Molecular Basis for T Lymphocyte Recognition of Antigens (Part 1 of 2)

1981 ◽  
pp. 182-201
Author(s):  
Robert E. Cone
Keyword(s):  
T Lymphocyte ◽  
Molecular Basis

scholarly journals Molecular basis for cytolytic T-lymphocyte recognition of the murine cytomegalovirus immediate-early protein pp89.

1988 ◽  
Vol 62 (11) ◽  
pp. 3965-3972 ◽  
Author(s):  
M Del Val ◽  
H Volkmer ◽  
J B Rothbard ◽  
S Jonjić ◽  
M Messerle ◽  
...  
Keyword(s):  
T Lymphocyte ◽  
Molecular Basis ◽  
Immediate Early ◽  
Murine Cytomegalovirus ◽  
Early Protein ◽  
Cytolytic T Lymphocyte

The T Lymphocyte Response to HIV: Molecular Basis for Immune Recognition and Escape

2015 ◽  
pp. 20-23
Author(s):  
Frances Gotch ◽  
Rodney Phillips ◽  
Sarah Rowland-Jones ◽  
Douglas Nixon ◽  
Jon Edwards ◽  
...  
Keyword(s):  
T Lymphocyte ◽  
Molecular Basis ◽  
Immune Recognition ◽  
Lymphocyte Response

scholarly journals Molecular Basis for Distinct, Antagonistic, Regulatory Functions of Ribosomal Protein Paralogs Rpl22 and Rpl22-Like1 (Like1) in Hematopoiesis

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 3575-3575
Author(s):  
Minshi Wang ◽  
Yong Zhang ◽  
Shuyun Rao ◽  
Jennifer Rhodes ◽  
Michele Rhodes
Keyword(s):  
Amino Acid ◽  
Ribosomal Protein ◽  
T Lymphocyte ◽  
Molecular Basis ◽  
Rna Binding ◽  
Lymphocyte Development ◽  
Homologous Proteins ◽  
Hematopoietic Stem ◽  
Terminal Amino ◽  
Regulatory Functions

Abstract The prevailing view of ribosomal proteins (RP) is that they act to facilitate the core function of the ribosome in synthesizing proteins. However, emerging evidence suggests that some RP perform regulatory functions outside of the context of the ribosome ("extra-ribosomally"). Indeed, our laboratory demonstrated that ribosomal protein, Rpl22 and its paralog Rpl22l1 (Like1), are dispensable for ribosome assembly and translation, yet they perform critical regulatory functions in hematopoiesis that are mediated by binding selected RNA targets and controlling their translation. Despite their high degree of homology, Rpl22 and Like1 antagonistically control the emergence of hematopoietic stem cells (HSC) by regulating the translation of the key transcription factor, Smad1, with Rpl22 repressing its translation and Like1 acting to oppose that translation. Here, we seek to establish the molecular basis for how such highly homologous proteins perform distinct and opposing functions. Since both Rpl22 and Like1 share highly conserved RNA-binding domains in the central core of the proteins, we hypothesize that their unique regulatory functions are likely to reside in their termini. To systematically test this hypothesis, we employed a domain-swapping approach, creating a series of Rpl22:Like1 chimeric proteins to assess which changes would confer on Like1, the Rpl22 function of blocking HSC emergence. In doing so, we utilized zebrafish as a model organism. During embryonic zebrafish development, the enforced expression of Rpl22, but not Like1, represses Smad1 expression and blocks HSC) emergence. Interestingly, our analysis of the Rpl22:Like1 chimeras revealed that transfer of the N-terminal amino acids of Rpl22 to Like1 was sufficient to confer upon Like1 the Rpl22 function of blocking HSC emergence. Moreover, this Rpl22:Like1 N-terminal chimera also was able to restore the block in T lymphocyte development observed upon loss of Rpl22, indicating that Rpl22 function in another hematopoietic process, supporting T lymphocyte development, can be conferred upon Like1 by the N-terminal sequences of Rpl22. Together, these data suggest that the unique and opposing functions of Rpl22 and Like1 reside in their N-termini. How these newly identified N-terminal amino acid sequences confer distinct biological functions on these two paralogs is unclear at present, but may involve the association with distinct co-factors. This possibility is currently under investigation. This study demonstrates that relative minor changes in amino acid sequence can have profound effects on the functions of these RP paralogs, enabling them to play divergent regulatory roles in controlling hematopoiesis. Disclosures No relevant conflicts of interest to declare.

Renilla Bioluminescence: A Morphologic Approach to the Location of Photocytes

1974 ◽  
Vol 32 ◽  
pp. 208-209
Author(s):  
Ben O. Spurlock ◽  
Milton J. Cormier
Keyword(s):  
Excited State ◽  
Ground State ◽  
Molecular Basis ◽  
Light Emission ◽  
Chemical Basis ◽  
Electronic Excited State ◽  
Colonial Form ◽  
The Common ◽  
Eighteenth And Nineteenth Centuries ◽  
Catalyzed Oxidation

The phenomenon of bioluminescence has fascinated layman and scientist alike for many centuries. During the eighteenth and nineteenth centuries a number of observations were reported on the physiology of bioluminescence in Renilla, the common sea pansy. More recently biochemists have directed their attention to the molecular basis of luminosity in this colonial form. These studies have centered primarily on defining the chemical basis for bioluminescence and its control. It is now established that bioluminescence in Renilla arises due to the luciferase-catalyzed oxidation of luciferin. This results in the creation of a product (oxyluciferin) in an electronic excited state. The transition of oxyluciferin from its excited state to the ground state leads to light emission.

Androgen-induced plasticity at a “vocal” neuromuscular synapse

1994 ◽  
Vol 52 ◽  
pp. 32-33
Author(s):  
Darcy B. Kelley ◽  
Martha L. Tobias ◽  
Mark Ellisman
Keyword(s):  
Xenopus Laevis ◽  
Motor Neurons ◽  
Sexual Differentiation ◽  
Molecular Basis ◽  
Neuromuscular Synapse ◽  
Sexually Dimorphic ◽  
Intracellular Protein ◽  
Developmental Program ◽  
Androgen Action ◽  
Clawed Frog

Brain and muscle are sexually differentiated tissues in which masculinization is controlled by the secretion of androgens from the testes. Sensitivity to androgen is conferred by the expression of an intracellular protein, the androgen receptor. A central problem of sexual differentiation is thus to understand the cellular and molecular basis of androgen action. We do not understand how hormone occupancy of a receptor translates into an alteration in the developmental program of the target cell. Our studies on sexual differentiation of brain and muscle in Xenopus laevis are designed to explore the molecular basis of androgen induced sexual differentiation by examining how this hormone controls the masculinization of brain and muscle targets.Our approach to this problem has focused on a highly androgen sensitive, sexually dimorphic neuromuscular system: laryngeal muscles and motor neurons of the clawed frog, Xenopus laevis. We have been studying sex differences at a synapse, the laryngeal neuromuscular junction, which mediates sexually dimorphic vocal behavior in Xenopus laevis frogs.

A molecular basis for opiate action

1998 ◽  
Vol 33 ◽  
pp. 65-77 ◽  
Author(s):  
Dominique Massotte ◽  
Brigitte L. Kieffer
Keyword(s):  
Molecular Basis
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