u>, 672-673 (2014).<\/p>\n
Yien EKLF\/KLF1: a tissue-restricted integrator of transcriptional control, chromatin remodeling, and lineage determination, Molecular and Cellular Biology<\/em>, 33<\/u>, 4-13 (2013).<\/p>\n
Siatecka \u00a0The multifunctional role of EKLF\/KLF1 during erythropoiesis, Blood<\/em>, 118<\/u>, 2044-2054 (2011).<\/p>\n
Putting a finger on the switch, Nature Genetics<\/em>, 42<\/u>, 733-734 (2010).<\/p>\n
Kr\u00fcppel-like Factors: Three Fingers in Many Pies, Journal of Biological Chemistry<\/em>, 276<\/u>, 34355-34358 (2001).<\/p>\n
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Team<\/h4>\n
[\/et_pb_text][\/et_pb_column][\/et_pb_row][et_pb_row column_structure=”1_4,3_4″ _builder_version=”3.25″ background_size=”initial” background_position=”top_left” background_repeat=”repeat”][et_pb_column type=”1_4″ _builder_version=”3.25″ custom_padding=”|||” custom_padding__hover=”|||”][et_pb_image src=”https:\/\/labs.icahn.mssm.edu\/wassarmanlab\/wp-content\/uploads\/sites\/357\/2020\/06\/11.jpg” align_tablet=”center” align_phone=”” align_last_edited=”on|desktop” admin_label=”Paul M. Wassarman, Ph.D.” _builder_version=”3.23″ border_radii=”on|5px|5px|5px|5px”][\/et_pb_image][\/et_pb_column][et_pb_column type=”3_4″ _builder_version=”3.25″ custom_padding=”|||” custom_padding__hover=”|||”][et_pb_text _builder_version=”3.27.4″ text_text_color=”#000000″]<\/p>\n
\nPaul M. Wassarman, Ph.D.<\/strong>, Brandeis University (Biochemistry), is a Full Professor at ISMMS. He was a Helen Hay Whitney Foundation Postdoctoral Fellow at the MRC Laboratory of Molecular Biology, Cambridge, England, and a Rockefeller Foundation Special Research Fellow at Harvard Medical School. Previously a faculty member in the Department of Biological Chemistry at Harvard Medical School and the Department of Cell and Developmental Biology at the Roche Institute of Molecular Biology, he has more than 40 years of research experience working on fertilization and extracellular coat proteins of mammalian and non-mammalian eggs and has published more than 240 primary papers and reviews. He is Series Editor of Current Topics in Developmental Biology published five-times annually by Academic Press\/Elsevier, editor of more than a dozen books and periodicals, and author of A Place in History: The Biography of John C. Kendrew published by Oxford University Press in 2020.
E-mail: paul.wassarman@mssm.edu<\/a><\/p>\n[\/et_pb_text][\/et_pb_column][\/et_pb_row][et_pb_row column_structure=”1_4,3_4″ _builder_version=”3.25″ background_size=”initial” background_position=”top_left” background_repeat=”repeat”][et_pb_column type=”1_4″ _builder_version=”3.25″ custom_padding=”|||” custom_padding__hover=”|||”][et_pb_image src=”https:\/\/labs.icahn.mssm.edu\/wassarmanlab\/wp-content\/uploads\/sites\/357\/2020\/06\/22.jpg” align_tablet=”center” align_phone=”” align_last_edited=”on|desktop” admin_label=”Eveline S. Litscher, Ph.D.” _builder_version=”3.23″ border_radii=”on|5px|5px|5px|5px”][\/et_pb_image][\/et_pb_column][et_pb_column type=”3_4″ _builder_version=”3.25″ custom_padding=”|||” custom_padding__hover=”|||”][et_pb_text _builder_version=”3.27.4″ text_text_color=”#000000″]<\/p>\n
\nEveline S. Litscher, Ph.D.<\/strong>, University of Z\u00fcrich (Cell Biology), is an Assistant Professor at ISMMS. Previously a Swiss National Science Foundation Postdoctoral Fellow in the Department of Cell and Developmental Biology at the Roche Institute of Molecular Biology, she has more than 30 years of research experience working on fertilization and extracellular coat proteins of mammalian and non-mammalian eggs and has published more than 50 primary papers and reviews. She is the author of A Guide to Zona Pellucida Domain Proteins published by John Wiley and Sons in 2015.
E-mail: eveline.litscher@mssm.edu<\/a><\/p>\n[\/et_pb_text][\/et_pb_column][\/et_pb_row][et_pb_row column_structure=”1_4,1_4,1_4,1_4″ disabled_on=”on|on|on” _builder_version=”3.25″ disabled=”on”][et_pb_column type=”1_4″ _builder_version=”3.25″ custom_padding=”|||” custom_padding__hover=”|||”][et_pb_text _builder_version=”3.27.4″ text_text_color=”#ffffff”]<\/p>\n
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