Results 51 to 60 of about 746 (145)

Elesclomol Loaded Copper Oxide Nanoplatform Triggers Cuproptosis to Enhance Antitumor Immunotherapy

open access: yesAdvanced 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   +17 more
wiley   +1 more source

The pyruvate and α-ketoglutarate dehydrogenase complexes of Pseudomonas aeruginosa catalyze pyocyanin and phenazine-1-carboxylic acid reduction via the subunit dihydrolipoamide dehydrogenase [PDF]

open access: yes, 2017
Phenazines are a class of redox-active molecules produced by diverse bacteria and archaea. Many of the biological functions of phenazines, such as mediating signaling, iron acquisition, and redox homeostasis, derive from their redox activity.
Glasser, Nathaniel R.   +3 more
core   +1 more source

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

open access: yesAdvanced 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

Identification of miRNAs involved in pear fruit development and quality [PDF]

open access: yes, 2014
BACKGROUND: MicroRNAs (miRNAs) are a class of small, endogenous RNAs that take part in regulating genes through mediating gene expressions at the post-transcriptional level in plants.
Defu Wang   +5 more
core   +1 more source

Human skeletal muscle pyruvate dehydrogenase phosphatase activity and expression : the effect of aerobic capacity [PDF]

open access: yes, 2009
Activation of pyruvate dehydrogenase (PDH), which converts pyruvate into acetyl-CoA, is accomplished by a pair of specific phosphatases (PDP 1 & 2). A cross-sectional study investigating the effect of aerobic capacity on PDP activity and expression ...
Love, Lorenzo Kenward.
core   +1 more source

Molecular architecture of the human pyruvate dehydrogenase complex [PDF]

open access: yes, 2006
Mammalian pyruvate dehydrogenase multi-enzyme complex (PDC) is a key metabolic assembly responsible for the maintenance of glucose homeostasis. PDC comprises a central pentagonal dodecahedral core of 60 dihydrolipoamide acetyltransferase (E2) and 12 E3 ...
Smolle, Michaela
core   +1 more source

Solution structures of lipoyl domains of the 2-oxo acid dehydrogenase complexes from Azotobacter vinelandii : implications for molecular recognition [PDF]

open access: yes, 1997
The 2-oxo acid dehydrogenase complexes are large multienzyme complexes that catalyse the irreversible oxidative decarboxylation of a specific 2-oxo acid to the corresponding acyl-CoA derivative.
Berg, A.
core   +1 more source

Subunit associations in the mammalian pyruvate dehydrogenase complex. Structure and role of protein X and the pyruvate dehydrogenase component binding domain of the dihydrolipoyl transacetylase component.

open access: yesThe 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 ...
M, Rahmatullah   +5 more
openaire   +2 more sources

Studies on the mammalian pyruvate dehydrogenase complex: pyruvate dehydrogenase kinase binding sites, reductive acetylation reaction and extrinsic control [PDF]

open access: yes, 1989
Call number: LD2668 .T4 BICH 1989 L5Master of ScienceBiochemistry and Molecular Biophysics Interdepartmental ...
Li, Lin.
core  

Engineering of escherichia coli 2-oxoglutarate dehydrogenase complex with mechanistic and synthetic goals [PDF]

open access: yes, 2019
The Escherichia coli 2-oxoglutarate dehydrogenase complex (OGDHc) compromises multiple copies of three enzymes - 2-oxoglutarate dehydrogenase (E1o), dihydrolipoyl succinyltransferase (E2o), and dihydrolipoyl dehydrogenase (E3).
Chakraborty, Joydeep
core   +1 more source

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