Cooperativity in antigen binding as a potential element in Tc cell recognition.

[1]  B. Manjula,et al.  A common mechanism of hapten binding to immunoglobulins and their heterologous chain recombinants. , 1980, Biochemistry.

[2]  K. J. Dorrington,et al.  Equilibrium and kinetic aspects of the interaction of isolated variable and constant domains of light chain with the Fd' fragment of immunoglobulin G. , 1979, Biochemistry.

[3]  R. Blanden,et al.  Primary anti-viral cytotoxic T-cell responses in semiallogeneic chimeras are not absolutely restricted to host H-2 type , 1979, The Journal of experimental medicine.

[4]  U. Kees,et al.  Specific adsorption of H-2-restricted cytotoxi T cells to macrophage monolayers , 1978, The Journal of experimental medicine.

[5]  D. Lancet,et al.  Hapten-linked conformational equilibria in immunolglobulins XRPC-24 and J-539 observed by chemical relaxation. , 1978, Biophysical journal.

[6]  P. Matzinger,et al.  In a fully H-2 incompatible chimera, T cells of donor origin can respond to minor histocompatibility antigens in association with either donor or host H-2 type , 1978, The Journal of experimental medicine.

[7]  N. K. Jerne,et al.  Major histocompatibility complex-linked immune-responsiveness is acquired by lymphocytes of low-responder mice differentiating in thymus of high-responder mice. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[8]  G. Ada,et al.  A Dual Recognition Model for Cytotoxic T Cells Based on Thymic Selection of Precursors with Low Affinity for Self H‐2 Antigens , 1978, Scandinavian journal of immunology.

[9]  R. Zinkernagel,et al.  On the thymus in the differentiation of "H-2 self-recognition" by T cells: evidence for dual recognition? , 1978, The Journal of experimental medicine.

[10]  D. Lancet,et al.  Hapten-induced allosteric transition in the light chain dimer of an immunoglobulin , 1977, Nature.

[11]  M. Bevan In a radiation chimaera, host H–2 antigens determine immune responsiveness of donor cytotoxic cells , 1977, Nature.

[12]  D. Lancet,et al.  Kinetic evidence for hapten-induced conformational transition in immunoglobin MOPC 460. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[13]  C. Janeway,et al.  Two Different VH Gene Products Make Up the T‐Cell Receptors , 1976, Scandinavian journal of immunology.

[14]  I. Schechter,et al.  Binding of 2,4-dinitrophenyl derivatives by the light chain dimer obtained from immunoglobulin A produced by MOPC-315 mouse myeloma. , 1976, Biochemistry.

[15]  R. Zinkernagel,et al.  Specificity of Virus‐Immune Effector T Cells for H‐2K or H‐2D Compatible Interactions: Implications for H‐Antigen Diversity , 1976, Transplantation reviews.

[16]  R. Zinkernagel H-2 compatibility requirement for virus-specific T-cell-mediated cytolysis. The H-2K structure involved is coded by a single cistron defined by H-2Kb mutant mice , 1976, The Journal of experimental medicine.

[17]  U. Kees,et al.  A single genetic element in H-2K affects mouse T-cell antiviral function in poxvirus infection , 1976, The Journal of experimental medicine.

[18]  K. Eichmann Idiotype suppression. II. Amplification of a suppressor T cell with anti‐idiotypic activity , 1975, European journal of immunology.

[19]  G. Shearer,et al.  Cell‐mediated cytotoxicity to trinitrophenyl‐modified syngeneic lymphocytes , 1974, European journal of immunology.

[20]  H. Grey,et al.  Studies on the structure of mouse gamma-A myeloma proteins. , 1968, Biochemistry.

[21]  J. Changeux,et al.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.

[22]  R. Langman,et al.  Cell-mediated immunity and the major histocompatibility complex. , 1978, Reviews of physiology, biochemistry and pharmacology.

[23]  D. Lancet,et al.  Thermodynamic and spectroscopic comparison of the binding sites of the mouse myeloma protein 315 and of its light chain dimer , 1977, FEBS letters.

[24]  H. Binz,et al.  Antigen-binding, idiotypic T-lymphocyte receptors. , 1977, Contemporary topics in immunobiology.