Results 21 to 30 of about 52 (52)

Elesclomol Loaded Copper Oxide Nanoplatform Triggers Cuproptosis to Enhance Antitumor Immunotherapy

Advanced Science, Volume 11, Issue 18, May 15, 2024.
A copper oxide (CuO)‐based and copper ionophore elesclomol (ES)‐loaded nanoplatform (denoted ES@CuO) is designed to trigger immunogenic cell death via cuproptosis. Meanwhile, combined therapy with ES@CuO nanoparticles and PD‐1 synergistically remodels the immunosuppressive tumor microenvironment to significantly inhibit the growth of murine melanoma ...
Xufeng Lu, Xiaodong Chen, Chengyin Lin, Yongdong Yi, Shengsheng Zhao, Bingzi Zhu, Wenhai Deng, Xiang Wang, Zuoliang Xie, Shangrui Rao, Zhonglin Ni, Tao You, Liyi Li, Yingpeng Huang, Xiangyang Xue, Yaojun Yu, Weijian Sun, Xian Shen   +17 more
wiley   +1 more source

A Brief Review on Manipulation of Essential Metal Ions as Nanomedicine for Cancer Therapy

Advanced NanoBiomed Research, Volume 4, Issue 2, February 2024.
In this review, the latest progression of essential metal‐ion‐based nanomedicine for tumor therapy is summarized, existing challenges are addressed, and possible directions of such therapeutic strategies are proposed. Such information benefits readers a general awareness for current research status and implication of the future clinical applications ...
Lin Weng, Xin Chen
wiley   +1 more source

Sequential ¹H and ¹⁵N nuclear magnetic resonance assignments and secondary structure of the N‐terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii [PDF]

European Journal of Biochemistry, 1994
The N‐terminal lipoyl domain (79 residues) of the transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii has been sub‐cloned and produced in Escherichia coli. Over‐expression exceeds the capacity of E. coli cells to lipoylate all expressed lipoyl domain, but addition of lipoic acid to the growth medium results in ...
A. de Kok, Jacques Vervoort, A. Berg
openaire   +3 more sources

Properties of the pyruvate dehydrogenase kinase bound to and separated from the dihydrolipoyl transacetylase-protein X subcomplex and evidence for binding of the kinase to protein X.

Journal of Biological Chemistry, 1986
Studies were conducted on four pyruvate dehydrogenase kinase-containing fractions: purified pyruvate dehydrogenase complex, the dihydrolipoyl transacetylase-protein X-kinase subcomplex (E2.X.K), a kinase fraction (K fraction) prepared from the E2.X.K subcomplex, and a kinase fraction generated by limited trypsin-digestion of E2.X.K.
Gary A. Radke, Thomas E. Roche, Mohammed Rahmatullah, J. M. Jilka   +3 more
openaire   +3 more sources

α-Keto Acid Dehydrogenase Complexes [PDF]

Journal of Biological Chemistry, 1968
Dihydrolipoyl transacetylase, one of the three enzymes comprising the Escherichia coli pyruvate dehydrogenase complex, consists of 24 identical polypeptide chains that are linked by noncovalent bonds. There appear to be 3 tyrosyl residues per chain of molecular weight about 40,000.
Edith R. Schwartz, Lester J. Reed
openaire   +3 more sources

Subunit Associations in the Mammalian Pyruvate Dehydrogenase Complex

Journal of Biological Chemistry, 1989
We have further distinguished the structures and roles of the two lipoyl-bearing components of the pyruvate dehydrogenase complex, the dihydrolipoyl transacetylase (E2) component and the component designated as protein X. The amino acid sequences of the NH2-terminal regions of the lipoyl-bearing domain of the E2 component and protein X are different ...
Gary A. Radke, Christina L. Chang, P. C. Andrews, Mohammed Rahmatullah, Thomas E. Roche, S. Gopalakrishnan   +5 more
openaire   +3 more sources

α-Keto Acid Dehydrogenase Complexes

Journal of Biological Chemistry, 1967
Abstract Dihydrolipoyl transacetylase, one of three enzymes comprising the Escherichia coli pyruvate dehydrogenase complex, dissociates into subunits in acidic solutions and in the presence of sodium dodecyl sulfate at neutral pH. Dissociation of the transacetylase in dilute acetic acid solution (0.83 m, pH 2.6) produces enzymatically inactive subunits
Henry R. Henney, Charles R. Willms, Barid B. Mukherjee, Tsuyoshi Muramatsu, Lester J. Reed   +4 more
openaire   +3 more sources

Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from bovine heart. [PDF]

Journal of Biological Chemistry, 1981
Flora H. Pettit, M L Hackert, Lester J. Reed, D. M. Bleile   +3 more
openaire   +2 more sources

Structural studies on dihydrolipoyl transacetylase : the core component of the pyruvate dehydrogenase complex of Azotobacter vinelandii

The studies described in this thesis deal with the structure of the Azotobactervinelandii dihydrolipoyl transacetylase, the core component (E 2 ) of the pyruvate dehydrogenase complex. in all organisms the pyruvate dehydrogenase complex is closely related to the 2-oxoglutarate dehydrogenase complex and, if present, the branched-chain 2-oxoacid ...
openaire   +2 more sources

Alpha-keto acid dehydrogenase complexes. VI. Dissociation and reconstitution of the dihydrolipoyl transacetylase of Escherichia coli.

The Journal of biological chemistry, 1967
C R, Willms, R M, Oliver, H R, Henney, B B, Mukherjee, L J, Reed   +4 more
openaire   +1 more source