Results 11 to 20 of about 1,725 (195)

New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals [PDF]

open access: yesBiol Chem, 2022
The intracellular trafficking of mitochondrial heme presents a fundamental challenge to animal cells. This article provides some background on heme allocation, discusses some of the concepts, and then reviews research done over the last decade, much in ...
D. Stuehr   +4 more
semanticscholar   +2 more sources

Bio-Electroanalysis Performance of Heme Redox-Center for π-π Interaction Bonding of a Methylene Blue-Graphene Modified Electrode [PDF]

open access: yesNanomaterials, 2023
Hemeprotein detection has motivated extensive research on the direct reaction of a heme molecule and a redox dye. The present study used methylene blue as both donor and acceptor for a redox reaction.
Porntip Khownarumit   +5 more
doaj   +2 more sources

Chemoselective Caging of Carboxyl Groups for On‐Demand Protein Activation with Small Molecules [PDF]

open access: yesAngewandte Chemie, Volume 135, Issue 22, May 22, 2023., 2023
The caging of amino acid side chains can provide exquisite control of protein function. The first chemical caging of carboxyl groups (Asp and Glu) in enzymic active sites is reported. Caging of a heme propionate in a protein was also feasible by this approach based on esterification with a tuned diazo compound.
Yana D. Petri   +2 more
wiley   +3 more sources

Rhabdomyolysis as cause, consequence, or mimicker of myocardial infarction: A case report [PDF]

open access: yesClinical Case Reports, Volume 11, Issue 11, November 2023., 2023
Key Clinical Message A timely diagnosis is essential to start appropriate therapy and to reduce risks of life‐threatening complications of rhabdomyolysis. Some cases can undergo differential diagnosis with other clinical conditions, e.g., myocardial infarction.
Marina Nasello   +11 more
wiley   +2 more sources

Hsp90 in Human Diseases: Molecular Mechanisms to Therapeutic Approaches [PDF]

open access: yesCells, 2022
The maturation of hemeprotein dictates that they incorporate heme and become active, but knowledge of this essential cellular process remains incomplete. Studies on chaperon Hsp90 has revealed that it drives functional heme maturation of inducible nitric
Mamta P. Sumi, Arnab Ghosh
doaj   +2 more sources

Behind the Optimization of the Sensor Film: Bioconjugation of Triangular Gold Nanoparticles with Hemoproteins for Sensitivity Enhancement of Enzymatic Biosensors [PDF]

open access: yesBiosensors, 2023
Electrochemical biosensors are widely used in a multitude of applications, such as medical, nutrition, research, among other fields. These sensors have been historically used and have not undergone many changes in terms of the involved electrochemical ...
Miriam Chávez   +6 more
doaj   +2 more sources

The Histone Chaperones SET/TAF‐1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c‐Dependent Manner [PDF]

open access: yesAdvanced Science, Volume 10, Issue 29, October 17, 2023., 2023
This study focuses on the molecular action of two histone chaperones: SET/template‐activating factor‐Iβ and nucleophosmin 1. It is shown how these chaperones have specificity for fully dismantled nucleosomes, characterized the histone eviction (removal) process, and its modulation by cytochrome c.
Pedro Buzón   +5 more
wiley   +2 more sources

Evolutionary Pro‐To‐Thr Mutation in the Intrinsically Disordered Domain of ANP32 Family Members Modulates Their Target Binding Modes [PDF]

open access: yesAdvanced Science, Volume 12, Issue 12, March 27, 2025.
Protein evolution usually lies on mutations at disordered domains to promote novel functions and regulations. Here it is demonstrated that this is the case of ANP32A and ANP32B, two paralogs with apparently similar structures and functions, where a single amino‐acid substitution in the disordered domain triggers the extended‐to‐compact conformational ...
Blanca Baños‐Jaime   +8 more
wiley   +2 more sources

Phosphorylation of cytochrome c at tyrosine 48 finely regulates its binding to the histone chaperone SET/TAF‐Iβ in the nucleus [PDF]

open access: yesProtein Science, Volume 33, Issue 12, December 2024.
Abstract Post‐translational modifications (PTMs) of proteins are ubiquitous processes present in all life kingdoms, involved in the regulation of protein stability, subcellular location and activity. In this context, cytochrome c (Cc) is an excellent case study to analyze the structural and functional changes induced by PTMS as Cc is a small ...
Joaquin Tamargo‐Azpilicueta   +7 more
wiley   +2 more sources

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries [PDF]

open access: greenAntioxidants & Redox Signaling, 2010
Historically, hydrogen sulfide (H(2)S) has been regarded as a poisonous gas, with a wide spectrum of toxic effects. However, like ·NO and CO, H(2)S is now referred to as a signaling gas involved in numerous physiological processes. The list of reports highlighting the physiological effects of H(2)S is rapidly expanding and several drug candidates are ...
Ruth Pietri   +2 more
openalex   +4 more sources

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