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Single Domain Metallothioneins: Supermetalation of Human MT 1a
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/chem.200802105openalex-snapshot
The Correlation of 113 Cd NMR and 111m Cd PAC Spectroscopies Provides a Powerful Approach for the Characterization of the Structure of Cd II ‐Substituted Zn II Proteins
inferredcites →https://doi.org/10.1002/jnr.22342openalex-snapshot
The comparison of mouse full metallothionein‐1 versus α and β domains and metallothionein‐1‐to‐3 mutation following traumatic brain injury reveals different biological motifs
inferredcites →https://doi.org/10.1002/mas.20247openalex-snapshot
Electrospray: From ions in solution to ions in the gas phase, what we know now
inferredcites →https://doi.org/10.1006/taap.1996.0011openalex-snapshot
Induction of Metallothionein mRNA and Protein in Murine Astrocyte Cultures
inferredcites →https://doi.org/10.1006/taap.1996.0253openalex-snapshot
Induction of Metallothionein mRNA and Protein in Primary Murine Neuron Cultures
inferredcites →https://doi.org/10.1006/taap.1997.8321openalex-snapshot
Ectopic Expression of Metallothionein-III Causes Pancreatic Acinar Cell Necrosis in Transgenic Mice
inferredcites →https://doi.org/10.1007/s00775-003-0481-4openalex-snapshot
Is Ag(I) an adequate probe for Cu(I) in structural copper–metallothionein studies?
inferredcites →https://doi.org/10.1007/s00775-006-0187-5openalex-snapshot
Probing structural changes in the α and β domains of copper- and silver-substituted metallothionein by emission spectroscopy and electrospray ionization mass spectrometry
inferredcites →https://doi.org/10.1007/s00775-009-0557-xopenalex-snapshot
Reaction of human metallothionein-3 with cisplatin and transplatin
inferredcites →https://doi.org/10.1007/s00775-011-0801-zopenalex-snapshot
Structural features specific to plant metallothioneins
inferredcites →https://doi.org/10.1007/s00775-011-0802-yopenalex-snapshot
Metallothionein and brain inflammation
inferredcites →https://doi.org/10.1007/s007750050276openalex-snapshot
Identification of a four copper folding intermediate in mammalian copper metallothionein by electrospray ionization mass spectrometry
inferredcites →https://doi.org/10.1016/0022-2836(88)90106-4openalex-snapshot
Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy
inferredcites →https://doi.org/10.1016/0022-2836(88)90644-4openalex-snapshot
Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
inferredcites →https://doi.org/10.1016/0022-2836(90)90291-sopenalex-snapshot
Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy
inferredcites →https://doi.org/10.1016/0022-2836(91)80126-fopenalex-snapshot
Refined crystal structure of Cd, Zn metallothionein at 2·0 Å resolution
inferredcites →https://doi.org/10.1016/0022-2836(92)90930-iopenalex-snapshot
Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy
inferredcites →https://doi.org/10.1016/0076-6879(91)05078-aopenalex-snapshot
[2] Definitions and nomenclature of metallothioneins
inferredcites →https://doi.org/10.1016/0896-6273(91)90272-2openalex-snapshot
The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
inferredcites →https://doi.org/10.1016/j.bbrc.2004.03.183openalex-snapshot
Cu+ distribution in metallothionein fragments
inferredcites →https://doi.org/10.1016/j.bbrc.2005.04.170openalex-snapshot
Metallothionein transfers zinc to mitochondrial aconitase through a direct interaction in mouse hearts
inferredcites →https://doi.org/10.1016/j.bbrc.2008.05.142openalex-snapshot
Noncooperative cadmium(II) binding to human metallothionein 1a
inferredcites →https://doi.org/10.1016/j.bbrc.2010.04.053openalex-snapshot
Bismuth binding studies to the human metallothionein using electrospray mass spectrometry
inferredcites →https://doi.org/10.1016/j.bbrc.2010.09.010openalex-snapshot
Arsenic transfer between metallothionein proteins at physiological pH
inferredcites →https://doi.org/10.1016/j.febslet.2005.12.099openalex-snapshot
Solution structure and dynamics of human metallothionein‐3 (MT‐3)
inferredcites →https://doi.org/10.1016/j.marenvres.2004.03.082openalex-snapshot
Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein
inferredcites →https://doi.org/10.1016/s0014-5793(02)03169-1openalex-snapshot
Evidence for non‐isostructural replacement of Zn2+ with Cd2+ in the β‐domain of brain‐specific metallothionein‐3
inferredcites →https://doi.org/10.1016/s0021-9258(18)33506-3openalex-snapshot
113Cd NMR study of a metallothionein fragment. Evidence for a two-domain structure.
