Ngo J.T, Marks J., Karplus M., Computational complexity, protein structure prediction, and the Levinthal paradox in The Protein Folding Problem, ch.14, pp. 435-508, Birkhauser, 1994.* |
Docherty AJ, Lyons A, Smith BJ, Wright EM, Stephens PE, Harris TJ, Murphy G, Reynolds JJ. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature. Nov. 7-13, 1985;318(6041):66-9.* |
Colman PM. Effects of amino acid sequence changes on antibody-antigen interactions. Res Immunol. Jan. 1994;145(1)33-6.* |
Abaza MS, Atassi MZ. Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 145-151 (antigenic site 5) of myoglobin.* |
Lederman S, et al. A single amino acid substitution in a common African allele of the CD4 molecule ablates binding of the monoclonal antibody, OKT4. Mol Immunol. Nov. 1991;28(11):1171-81.* |
Li CH, Yamashiro D, Tseng LF, Chang WC, Ferrara P. beta-Endorphin omission analogs: dissociation of immunoreactivity from other biological activities. Proc Natl Acad Sci U S A. Jun. 1980; 77(6):3211-4.* |
Amthauer et al., “Placental Alkaline Phosphatase: A Model for Studying COOH-Terminal Processing of Phosphatidylinositol-Glycan-Anchored Membrane Proteins”, Clin. Chem., 38:2510-16 (1992). |
Bennett, “The Molecular Biology of Platelet Membrane Proteins”, Seminars in Hematology, 27:186-204 (1990). |
Berman et al., “A Platelet Alpha Granule Membrane Protein That Is Associated with the Plasma Membrane After Activation”, J. Clin. Invest., 78:130-137 (1986). |
Coller, “A New Murine Monoclonal Antibody Reports an Activation-dependent Change in the Conformation and/or Microenvironment of the Platelet Glycoprotein IIb/IIIa Complex”, J. Clin. Invest., 76:101-108 (1985). |
Einfeld et al., “Transport of Membrane Proteins to the Cell Surface”, Curr. Topics Microbiol. Immunol., 170:107-39 (1991). |
Febbraio et al., “Identification and Characterization of LAMP-1 as an Activation-dependent Plattelet Surface Glycoprotein”, J. Biol. Chem., 265:18531-18537 (1990). |
Feinberg et al., ADDENDUM: “A Technique for Radiolabeling DNA Restriction Endonuclease Fragments to High Specific Activity”, Anal. Biochem., 137:266-67 (1984). |
Foley et al., “Continuous Culture Of Human Lymphoblasts From Peripheral Blood Of A Child With Acute Leukemia”, Cancer, 18:522-529 (1965). |
Fox et al., “Poly(A) Addition During Maturation of Frog Oocytes: Distinct Nuclear and Cytoplasmic Activities and Regulation by the Sequence UUUUUAU”, Genes & Dev., 3:2151-62 (1989). |
Fraker et al., “Protein and Cell Membrane Iodinations With A Sparingly Soluble Chloroamide,1,3,4,6-Tetrachloro-3a, 6a-Diphenylglycoluril”, Biochem. Biophys. Res. Commun., 80:849-57 (1978). |
Fugman et al., “In Vitro Establishment and Characterization of a Human Megakaryoblsatic Cell Line”, Blood, 75:1252-1261 (1990). |
Gish et al., “Identification of Protein Coding Regions by Database Similary Search”, Nat. Genet., 3:266-72 (1993). |
Grange et al., “Human mRNA Polyadenylate Binding Protein: Evolutionary Conservation of a Nucleic Acid Binding Motif”, Nucleic Acids Res., 15:4771-4787 (1987). |
Greenberg et al., “Characterization of a New Megakaryocytic Cell Line: The Dami Cell”, Blood, 72:1968-1977 (1988). |
Hamburger et al., “GMP-140 Mediates Adhesion of Stimulated Platelets to Neutrophils”, Blood, 75:550-554 (1990). |
Hayward et al., “A Novel, Multimeric Platelet Protein that is Released with Platelet Activation and Expressed on the Surface of Activated Platelets”, Blood, 76 (Suppl 1) 458A:P-155 (1990). |
Houng et al., “A Novel Platelet-Cell Activated Protein”, Circulation, Abstracts from the 67th Scientific Sessions, vol. 90, p. I-31, Abstract No. 0699 (1994). |
Johnston et al., “Cloning of GMP-140, a Granule Membrane Protein of Platelets and Endothelium: Sequence Similarity to Proteins Involved in Cell Adhesion and Inflammation”, Cell, 56:1033-44 (1989). |
Kennedy et al., “Protein-Protein Coupling Reactions and the Applications of Protein Conjugates”, Clin. Chim. Acta. 70:1-31 (1976). |
Khyse-Andersen, “Electroblotting of Multiple Gels: A Simple Apparatus Without Buffer Tank for Rapid Transfer of Proteins from Polyacrylamide to Nitrocellulose”, J. Biochem. Biophys. Meth., 10:203-209 (1984). |
Kozak, “The Scanning Model for Translation: An Update”, J. Cell. Biol., 108:229-41 (1989). |
Larsen et al., “PADGEM Protein: A Receptor That Mediates the Interaction of Activated Platelets with Neutrophils and Monocytes”, Cell, 59:305-312 (1989). |
Lefrere et al., “Drosophila Melanogaster Poly(A)-binding Protein: cDNA Cloning Reveals an Usually Long 3′-untranslated Region of the mRNA, also Present in Other Eukaryotic Species”, Gene, 96:219-255 (1990). |
Lin et al., “A Platelet Membrane Protein Expressed During Platelet Activation and Secretion”, J. Bio. Chem., 259:9121-26 (1984). |
