Relevant bibliographies by topics / Protein metalation

Academic literature on the topic 'Protein metalation'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Protein metalation"

1

Foster, Andrew W., Tessa R. Young, Peter T. Chivers, and Nigel J. Robinson. "Protein metalation in biology." Current Opinion in Chemical Biology 66 (February 2022): 102095. http://dx.doi.org/10.1016/j.cbpa.2021.102095.

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Wong, Daisy L., Amelia T. Yuan, Natalie C. Korkola, and Martin J. Stillman. "Interplay between Carbonic Anhydrases and Metallothioneins: Structural Control of Metalation." International Journal of Molecular Sciences 21, no. 16 (August 9, 2020): 5697. http://dx.doi.org/10.3390/ijms21165697.

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Carbonic anhydrases (CAs) and metallothioneins (MTs) are both families of zinc metalloproteins central to life, however, they coordinate and interact with their Zn2+ ion cofactors in completely different ways. CAs and MTs are highly sensitive to the cellular environment and play key roles in maintaining cellular homeostasis. In addition, CAs and MTs have multiple isoforms with differentiated regulation. This review discusses current literature regarding these two families of metalloproteins in carcinogenesis, with a dialogue on the association of these two ubiquitous proteins in vitro in the context of metalation. Metalation of CA by Zn-MT and Cd-MT is described. Evidence for protein–protein interactions is introduced from changes in metalation profiles of MT from electrospray ionization mass spectrometry and the metalation rate from stopped-flow kinetics. The implications on cellular control of pH and metal donation is also discussed in the context of diseased states.
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Sullivan, Matthew P., Michael Groessl, Samuel M. Meier, Richard L. Kingston, David C. Goldstone, and Christian G. Hartinger. "The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography." Chemical Communications 53, no. 30 (2017): 4246–49. http://dx.doi.org/10.1039/c6cc10150j.

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Yuan, Amelia T., Natalie C. Korkola, Daisy L. Wong, and Martin J. Stillman. "Metallothionein Cd4S11 cluster formation dominates in the protection of carbonic anhydrase." Metallomics 12, no. 5 (2020): 767–83. http://dx.doi.org/10.1039/d0mt00023j.

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5

Young, Tessa R., and Zhiguang Xiao. "Principles and practice of determining metal–protein affinities." Biochemical Journal 478, no. 5 (March 10, 2021): 1085–116. http://dx.doi.org/10.1042/bcj20200838.

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Metal ions play many critical roles in biology, as structural and catalytic cofactors, and as cell regulatory and signalling elements. The metal–protein affinity, expressed conveniently by the metal dissociation constant, KD, describes the thermodynamic strength of a metal–protein interaction and is a key parameter that can be used, for example, to understand how proteins may acquire metals in a cell and to identify dynamic elements (e.g. cofactor binding, changing metal availabilities) which regulate protein metalation in vivo. Here, we outline the fundamental principles and practical considerations that are key to the reliable quantification of metal–protein affinities. We review a selection of spectroscopic probes which can be used to determine protein affinities for essential biological transition metals (including Mn(II), Fe(II), Co(II), Ni(II), Cu(I), Cu(II) and Zn(II)) and, using selected examples, demonstrate how rational probe selection combined with prudent experimental design can be applied to determine accurate KD values.
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Osman, Deenah, Anastasia Cooke, Tessa R. Young, Evelyne Deery, Nigel J. Robinson, and Martin J. Warren. "The requirement for cobalt in vitamin B12: A paradigm for protein metalation." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1868, no. 1 (January 2021): 118896. http://dx.doi.org/10.1016/j.bbamcr.2020.118896.

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7

Bode, Manuela, Michael W. Woellhaf, Maria Bohnert, Martin van der Laan, Frederik Sommer, Martin Jung, Richard Zimmermann, Michael Schroda, and Johannes M. Herrmann. "Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase." Molecular Biology of the Cell 26, no. 13 (July 2015): 2385–401. http://dx.doi.org/10.1091/mbc.e14-11-1526.

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Members of the twin Cx9C protein family constitute the largest group of proteins in the intermembrane space (IMS) of mitochondria. Despite their conserved nature and their essential role in the biogenesis of the respiratory chain, the molecular function of twin Cx9C proteins is largely unknown. We performed a SILAC-based quantitative proteomic analysis to identify interaction partners of the conserved twin Cx9C protein Cox19. We found that Cox19 interacts in a dynamic manner with Cox11, a copper transfer protein that facilitates metalation of the Cu(B) center of subunit 1 of cytochrome c oxidase. The interaction with Cox11 is critical for the stable accumulation of Cox19 in mitochondria. Cox19 consists of a helical hairpin structure that forms a hydrophobic surface characterized by two highly conserved tyrosine-leucine dipeptides. These residues are essential for Cox19 function and its specific binding to a cysteine-containing sequence in Cox11. Our observations suggest that an oxidative modification of this cysteine residue of Cox11 stimulates Cox19 binding, pointing to a redox-regulated interplay of Cox19 and Cox11 that is critical for copper transfer in the IMS and thus for biogenesis of cytochrome c oxidase.
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Messori, L., and A. Merlino. "Protein metalation by metal-based drugs: X-ray crystallography and mass spectrometry studies." Chem. Commun. 53, no. 85 (2017): 11622–33. http://dx.doi.org/10.1039/c7cc06442j.

