The Molecular Basis of Mutant Hemoglobin Dysfunction

Content: 
Front Matter, Page iii
Copyright, Page iv
Dedication, Page v
Preface, Pages xi-xii, Paul B. Sigler
Plenary Address: Molecular Disease, Pages 1-14, Vernon M. Ingram
The Influence of Fetal Hemoglobin on the Risk of Complications of Sickle Cell Anemia, Pages 17-28, D.R. Powars, W.A. Schroeder, Joyce N. Weiss, Linda S. Chan
Ocular Manifestations of Sickle Cell Disease, Pages 29-42, Maurice F. Rabb
Introductory Remarks: Human Globin Gene Expression, Pages 45-49, Bernard G. Forget
Organization of Normal and Abnormal Human Globin Genes by Restriction Enzyme Analysis, Pages 51-62, Arthur Bank, J. Gregory Mears, Francesco Ramirez, Michael Baird, John Feldenzer
The α-Globin Genotype as a Determinant of Hematologic Parameters in Sickle Cell Trait, Pages 63-67, Stephen H. Embury, Andrée M. Dozy
Characterization of Linked Human Globin Genes by Molecular Cloning Procedures, Pages 69-78, Edward F. Fritsch, Richard M. Lawn, Tom Maniatis
Regulation of Human Globin Gene Expression after Gene Transfer, Pages 79-96, W. French Anderson, Lillian Killos, Linda Sanders-Haigh, Peter Kretschmer, Elaine Diacumakos, Arthur Nienhuis, Marcia Willing, Devi Vembu
The Introduction of Normal and Mutant Globin Genes into Mammalian Cells Using SV40 Vectors, Pages 97-102, Dean H. Hamer
Introductory Remarks: Structural Analysis of Mutant Hemoglobins and Their Aggregates, Pages 105-108, Robert Josephs
Flexibility of the NH2-Terminal Region of the β Chains of Hemoglobin: Correlation with the Gelation Properties of Deoxyhemoglobin S, Pages 109-118, Arthur Arnone, Patrick D. Briley, Paul H. Rogers, Joel O. Johnson
Contacts Between Molecular Surfaces in Crystals of Deoxygenated Human Hemoglobins A, C, F, and S, Pages 119-124, Warner E. Love, Paula M.D. Fitzgerald, Jonathan C. Hanson, Bradford C. Braden, William E. Royer Jr., John S. Sack
Double Filaments: the Basic Structural Unit of Deoxygenated Sickle Hemoglobin Fibers, Pages 125-135, Beatrice Magdoff-Fairchild, Celia C. Chiu, John F. Bertles
A Plausible Molecular Model for the 14-Filament Fibers of Sickle Cell Hemoglobin, Pages 137-143, Stuart J. Edelstein
Polymorphic Assemblies of Double Strands of Sickle Cell Hemoglobin and their Role in Fiber and Crystal Formation, Pages 145-163, Thomas E. Wellems, Robert J. Vassar, Robert Josephs
The Effect of Additive Conformation on Enhancement of Deoxyhemoglobin Polymerization, Pages 165-186, Maryann McD. Jones, Jacinto Steinhardt
Introductory Remarks: The Molecular Dynamics of Dysfunction and Aggregation of Mutant Hemoglobins, Pages 189-190, Marvin W. Makinen
Subunit Assembly and Interactions in Normal and Abnormal Human Hemoglobins, Pages 191-197, Donald W. Pettigrew, Benjamin W. Turner, Gary K. Ackers
Is It Possible to Deduce the Interaction Between Two Proteins from Their Three-Dimensional Structure?, Pages 199-211, Shoshana J. Wodak
Peptide Inhibitors of the Gelation of Sickle Hemoglobin, Pages 213-223, Kenneth L. Luskey, Vincenzo Pavone, Constance T. Noguchi, Alan N. Schechter
Oxygen Binding and the Gelation of Sickle Cell Hemoglobin, Pages 225-236, J. Hofrichter, H.R. Sunshine, F.A. Ferrone, W.A. Eaton
Rheological Properties of the Gelled Phase of Hemoglobin S, Pages 237-252, Robin W. Briehl
Decreased Binding of 2,3-Diphosphoglycerate to Deoxy Hemoglobin S: A Polymerization-Independent Functional Abnormality, Pages 253-258, Danek Elbaum, Rhoda Elison Hirsch, Ronald L. Nagel
Introductory Remarks: Introductory Comments, Pages 261-262, J.G. White
Red Cell Membrane Alterations Associated with the Sickling Phenomenon, Pages 263-272, Jiri Palek, Pi Kwang Tsung, Zaven Boornazian, Brian Timura, Pi Yao Liu
Sickle Erythrocyte Adherence to Cultured Human Endothelial Cells, Pages 273-279, Robert P. Hebbel, James G. White, John W. Eaton
Introductory Remarks, Pages 283-284, Donald R. Harkness
Prospects for Therapy at the Molecular Level: Historical Review, Pages 285-291, Donald R. Harkness
Covalent Inhibitors of Sickling, Pages 293-304, William C. Mentzer Jr., Rukmani Pennathur-Das, Bertram Lubin, William M. Lande
Weak Binding Gases as Modulators of Hemoglobin Function, Pages 305-312, Benno P. Schoenborn, Anand Saxena, Barry E. North
Chemical Modifications of Hemoglobin S at the 2,3-Diphosphoglycerate Binding Site: An Approach to Therapy of Sickle Cell Disease, Pages 313-331, Joseph A. Walder, Roxanne Y. Walder
Index, Pages 333-338