The salt-sensitive structure and zinc inhibition ofBorrelia burgdorferiprotease BbHtrA

2015 ◽  
Vol 99 (3) ◽  
pp. 586-596 ◽  
Author(s):  
Theresa M. Russell ◽  
Xiaoling Tang ◽  
Jason M. Goldstein ◽  
Dennis Bagarozzi ◽  
Barbara J. B. Johnson
Keyword(s):  
Sensitive Structure ◽  
Zinc Inhibition

A hydrogen-sensitive structure based on semi-insulating gallium arsenide

2002 ◽  
Vol 28 (4) ◽  
pp. 320-322
Author(s):  
I. A. Karpovich ◽  
S. V. Tikhov ◽  
E. L. Shobolov ◽  
B. N. Zvonkov
Keyword(s):  
Gallium Arsenide ◽  
Sensitive Structure

scholarly journals AMPA receptor inhibition by synaptically released zinc

2015 ◽  
Vol 112 (51) ◽  
pp. 15749-15754 ◽  
Author(s):  
Bopanna I. Kalappa ◽  
Charles T. Anderson ◽  
Jacob M. Goldberg ◽  
Stephen J. Lippard ◽  
Thanos Tzounopoulos
Keyword(s):  
Dorsal Cochlear Nucleus ◽  
Fine Tuning ◽  
Receptor Inhibition ◽  
Endogenous Modulator ◽  
Excitatory Neurotransmission ◽  
Zinc Levels ◽  
Zinc Inhibition ◽  
Endogenous Modulators ◽  
Activity Dependent

The vast amount of fast excitatory neurotransmission in the mammalian central nervous system is mediated by AMPA-subtype glutamate receptors (AMPARs). As a result, AMPAR-mediated synaptic transmission is implicated in nearly all aspects of brain development, function, and plasticity. Despite the central role of AMPARs in neurobiology, the fine-tuning of synaptic AMPA responses by endogenous modulators remains poorly understood. Here we provide evidence that endogenous zinc, released by single presynaptic action potentials, inhibits synaptic AMPA currents in the dorsal cochlear nucleus (DCN) and hippocampus. Exposure to loud sound reduces presynaptic zinc levels in the DCN and abolishes zinc inhibition, implicating zinc in experience-dependent AMPAR synaptic plasticity. Our results establish zinc as an activity-dependent, endogenous modulator of AMPARs that tunes fast excitatory neurotransmission and plasticity in glutamatergic synapses.

Role of specific simian virus 40 sequences in the nuclease-sensitive structure in viral chromatin

1985 ◽  
Vol 5 (1) ◽  
pp. 52-58
Author(s):  
R D Gerard ◽  
B A Montelone ◽  
C F Walter ◽  
J W Innis ◽  
W A Scott
Keyword(s):  
Simian Virus 40 ◽  
Simian Virus ◽  
Origin Of Replication ◽  
Viral Origin ◽  
Deletion Mutations ◽  
Sensitive Region ◽  
Complete Independence ◽  
Sensitive Structure ◽  
Nuclease Sensitivity

A nuclease-sensitive region forms in chromatin containing a 273-base-pair (bp) segment of simian virus 40 DNA encompassing the viral origin of replication and early and late promoters. We have saturated this region with short deletion mutations and compared the nuclease sensitivity of each mutated segment to that of an unaltered segment elsewhere in the partially duplicated mutant. Although no single DNA segment is required for the formation of a nuclease-sensitive region, a deletion mutation (dl45) which disrupted both exact copies of the 21-bp repeats substantially reduced nuclease sensitivity. Deletion mutations limited to only one copy of the 21-bp repeats had little, if any, effect. A mutant (dl135) lacking all copies of the 21- and 72-bp repeats, while retaining the origin of replication and the TATA box, did not exhibit a nuclease-sensitive region. Mutants which showed reduced nuclease sensitivity had this effect throughout the nuclease-sensitive region, not just at the site of the deletion, indicating that although multiple determinants must be responsible for the nuclease-sensitive chromatin structure they do not function with complete independence. Mutant dl9, which lacks the late portion of the 72-bp segment, showed reduced accessibility to BglI, even though the BglI site is 146 bp away from the site of the deletion.

scholarly journals High-Affinity Zinc Inhibition of NMDA NR1–NR2A Receptors

1997 ◽  
Vol 17 (15) ◽  
pp. 5711-5725 ◽  
Author(s):  
Pierre Paoletti ◽  
Philippe Ascher ◽  
Jacques Neyton
Keyword(s):  
High Affinity ◽  
Zinc Inhibition
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