Results 41 to 50 of about 10,826 (186)

Human 2-Oxoglutarate Dehydrogenase Complex E1 Component Forms a Thiamin-derived Radical by Aerobic Oxidation of the Enamine Intermediate. [PDF]

, 2014
Herein are reported unique properties of the human 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc), a rate-limiting enzyme in the Krebs (citric acid) cycle.
Ambrus, Attila, Gerfen, Gary, Nemeria, Natalia S., Patel, Hetalben, Tretter, László, Ádám, Veronika   +5 more
core   +4 more sources

Nucleotide sequence for yeast dihydrolipoamide dehydrogenase. [PDF]

Proceedings of the National Academy of Sciences, 1988
Rabbit antiserum to the dihydrolipoamide dehydrogenase (dihydrolipoamide:NAD+ oxidoreductase, EC 1.8.1.4) component of the pyruvate dehydrogenase complex from bakers' yeast was used to screen plaques produced by a lambda gt11 yeast cDNA library.
K S, Browning, D J, Uhlinger, L J, Reed
openaire   +2 more sources

Development of Recombinant Dihydrolipoamide Dehydrogenase Subunit Vaccine against Vibrio Infection in Large Yellow Croaker

Fishes, 2022
Large yellow croaker (Larimichthys crocea), an economically important marine fish in China, has suffered from serious vibriosis, which has resulted in great economic losses for the large yellow croaker industry.
Xiaomeng Li, Yuanzhen Tan, Zheng Zhang, Yupeng Huang, Pengfei Mu, Zhengwei Cui, Xinhua Chen   +6 more
doaj   +1 more source

Characterization and epitope mapping of human monoclonal antibodies to PDC-E2, the immunodominant autoantigen of primary biliary cirrhosis [PDF]

, 1992
Further to define the epitopes of PDC-E2, the major autoantigen in primary biliary cirrhosis (PBC), we have developed and characterized five human monoclonal antibodies. These antibodies were derived by fusing a regional hepatic lymph node from a patient
Bassendine, Baum, Casali, Chambers, Coppel, Coppel, Cram, Flannery, Fregeau, Fregeau, Fujikura, Fusey, Fussey, Gershwin, Gershwin, Griffin, Griffin, James, Kaplan, Kunicki, Larrick, Leung, Leung, Mackay, Mackay, Mathews, McNeilage, Okamoto, Pollack, Ramsden, Reeves, Reimer, Robbins, Rokeach, Rowley, Ruther, Salemuddin, Sturgess, Sudin, Surh, Surh, Surh, Surh, Tan, Uibo, Van de Water, Van de Water, Van de Water, Van de Water, Williams   +49 more
core   +1 more source

Alterations of the mitochondrial proteome caused by the absence of mitochondrial DNA: A proteomic view [PDF]

, 2006
The proper functioning of mitochondria requires that both the mitochondrial and the nuclear genome are functional. To investigate the importance of the mitochondrial genome, which encodes only 13 subunits of the respiratory complexes, the mitochondrial ...
Abdul, Appleby, Armstrong, Bai, Bourges, Buchet, Chai, Claros, Da Cruz, Dey, Du, Garcia, Gianazza, Joseph, King, King, Lescuyer, Luche, Manjasetty, Martinus, Perkins, Rabilloud, Rabilloud, Rabilloud, Rabilloud, Rabilloud, Santoni, Sharma, Sharp, Sherer, Singh, Sinha, Suzuki, Tastet, Taylor, Tryoen-Toth, Ugalde, Wiedemann, Zamzami, Zischka   +39 more
core   +4 more sources

Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis [PDF]

, 2013
Metabolic control of gene expression coordinates the levels of specific gene products to meet cellular demand for their activities. This control can be exerted by metabolites acting as regulatory signals and/or a class of metabolic enzymes with dual ...
Bohne, Alexandra-Viola, Lidschreiber, Michael, Nickelsen, Jörg, Piotrowski, Markus, Schottkowski, Marco, Schwarz, Christian, Zerges, William   +6 more
core   +3 more sources

Protein–protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase [PDF]

Structure, 1996
The ubiquitous pyruvate dehydrogenase multienzyme complex is built around an octahedral or icosahedral core of dihydrolipoamide acetyltransferase (E2) chains, to which multiple copies of pyruvate decarboxylase (E1) and dihydrolipoamide dehydrogenase (E3) bind tightly but non-covalently.
Mande, Sharmila S, Sarfaty, Steve, Allen, Mark D, Perham, Richard N, Hol, Wim GJ   +4 more
openaire   +2 more sources

Disruption of Mitochondrial Dynamics and Integrity Drives Divergent Metabolic Flexibility and Resilience in Podocytes. [PDF]

FASEB J
We investigated two models of mitochondrial dysfunction in podocytes, using two cell culture models: podocytes isolated from mice with Oma1 deletion (Oma1del) and mouse podocytes modified with an inducible knockdown of PHB2 (Phb2kd). OMA1 deficiency induced a glycolytic shift, enhanced glutamine anaplerosis, and sustained energy homeostasis after ...
Özel C, Reitmeier KM, Kieckhöfer E, Abualia K, Nguyen-Minh D, Matin M, Hagmann H, Coward RJM, Brähler S, Antczak P, Schermer B, Benzing T, Giavalisco P, Brinkkoetter PT.   +13 more
europepmc   +2 more sources

Reversible inactivation of dihydrolipoamide dehydrogenase by mitochondrial hydrogen peroxide. [PDF]

Free Radic Res, 2013
Under oxidative stress conditions, mitochondria are the major site for cellular production of reactive oxygen species (ROS) such as superoxide anion and H2O2 that can attack numerous mitochondrial proteins including dihydrolipoamide dehydrogenase (DLDH).
Yan LJ, Sumien N, Thangthaeng N, Forster MJ.   +3 more
europepmc   +4 more sources

The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens [PDF]

FEMS Microbiology Letters, 2008
A dihydrolipoamide dehydrogenase (DLDH) was purified and characterized for the first time from a crenarchaeon, Acidianus ambivalens. The holoenzyme consists of two identical subunits with a molecular mass of 45.4 kDa per monomer. It contains FAD as a prosthetic group and uses NAD+ as the preferential substrate, but can also reduce NADP+.
Ana P. Batista, Arnulf Kletzin, Manuela M. Pereira   +2 more
openaire   +2 more sources