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9

Merlino, Antonello, Tiziano Marzo, and Luigi Messori. "Protein Metalation by Anticancer Metallodrugs: A Joint ESI MS and XRD Investigative Strategy." Chemistry - A European Journal 23, no. 29 (February 14, 2017): 6942–47. http://dx.doi.org/10.1002/chem.201605801.

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10

Zoppi, Carlotta, Lara Massai, Damiano Cirri, Chiara Gabbiani, Alessandro Pratesi, and Luigi Messori. "Protein metalation by two structurally related gold(I) carbene complexes: An ESI MS study." Inorganica Chimica Acta 520 (May 2021): 120297. http://dx.doi.org/10.1016/j.ica.2021.120297.

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Dissertations / Theses on the topic "Protein metalation"

1

MASSAI, LARA. "Gold Compounds as Anticancer Agents: A Systematic Study of Gold–Protein Metalation." Doctoral thesis, 2014. http://hdl.handle.net/2158/982188.

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The main goal of the present work has been to elucidate the modes of action of cytotoxic gold compounds which are still poorly understood.Accordingly, a small panel of representative cytotoxic gold compounds have been extensively characterised from the chemical point of view. Particular attention has been paid to the description of their solution behaviour and of their stability under experimental conditions similar to those of the biological tests. Afterward, a systemic investigation has been carried out to describe the reactivity of gold compounds with likely protein targets; in particular, their reactions with a few model proteins have been assayed through ESI MS experiments. Remarkably, the peculiar coordination properties of the gold(III) center allow the obtainment of metal complexes showing an almost co-planar localization of extended aromatic surfaces, that seem highly suitable for a particular nucleic acid targeting: DNA G-quadruplex.
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MARZO, TIZIANO. "FROM CONVENTIONAL TO NOVEL Pt-BASED ANTINEOPLASTIC AGENTS: MECHANISTIC ASPECTS AND BIOLOGICAL EFFECTS." Doctoral thesis, 2016. http://hdl.handle.net/2158/1022440.

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In the last decades the research on inorganic drugs in medicine has registered remarkable progresses with particular emphasis to the field of anticancer drugs. Cisplatin, carboplatin and oxaliplatin are today widely used in the treatment of different type of malignance and often represent, even in combination with other drugs, a first choice therapy. Since the serendipitous discover of cisplatin and despite the efforts, still nowadays, these drug are the most important research products in this field, although resistance to the treatments and heavy side effects, are important limiting factors to their use in clinical protocols. Thus, there is urgent need of new and more effective Pt-based anticancer drugs able to circumvent these problems. The development of new metal-based anticancer molecules is not easy, mostly because it is difficult to predict their effects in vivo, starting from the analysis of the cellular effects in vitro. Furthermore it should taken into account the extreme complexity of biological systems; even limiting our consideration only to studies at the cellular level, already, there are an outstanding number of factors and variables to be consider. In this frame we have carried out studies on cell-free systems as well as cellular studies, characterising the reactivity and the cellular effects of cisplatin and a series of its analogues to shed light on analogies and differences between these drugs. Interestingly, it has been extensively characterised their interaction with model proteins. Despite today it is recognised that formation of Pt-protein adducts, is of central importance in relation to overall pharmacological and toxicological impact of cisplatin and its analogues, yet, the structural information concerning platination of protein, and the characterization of the resulting adducts, is limited. Thus the studies summarising in this thesis aimed to: i) gather information on mechanistic aspects correlated with the mode of action of Pt-based anticancer compounds that, to date, remains in part unclear; ii) compare, at different level, the behaviour of conventional platinum anticancer drugs with experimental complexes in order to find differences that may be significant in terms of pharmacological effect in vivo, iii) evaluate or re-evaluate comparatively the anticancer properties of selected cisplatin analogues. All these issues are addressed within this work, where the comparative characterization of protein binding for conventional platinum-based anticancer drugs is reported (chapter 3) as well as the reappraisal of old cisplatin analogues, overlooked so far as anticancer agents, studied in comparison with clinical used Pt compounds (chapter 4 and 5). Preliminary in vivo studies are also described (chapter 6).
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