Superoxide Dismutase Isozymes in Different Human Tissues, Their Genetic Control and Intracellular Localization

1973 ◽  
Vol 23 (4) ◽  
pp. 338-345 ◽  
Author(s):  
Gunhild Beckman ◽  
E. Lundgren ◽  
A. Tärnvik
Keyword(s):  
Superoxide Dismutase ◽  
Genetic Control ◽  
Intracellular Localization ◽  
Human Tissues

The levels of superoxide dismutase and catalase in human tissues as determined immunochemically

1973 ◽  
Vol 46 (2) ◽  
pp. 125-132 ◽  
Author(s):  
J.W. Hartz ◽  
S. Funakoshi ◽  
H.F. Deutsch
Keyword(s):  
Superoxide Dismutase ◽  
Human Tissues

Genetic control and intracellular localization of glutamate oxaloacetic transaminase in maize

1975 ◽  
Vol 13 (11-12) ◽  
pp. 759-769 ◽  
Author(s):  
John G. Scandalios ◽  
John C. Sorenson ◽  
Lila A. Ott
Keyword(s):  
Genetic Control ◽  
Intracellular Localization ◽  
Glutamate Oxaloacetic Transaminase

Intracellular localization of superoxide dismutase and its relation to the distribution and mechanism of hydrogen peroxide-producing enzymes

1973 ◽  
Vol 321 (1) ◽  
pp. 98-102 ◽  
Author(s):  
G. Rotillo ◽  
L. Calabrese ◽  
A. Finazzi Agrò ◽  
M.P. Argento-Cerù ◽  
F. Autuori ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Intracellular Localization

scholarly journals The molecular basis, genetic control and pleiotropic effects of local gene co-expression

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Diogo M. Ribeiro ◽  
Simone Rubinacci ◽  
Anna Ramisch ◽  
Robin J. Hofmeister ◽  
Emmanouil T. Dermitzakis ◽  
...  
Keyword(s):  
Gene Expression ◽  
Genetic Control ◽  
Molecular Basis ◽  
Molecular Mechanisms ◽  
Gene Interactions ◽  
Human Tissues ◽  
Public Database ◽  
Functional Interpretation ◽  
Molecular Assays ◽  
Gene Pairs

AbstractNearby genes are often expressed as a group. Yet, the prevalence, molecular mechanisms and genetic control of local gene co-expression are far from being understood. Here, by leveraging gene expression measurements across 49 human tissues and hundreds of individuals, we find that local gene co-expression occurs in 13% to 53% of genes per tissue. By integrating various molecular assays (e.g. ChIP-seq and Hi-C), we estimate the ability of several mechanisms, such as enhancer-gene interactions, in distinguishing gene pairs that are co-expressed from those that are not. Notably, we identify 32,636 expression quantitative trait loci (eQTLs) which associate with co-expressed gene pairs and often overlap enhancer regions. Due to affecting several genes, these eQTLs are more often associated with multiple human traits than other eQTLs. Our study paves the way to comprehend trait pleiotropy and functional interpretation of QTL and GWAS findings. All local gene co-expression identified here is available through a public database (https://glcoex.unil.ch/).

Studies on the expression of Cu,Zn superoxide dismutase in human tissues during development

1988 ◽  
Vol 964 (2) ◽  
pp. 260-265 ◽  
Author(s):  
Richard C. Strange ◽  
William Cotton ◽  
Anthony A. Fryer ◽  
Roger Drew ◽  
Arthur R. Bradwell ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Human Tissues

scholarly journals The molecular basis, genetic control and pleiotropic effects of local gene co-expression

2020 ◽  
Author(s):  
Diogo M. Ribeiro ◽  
Simone Rubinacci ◽  
Anna Ramisch ◽  
Robin J. Hofmeister ◽  
Emmanouil T. Dermitzakis ◽  
...  
Keyword(s):  
Gene Expression ◽  
Genetic Control ◽  
Gene Targeting ◽  
Molecular Basis ◽  
Molecular Mechanisms ◽  
Human Tissues ◽  
Functional Interpretation ◽  
Molecular Assays ◽  
Gene Pairs ◽  
Extensive Search

Nearby genes are often expressed as a group. Yet, the prevalence, molecular mechanisms and genetic control of local gene co-expression are far from being understood. Here, by leveraging gene expression measurements across 49 human tissues and hundreds of individuals, we found that local gene co-expression occurs in 13% to 53% genes per tissue. By integrating various molecular assays (e.g. ChIP-seq and Hi-C), we estimated the ability of several mechanisms, such as enhancer-gene targeting, in distinguishing gene pairs that are co-expressed from those that are not. Notably, we identified 32,636 expression quantitative trait loci (eQTLs) which associate to co-expressed gene pairs and often overlap enhancer regions. Due to affecting several genes, these eQTLs are more often associated with multiple human traits than other eQTLs. Our extensive search for local gene co-expression opens the way to comprehend trait pleiotropy and comorbidity and provide functional interpretation of QTL and GWAS findings.

scholarly journals Intracellular localization, isolation and characterization of two distinct varieties of superoxide dismutase from Neurospora crassa

1980 ◽  
Vol 187 (2) ◽  
pp. 321-328 ◽  
Author(s):  
Landis E. A. Henry ◽  
Richard Cammack ◽  
Jean-Paul Schwitzguebel ◽  
John M. Palmer ◽  
David O. Hall
Keyword(s):  
Superoxide Dismutase ◽  
Neurospora Crassa ◽  
Analytical Ultracentrifugation ◽  
Intracellular Localization ◽  
Total Activity ◽  
Superoxide Dismutases ◽  
Intermembrane Space ◽  
Matrix Space ◽  
Isolation And Characterization ◽  
High Yields

1. Neurospora crassa was found to contain two distinct superoxide dismutases. 2. Most of the activity is associated with the cytosolic fraction and was shown to be the Cu/Zn-containing form of the protein. 3. Mitochondria isolated from Neurospora crassa showed two distinct superoxide dismutases: a cyanide-sensitive Cu/Zn-containing protein and a cyanide-insensitive form which probably contains manganese. 4. Localization experiments, using selective marker enzymes and digitonin fractionation, indicated that the cyanide-sensitive form is localized in the intermembrane space, whereas the cyanide-insensitive form is confined to the mitochondrial matrix space. 5. The cytosolic Cu/Zn-containing superoxide dismutase was isolated in high yields and extensively characterized by using e.p.r. spectroscopy, isoelectric focusing and analytical ultracentrifugation. 6. E.p.r. spectroscopy was used to monitor changes in the copper environment of the native protein after the addition of a number of potential inhibitors and after high-pH treatment. 7. Both of the cyanide-sensitive Cu/Zn-containing enzymes (cytosolic and mitochondrial) appeared to have identical properties which in turn were different from the cyanide-insensitive enzyme. 8. It is probable that the cyanide-insensitive enzyme was not previously detected, owing to its low amount (less than 10% of the total activity), greater lability than the cyanide-sensitive enzyme and the necessity of obtaining a mitochondrial-enriched fraction before its isolation.

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