Results 31 to 40 of about 21,893 (312)
Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy
Biomolecules, 2022 Metalloproteins are involved in key cell processes such as photosynthesis, respiration, and oxygen transport. However, the presence of transition metals (notably iron as a component of [Fe-S] clusters) often makes these proteins sensitive to oxygen ...
Mickaël V. Cherrier +8 more
doaj +1 more source
Angewandte Chemie, 2020 De Novo metalloprotein design assesses the relationship between metal active site architecture and catalytic reactivity. Herein, we use an α-helical scaffold to control the iron coordination geometry when a heme cofactor is allowed to bind to either ...
K. Koebke +7 more
semanticscholar +1 more source
Electrochemical titrations and reaction time courses monitored in situ by magnetic circular dichroism spectroscopy [PDF]
, 2011 Magnetic circular dichroism (MCD) spectra, at ultraviolet–visible or near-infrared wavelengths (185–2000 nm), contain the same transitions observed in conventional absorbance spectroscopy, but their bisignate nature and more stringent selection rules ...
Abramson +52 more
core +1 more source
Dependence of TIMP-1 plasma levels on preanalytical specimen handling [PDF]
, 2008 Background: Tissue inhibitor of metalloproteinases-1 (TIMP-1) in blood might be a helpful biomarker in various diseases. However, various authors report that TIMP-1 is dependent on preanalytical procedures.
Davis, Gerard +6 more
core +1 more source
Stealthy microbes: How Neisseria gonorrhoeae hijacks bulwarked iron during infection
Frontiers in Cellular and Infection Microbiology, 2022 Transition metals are essential for metalloprotein function among all domains of life. Humans utilize nutritional immunity to limit bacterial infections, employing metalloproteins such as hemoglobin, transferrin, and lactoferrin across a variety of ...
Julie Lynn Stoudenmire +2 more
doaj +1 more source
Design of functional metalloproteins [PDF]
Nature, 2009 Metalloproteins catalyse some of the most complex and important processes in nature, such as photosynthesis and water oxidation. An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins. Doing so not only can reveal hidden structural features that may be missing from studies of native metalloproteins and their ...
Yi Lu +3 more
openalex +5 more sources
From Zn to Mn: the study of novel manganese-binding groups in the search for new drugs against tuberculosis. [PDF]
, 2011 In most eubacteria, apicomplexans, and most plants, including the causal agents for diseases such as malaria, leprosy, and tuberculosis, the methylerythritol phosphate pathway is the route for the biosynthesis of the C(5) precursors to the essential ...
de Oliveira, César Augusto F +3 more
core +2 more sources
Molecules, 2022 Almost half of all known proteins contain metal co-factors. Crucial for the flawless performance of a metalloprotein is the selection with high fidelity of the cognate metal cation from the surrounding biological fluids.
Todor Dudev
doaj +1 more source
The Fe Protein: An Unsung Hero of Nitrogenase
Inorganics, 2018 Although the nitrogen-fixing enzyme nitrogenase critically requires both a reductase component (Fe protein) and a catalytic component, considerably more work has focused on the latter species.
Andrew J. Jasniewski +3 more
doaj +1 more source
Matrix Metalloproteinase-9 and Inflammation in Different Types of Multiple Sclerosis [PDF]
, 2016 Different clinical courses of multiple sclerosis, heterogeneity of its clinical implications, different effect of immunomodulatory therapy for the same clinical forms implies various pathogenetic mechanisms of central nervous system damage at this ...
Chernenko, M. (Maksym) +4 more
core +2 more sources