Lukacova et al., “Single Step Purification of Platelet Factor XIII Using an Immobilized Factor XIII A-Subunit Monoclonal Antibody”, Thromb. Haemostas., 69:397-400 (1993). |
Lukacova et al., “Inhibition of Factor XIII Activation by an Anti-Peptide Monoclonal Antibody” Biochemistry, 30:10164-10170 (1991). |
McEver et al., “A Monoclonal Antibody to a Membrane Glycoprotein Binds Only to Activated Platelets”, J. Biol. Chem., 259:9799-804 (1984). |
McGrew et al., “Poly(A) Elongation During Xenopus Oocyte Maturation is Required for Translational Recruitment and is Mediated by a Short Sequence Element,”, Genes Dev., 3:803-15 (1989). |
Mudgett-Hunter et al., “Binding and Structural Diversity Among High-Affinity Monoclonal Anti-Digoxin Antibodies”, Mol. Biol., 22:477-88 (1985). |
Munson et al., “LIGAND: A Versatile Computerized Approach for Characterization of Ligand-Binding Systems”, Anal. Biochem., 107:220-39 (1980). |
Mustard et al., “Isolation of Human Platelets from Plasma by Centrifugation and Washing”, Meth. Enzymol., 169(1):3-11 (1989). |
Nietfeld et al., “The Xenopus Laevis poly(A) Binding Protein is Composed of Multiple Functionally Independent RNA Binding Domains”, EMBO J., 9:3699-3705 (1990). |
Reed et al., “Characterization of APP: A Protein Expressed on the Platelet Membrane after Cellular Activation”, Circulation, Abstracts from the 66th Scientific Sessions, p. I-457, Abstract No. 2459 (1993). |
Reed et al., Acceleration of Plasma Clot Lysis by an Antibody to a2-Antiplasmin, Trans. Assoc. Am. Phys., 101st Session, D.C., vol. C1:250-256 (1988). |
Runge et al., “Paramagnetic NMR Contrast Agents Development and Evaluation”, Invest. Radiol. 19:408-15 (1984). |
Sachs et al., “A Single Gene From Yeast for Both Nuclear and Cytoplasmic Polyadenlyate-Binding Proteins: Domain Structure and Expression”, Cell, 45:827-835 (1986). |
Sachs et al., “A Single Domain of Yeast Poly(A)-Binding Protein is Necessary and Sufficient for RNA Binding and Cell Viability”, Mol. Cell. Biol., 7:3268-76 (1987). |
Sandoval et al., “Targeting of Membrane Proteins to Endosomes and Lysosomes”, Trends Cell Biol., 4:292-297 (1994). |
Savage et al., “Thrombin-Induced Increase in Surface Expression of Epitopes on Platelet Membrane Glycoprotein IIb/IIIa Complex and GMP-140 Is a Function of Platelet Age”, Blood, 74:1007-14 (1989). |
Schaefer et al., “In Vivo Nuclear Magnetic Resonance Imagine of Myocardial Perfusion Using the Paramagnetic Contrast Agent Manganese Gluconate”, JACC, 14:472-80 (1989). |
Schuurs et al., Enzyme-Immunoassay, Clin. Chim. Acta., 81:1-40 (1977). |
Shreve et al., “Monoclonal Antibodies Labeled with Polymeric Paramagnetic Ion Chelates”, Magn. Reson. Med., 3:336-40 (1986). |
Singer et al., “The Fluid Mosaic Model of the Structure of Cell Membranes”, Science, 175:720-31 (1972). |
Stambuck et al., “Purification and Characterization of Recombinant Xenopus poly(A)± Binding Protein Expressed in a Baculovirus System”, Biochem. J., 287:761-766 (1992). |
Stenberg et al., “A Platelet Alpha-Granule Membrane Protein (GMP-140) Is Expressed on the Plasma Membrane after Activation”, J. Cell. Biol., 101:880-886 (1985). |
Tian et al., “A Polyadenylate Binding Protein Localized to the Granules of Cytolytic Lymphocutes Induces DNA Fragmentation in Target Cells”, Cell, 67:629-639 (1991). |
Timmons et al., “Isolation of Human Platelets by Albumin Gradient and Gel Filteration”, Methods in Enzymology, 169:11-12 (1989). |
Wang et al., “Nucleotide Sequence of a Mouse Testis ploy(A) Binding Protein cDNA” Nucleic Acids Res., 20:3519 (1992). |
Wesbey et al., “Paramagnetic Pharmaceuticals for Magnetic Resonance Imaging”, Physiol. Chem. Phys. Med. NMR, 16:145-55 (1984). |
Wolf, “Contrast Enhancement in Biomedical NMR”, Physiol. Chem. Phys. Med. NMR, 16:93-95 (1984). |
Zelus et al., “Expression of the Poly(A)-Binding Protein During Development of Xenopus laevis”, Mol. Cell. Biol., 9:2756-2760 (1989). |
Sutherland et al., “Identification of a cell-surface antigen associated with activated T lymphoblasts and activated platelets”, Blood, 77:84:93 (1991). |
Yang et al., “IPABP, an inducible poly(A)-binding protein detected in activated human T cells”, Molecular and Cellular Biology, 15:6770-6776 (1995). |
Scott et al., “Characterization of a novel membrane glycoprotein involved in platelet activation”, J. Biol. Chem., 264:13475-13482 (1989). |
Niewenhuis et al., “Studies with a monoclonal antibody against activated platelets. Evidence that a secreted 53000-molecular weight lysosome-like granule protein is exposed on the surface of activated platelets in the circulation”, Blood, 70:838-845 (1987). |