Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn
K Mosna, K Jurczak, A Krężel - Metallomics, 2023 - academic.oup.com
Abstract Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn.
K Mosna, K Jurczak, A Krężel - Metallomics: Integrated Biometal …, 2023 - europepmc.org
Abstract Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn
K Mosna, K Jurczak, A Krężel - Metallomics: integrated …, 2023 - pubmed.ncbi.nlm.nih.gov
Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all organisms,
from bacteria to humans. They participate in zinc and copper metabolism, toxic metals …
from bacteria to humans. They participate in zinc and copper metabolism, toxic metals …
Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn
K Mosna, K Jurczak, A Krężel - Metallomics, 2023 - academic.oup.com
Abstract Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
[PDF][PDF] Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn
K Mosna, K Jurczak, A Krezel - 2023 - researchgate.net
Abstract Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
[HTML][HTML] Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn
K Mosna, K Jurczak, A Krężel - Metallomics: Integrated Biometal …, 2023 - ncbi.nlm.nih.gov
Abstract Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn.
K Mosna, K Jurczak, A Krężel - Metallomics: Integrated Biometal …, 2023 - europepmc.org
Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all organisms,
from bacteria to humans. They participate in zinc and copper metabolism, toxic metals …
from bacteria to humans. They participate in zinc and copper metabolism, toxic metals …