inferredcites →https://doi.org/10.1016/s0021-9258(18)61226-8openalex-snapshot
Cadmium binding to metallothioneins. Domain specificity in reactions of alpha and beta fragments, apometallothionein, and zinc metallothionein with Cd2+.
inferredcites →https://doi.org/10.1016/s0021-9258(18)89027-5openalex-snapshot
Distinct metal-binding configurations in metallothionein.
inferredcites →https://doi.org/10.1016/s0021-9258(19)68184-6openalex-snapshot
Evidence for site-selective metal binding in calf liver metallothionein.
inferredcites →https://doi.org/10.1016/s0162-0134(00)80083-5openalex-snapshot
113Cd nmr study of the metal cluster structure of human liver metallothionein
inferredcites →https://doi.org/10.1016/s1387-3806(02)00588-2openalex-snapshot
Origin and number of charges observed on multiply-protonated native proteins produced by ESI
inferredcites →https://doi.org/10.1021/bi00189a029openalex-snapshot
Induction of a New Metallothionein Isoform (MT-IV) Occurs during Differentiation of Stratified Squamous Epithelia
inferredcites →https://doi.org/10.1021/bi00393a049openalex-snapshot
Cadmium-thiolate clusters in metallothionein: spectrophotometric and spectropolarimetric features
inferredcites →https://doi.org/10.1021/bi0205956openalex-snapshot
Structural Consequences of Metallothionein Dimerization: Solution Structure of the Isolated Cd4-α-Domain and Comparison with the Holoprotein Dimer
inferredcites →https://doi.org/10.1021/bi025664vopenalex-snapshot
Brain-Specific Metallothionein-3 Has Higher Metal-Binding Capacity than Ubiquitous Metallothioneins and Binds Metals Noncooperatively
inferredcites →https://doi.org/10.1021/bi1003537openalex-snapshot
Supermetalation of the β Domain of Human Metallothionein 1a
inferredcites →https://doi.org/10.1021/bi801253xopenalex-snapshot
Interaction of Metallothionein-2 with Platinum-Modified 5′-Guanosine Monophosphate and DNA
inferredcites →https://doi.org/10.1021/bi900366popenalex-snapshot
Effects of Zn2+, Ca2+, and Mg2+ on the Structure of Zn7Metallothionein-3: Evidence for an Additional Zinc Binding Site
inferredcites →https://doi.org/10.1021/bi961401nopenalex-snapshot
111Cd NMR Studies of the Domain Specificity of Ag+ and Cu+ Binding to Metallothionein
inferredcites →https://doi.org/10.1021/bi9913000openalex-snapshot
MRE-Binding Transcription Factor-1: Weak Zinc-Binding Finger Domains 5 and 6 Modulate the Structure, Affinity, and Specificity of the Metal-Response Element Complex
inferredcites →https://doi.org/10.1021/ic00096a046openalex-snapshot
Luminescence Probe of Copper-Thiolate Cluster Formation within Mammalian Metallothionein
inferredcites →https://doi.org/10.1021/ic048871nopenalex-snapshot
XAFS Spectral Analysis of the Cadmium Coordination Geometry in Cadmium Thiolate Clusters in Metallothionein
inferredcites →https://doi.org/10.1021/ja01574a064openalex-snapshot
A CADMIUM PROTEIN FROM EQUINE KIDNEY CORTEX
inferredcites →https://doi.org/10.1021/ja062914copenalex-snapshot
Arsenic Binding to Human Metallothionein
inferredcites →https://doi.org/10.1021/ja071979sopenalex-snapshot
Dual Nanomolar and Picomolar Zn(II) Binding Properties of Metallothionein
inferredcites →https://doi.org/10.1021/ja8060326openalex-snapshot
Kinetic Analysis of Arsenic−Metalation of Human Metallothionein: Significance of the Two-Domain Structure
inferredcites →https://doi.org/10.1021/jm070271lopenalex-snapshot
Reaction of Zn7Metallothionein with cis- and trans-[Pt(N-donor)2Cl2] Anticancer Complexes: trans-PtII Complexes Retain Their N-Donor Ligands
inferredcites →https://doi.org/10.1038/nchembio.89openalex-snapshot
Metal swap between Zn7-metallothionein-3 and amyloid-β–Cu protects against amyloid-β toxicity
inferredcites →https://doi.org/10.1039/b909185hopenalex-snapshot
Reactivity of an antimetastatic organometallic ruthenium compound with metallothionein-2: relevance to the mechanism of action
inferredcites →https://doi.org/10.1039/c0mt00102copenalex-snapshot
The “magic numbers” of metallothionein
inferredcites →https://doi.org/10.1073/pnas.0408254101openalex-snapshot
The crystal structure of yeast copper thionein: The solution of a long-lasting enigma
inferredcites →https://doi.org/10.1073/pnas.171120098openalex-snapshot
A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity
inferredcites →https://doi.org/10.1073/pnas.94.6.2233openalex-snapshot
Coordination dynamics of biological zinc “clusters” in metallothioneins and in the DNA-binding domain of the transcription factor Gal4
inferredcites →https://doi.org/10.1074/jbc.m106517200openalex-snapshot
Conformational Heterogeneity in the C-terminal Zinc Fingers of Human MTF-1
inferredcites →https://doi.org/10.1110/ps.8.12.2630openalex-snapshot
Three‐dimensional solution structure of mouse [Cd7]‐metallothionein‐l by homonuclear and heteronuclear NMR spectroscopy
inferredcites →https://doi.org/10.1110/ps.9.2.395openalex-snapshot
Electrospray ionization mass spectrometry of zinc, cadmium, and copper metallothioneins: Evidence for metal‐binding cooperativity
inferredcites →https://doi.org/10.1111/j.1742-4658.2007.05762.xopenalex-snapshot
Evidence for noncooperative metal binding to the α domain of human metallothionein
inferredcites →https://doi.org/10.1111/j.1742-4658.2008.06375.xopenalex-snapshot
Metal exchange in metallothioneins – a novel structurally significant Cd5 species in the alpha domain of human metallothionein 1a
inferredcites →https://doi.org/10.1111/j.1742-4658.2010.07667.xopenalex-snapshot
The two Caenorhabditis elegans metallothioneins (CeMT‐1 and CeMT‐2) discriminate between essential zinc and toxic cadmium
inferredcites →https://doi.org/10.1124/dmd.31.7.916openalex-snapshot
KINETIC STUDY ON THE REACTION OF CISPLATIN WITH METALLOTHIONEIN
inferredcites →https://doi.org/10.1126/science.221.4616.1141openalex-snapshot
Cadmium-113 Magnetic Resonance Spectroscopy
inferredcites →https://doi.org/10.1128/mcb.23.23.8471-8485.2003openalex-snapshot
Activity of Metal-Responsive Transcription Factor 1 by Toxic Heavy Metals and H2O2 In Vitro Is Modulated by Metallothionein
inferredcites →https://doi.org/10.1139/v07-111openalex-snapshot
Characterization of the conformational changes in recombinant human metallothioneins using ESI-MS and molecular modeling
inferredcites →https://doi.org/10.2174/092986709787458452openalex-snapshot
Metallothioneins and Platinum(II) Anti-Tumor Compounds
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4654986openalex-extracted
Joint Forces of Mass Spectrometric Techniques (Icp-Ms and Maldi-Tof-Ms) and Fluorescence Spectrometry in the Study of Platinum-Based Cytostatic Drugs Interactions with Metallothionein Mt2 and Mt3
inferred← citeshttps://doi.org/10.1002/chem.202304216openalex-snapshot
Bi(III) Binding Stoichiometry and Domain‐Specificity Differences Between Apo and Zn(II)‐bound Human Metallothionein 1a
inferred← citeshttps://doi.org/10.1002/pmic.201300496openalex-snapshot
The role of metallothionein interactions with other proteins
inferred← citeshttps://doi.org/10.1016/b978-0-12-409547-2.10947-3openalex-snapshot
Application of Heteronuclear NMR Spectroscopy to Bioinorganic and Medicinal Chemistry ☆
inferred← citeshttps://doi.org/10.1016/j.bbrc.2012.08.136openalex-snapshot
Modeling the Zn2+ and Cd2+ metalation mechanism in mammalian metallothionein 1a
inferred← citeshttps://doi.org/10.1016/j.bbrc.2017.08.137openalex-snapshot
Zinc binds non-cooperatively to human liver metallothionein 2a at physiological pH
inferred← citeshttps://doi.org/10.1016/j.bios.2013.09.008openalex-snapshot
Simultaneous detection of multiple DNA targets based on encoding metal ions
inferred← citeshttps://doi.org/10.1016/j.chemosphere.2020.129136openalex-snapshot
Identification of a new function of metallothionein-like gene OsMT1e for cadmium detoxification and potential phytoremediation
inferred← citeshttps://doi.org/10.1016/j.jbc.2023.102899openalex-snapshot
Apo-metallothionein-3 cooperatively forms tightly compact structures under physiological conditions
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2013.01.005openalex-snapshot
Lessons on the critical interplay between zinc binding and protein structure and dynamics
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2023.112392openalex-snapshot
Supermetalation of Cd-MT3 beyond the two-domain model
inferred← citeshttps://doi.org/10.1016/j.talanta.2024.125920openalex-snapshot
Joint forces of mass spectrometric techniques (ICP-MS and MALDI-TOF-MS) and fluorescence spectrometry in the study of platinum-based cytostatic drugs interactions with metallothionein MT2 and MT3
