Thomas P. Singer

ORCID: 0000-0003-2495-4151
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About
Contact & Profiles
Research Areas
  • Electrochemical sensors and biosensors
  • Microbial Metabolic Engineering and Bioproduction
  • Metabolism and Genetic Disorders
  • Amino Acid Enzymes and Metabolism
  • Parkinson's Disease Mechanisms and Treatments
  • Mitochondrial Function and Pathology
  • Biochemical Acid Research Studies
  • Biochemical effects in animals
  • Coenzyme Q10 studies and effects
  • Photosynthetic Processes and Mechanisms
  • Muscle metabolism and nutrition
  • Molecular Sensors and Ion Detection
  • Enzyme Catalysis and Immobilization
  • Monoclonal and Polyclonal Antibodies Research
  • Neuroscience and Neuropharmacology Research
  • Cardiac electrophysiology and arrhythmias
  • Enzyme function and inhibition
  • Biotin and Related Studies
  • Biochemical Analysis and Sensing Techniques
  • Ion channel regulation and function
  • Analytical Chemistry and Chromatography
  • Neurological disorders and treatments
  • Adipose Tissue and Metabolism
  • Pharmacogenetics and Drug Metabolism
  • Meat and Animal Product Quality

University of Bern
2020-2024

Oeschger Centre for Climate Change Research
2020-2024

Paul Scherrer Institute
2020-2024

Roche (Switzerland)
2013-2022

TU Dresden
2016-2020

Sinclair Community College
2020

First Technical University
2020

Tennessee Technological University
2020

Community College of Philadelphia
2020

University of Louisville Hospital
2020

MPTP, l-methyl-4-phenyl-l,2,3,6tetrahydropyridine; MPP+, 1-methyl-4-phenylpyridinium ion; MPDP+, l-methyl-4-phenyl-2,3,-dihydropyridinium MOPS, 3-(N-morpho1ino)propanesulfonic acid; EGTA, [ethylenebis

10.1016/s0021-9258(19)57434-8 article EN cc-by Journal of Biological Chemistry 1986-06-01

Modeling clinically relevant tissue responses using cell models poses a significant challenge for drug development, in particular induced liver injury (DILI). This is mainly because existing lack longevity and tissue-level complexity which limits their utility predictive toxicology. In this study, we established characterized novel bioprinted human mimetics comprised of patient-derived hepatocytes non-parenchymal cells defined architecture. Scaffold-free assembly different types an...

10.1371/journal.pone.0158674 article EN cc-by PLoS ONE 2016-07-07

This chapter contains sections titled: Introduction Assay of Succinate Dehydrogenase and Succinoxidase in Animal Tissues Application Assays to Yeast, Bacteria, Higher Plans NADH Oxidase Choline Mitochondrial α-Glycerophosphate

10.1002/9780470110423.ch3 article EN Methods of biochemical analysis 1974-10-28

10.1016/s0021-9258(18)50574-3 article EN cc-by Journal of Biological Chemistry 1979-06-01

10.1016/s0021-9258(18)65059-8 article EN cc-by Journal of Biological Chemistry 1956-12-01

10.1016/s0021-9258(17)41645-0 article EN cc-by Journal of Biological Chemistry 1945-01-01

Dilute solutions of sulfhydryl enzymes (phosphoglyceraldehyde dehydrogenase, adenosinetriphosphatase, succinoxidase) showed reduced activity on irradiation by small amounts x-rays. When the inhibition was partial enzyme reactivated addition glutathione. more complete, reactivation only partial. These observations are interpreted as being due to oxidation -SH groups protein products water irradiation, radicals OH and O(2)H, H(2)O(2) atomic oxygen. The irreversible which occurs when dose...

10.1085/jgp.32.4.537 article EN The Journal of General Physiology 1949-03-20

10.1016/s0076-6879(78)53050-4 article EN Methods in enzymology on CD-ROM/Methods in enzymology 1978-01-01

Abstract: Nigrostriatal cell death in 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP)‐induced Parkinson's disease results from the inhibition of mitochondrial respiration by 1‐methyl‐4‐phenylpyridinium (MPP + ). MPP blocks electron flow NADH dehydrogenase to coenzyme Q at or near same site as do rotenone and piericidin protects against binding loss activity due these inhibitors. The 4′‐analogs showed increasing affinity for with length alkyl chain, lowest K i , 4′‐heptyl‐MPP being 6 μ M...

10.1111/j.1471-4159.1991.tb11409.x article EN Journal of Neurochemistry 1991-04-01

A method has been elaborated for the large scale isolation of outer membranes beef liver mitochondria. From these monoamine oxidase was partially purified and digested with trypsin chymotrypsin to yield peptides containing riboflavin covalently linked peptide chain. pure pentapeptide riboflavin‐5′‐phosphate obtained by a series chromatographic procedures. Edman degradation, followed dansylation, revealed amino acid sequence: Ser‐Gly‐Gly‐X‐Tyr, X being which flavin is attached via 8α‐carbon...

10.1111/j.1432-1033.1971.tb19689.x article EN European Journal of Biochemistry 1971-12-01

The binding sites of rotenone, piericidin A, and Amytal in the reduced nicotinamide adenine dinucleotide oxidase chain heart have been studied with aid rotenone-6a-14C. Binding rotenone continues a linear manner beyond point maximal inhibition respiration, indicating that is tightly bound not only at specific site NADH dehydrogenase segment respiratory but also other submitochondrial particles. Unspecific by treatment particles presence bovine serum albumin (BSA) further minimized successive...

10.1016/s0021-9258(19)81741-6 article EN cc-by Journal of Biological Chemistry 1968-02-01

This chapter contains sections titled: Introduction Assay of the Primary Dehydrogenase Succinic Complex

10.1002/9780470110201.ch9 article EN Methods of biochemical analysis 1957-01-01

Abstract On the addition of NADH to submitochondrial particles in which oxidase is blocked by rotenone, piericidin A, or Amytal, g = 1.94 signal dehydrogenase appears essentially same manner as untreated preparations. However, appearance NADHinduced iron succinate and cytochromes b c1 inhibited these agents. It concluded that block oxidation on O2 side non-heme dehydrogenase.

10.1016/s0021-9258(19)81742-8 article EN cc-by Journal of Biological Chemistry 1968-02-01
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