inferred← citeshttps://doi.org/10.1021/ac303522hopenalex-snapshot
Combining Chemical Labeling, Bottom-Up and Top-Down Ion-Mobility Mass Spectrometry To Identify Metal-Binding Sites of Partially Metalated Metallothionein
inferred← citeshttps://doi.org/10.1021/acs.analchem.0c00829openalex-snapshot
Ag+ Ion Binding to Human Metallothionein-2A Is Cooperative and Domain Specific
inferred← citeshttps://doi.org/10.1021/acs.inorgchem.2c03088openalex-snapshot
Homo- and Heteronuclear Group 12 Metallothionein Type B Cluster Analogs: Synthesis, Structure, 1H NMR and ESI-MS
inferred← citeshttps://doi.org/10.1021/bi3004523openalex-snapshot
Noncooperative Metalation of Metallothionein 1a and Its Isolated Domains with Zinc
inferred← citeshttps://doi.org/10.1021/bi400021bopenalex-snapshot
Single-Domain Metallothioneins: Evidence of the Onset of Clustered Metal Binding Domains in Zn-rhMT 1a
inferred← citeshttps://doi.org/10.1021/jacs.2c13578openalex-snapshot
Structural Role of Cadmium and Zinc in Metallothionein Oxidation by Hydrogen Peroxide: The Resilience of Metal–Thiolate Clusters
inferred← citeshttps://doi.org/10.1039/c3mt00216kopenalex-snapshot
Challenging conventional wisdom: single domain metallothioneins
inferred← citeshttps://doi.org/10.1039/c5mt00225gopenalex-snapshot
Defining the metal binding pathways of human metallothionein 1a: balancing zinc availability and cadmium seclusion
inferred← citeshttps://doi.org/10.1039/c7dt03319bopenalex-snapshot
Unravelling the mechanistic details of metal binding to mammalian metallothioneins from stoichiometric, kinetic, and binding affinity data
inferred← citeshttps://doi.org/10.1039/c7mt00041copenalex-snapshot
Stepwise copper( i ) binding to metallothionein: a mixed cooperative and non-cooperative mechanism for all 20 copper ions
inferred← citeshttps://doi.org/10.1039/d0mt00023jopenalex-snapshot
Metallothionein Cd4S11 cluster formation dominates in the protection of carbonic anhydrase
inferred← citeshttps://doi.org/10.1039/d2an01556kopenalex-snapshot
An ion mobility-mass spectrometry study of copper-metallothionein-2A: binding sites and stabilities of Cu-MT and mixed metal Cu–Ag and Cu–Cd complexes
inferred← citeshttps://doi.org/10.1073/pnas.1620987114openalex-snapshot
Mass spectrometric identification of intermediates in the O 2 -driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR
inferred← citeshttps://doi.org/10.1093/biomethods/bpy015openalex-snapshot
Generation of 34S-substituted protein-bound [4Fe-4S] clusters using 34S-L-cysteine
inferred← citeshttps://doi.org/10.1093/mtomcs/mfad056openalex-snapshot
Metallothionein-3 and carbonic anhydrase metalation properties with Zn(II) and Cd(II) change as a result of protein–protein interactions
inferred← citeshttps://doi.org/10.1093/nar/gkad1043openalex-snapshot
MAJIQlopedia: an encyclopedia of RNA splicing variations in human tissues and cancer
inferred← citeshttps://doi.org/10.1111/febs.12731openalex-snapshot
In vivo‐folded metal–metallothionein 3 complexes reveal the Cu–thionein rather than Zn–thionein character of this brain‐specific mammalian metallothionein
inferred← citeshttps://doi.org/10.3389/fnagi.2017.00300openalex-snapshot
Serum Copper, Zinc, and Iron Levels in Patients with Alzheimer's Disease: A Meta-Analysis of Case-Control Studies
inferred← citeshttps://doi.org/10.3390/biom10081176openalex-snapshot
The Role of Fe, Zn, and Cu in Pregnancy
inferred← citeshttps://doi.org/10.3390/ijms17010065openalex-snapshot
Earthworm Lumbricus rubellus MT-2: Metal Binding and Protein Folding of a True Cadmium-MT
inferred← citeshttps://doi.org/10.3390/ijms18050913openalex-snapshot
Residue Modification and Mass Spectrometry for the Investigation of Structural and Metalation Properties of Metallothionein and Cysteine-Rich Proteins
inferred← citeshttps://doi.org/10.3390/ijms18061237openalex-snapshot
The Functions of Metamorphic Metallothioneins in Zinc and Copper Metabolism
inferred← citeshttps://doi.org/10.3390/ijms21165697openalex-snapshot
Interplay between Carbonic Anhydrases and Metallothioneins: Structural Control of Metalation
inferred← citeshttps://doi.org/10.3390/ijms21239003openalex-snapshot
The Function of Transthyretin Complexes with Metallothionein in Alzheimer’s Disease
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