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Copper interaction with cystatin C: effects on protein structure and oligomerization.

• Authors : Żygowska, Justyna¹ (AUTHOR); Orlikowska, Marta¹ (AUTHOR); Zhukov, Igor² (AUTHOR)

Subjects: *Cystatin C; *Protein structure; *Gel permeation chromatography

• Source: FEBS Journal. May2024, Vol. 291 Issue 9, p1974-1991. 18p.

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The influence of a copper efflux pump in Histoplasma capsulatum virulence.

• Authors : Moraes, Dayane¹ (AUTHOR); Tristão, Gabriel Brum¹ (AUTHOR); Rappleye, Chad A.² (AUTHOR)

Subjects: *Copper; *Copper poisoning; *Yeast culture

• Source: FEBS Journal. Feb2024, Vol. 291 Issue 4, p744-760. 17p.

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Rational engineering of AA5_2 copper radical oxidases to probe the molecular determinants governing their substrate selectivity.

• Authors : Koncitikova, Radka^1,2 (AUTHOR); Zuily, Lisa¹ (AUTHOR); Lemarié, Emeline^1,2 (AUTHOR)

Subjects: *Molecular probes; *Copper; *Oxidases

• Source: FEBS Journal. May2023, Vol. 290 Issue 10, p2658-2672. 15p.

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Copper interaction with cystatin C: effects on protein structure and oligomerization

Subjects: 0303 health sciences; 03 medical and health sciences; binding site

• Source: FEBS Journal. 291(9):1974-1991

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Low copper availability limits Helicobacter infection in mice.

• Authors : Esposito, Roberta¹ (AUTHOR); Vllahu, Megi^1,2 (AUTHOR); Morello, Silvana¹ (AUTHOR)

Subjects: *Helicobacter pylori; *Trefoil factors; *Mice

• Source: FEBS Journal. Jul2020, Vol. 287 Issue 14, p2948-2960. 13p.

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Rv0474 is a copper‐responsive transcriptional regulator that negatively regulates expression of RNA polymerase β subunit in Mycobacterium tuberculosis.

• Authors : Raghunandanan, Sajith¹; Ramachandran, Ranjit¹; Gomez, Roshna Lawrence¹

Subjects: *Copper; *RNA polymerases; *Transcription factors

• Source: FEBS Journal. Oct2018, Vol. 285 Issue 20, p3849-3869. 21p.

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Ace1 prevents intracellular copper accumulation by regulating Fet3 expression and thereby restricting Aft1 activity.

• Authors : Gaspar‐Cordeiro, Ana¹; Marques Caetano, Soraia¹; Amaral, Catarina¹

Subjects: *Copper; *Saccharomyces cerevisiae; *Gene expression

• Source: FEBS Journal. May2018, Vol. 285 Issue 10, p1861-1872. 12p.

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Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction.

• Authors : Sasaki D; Molecular Biophysics Group, Institute of Systems, Molecular and Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, UK.; Watanabe TF

Subjects: Achromobacter cycloclastes/Achromobacter cycloclastes/Achromobacter cycloclastes/*chemistry ; Alcaligenes/Alcaligenes/Alcaligenes/*chemistry ; Bacterial Proteins/Bacterial Proteins/Bacterial Proteins/*chemistry

• Source: The FEBS journal [FEBS J] 2021 Jan; Vol. 288 (1), pp. 262-280. Date of Electronic Publication: 2020 Apr 28.Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication

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Structural and functional characterisation of multi‐copper oxidase CueO from lignin‐degrading bacterium Ochrobactrum sp. reveal its activity towards lignin model compounds and lignosulfonate.

• Authors : Granja‐Travez, Rommel Santiago¹; Wilkinson, Rachael C.²; Persinoti, Gabriela Felix³

Subjects: *Copper oxide; *Lignins; *Lignosulfonates

• Source: FEBS Journal. May2018, Vol. 285 Issue 9, p1684-1700. 17p.

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Characterization of a bacterial copper-dependent lytic polysaccharide monooxygenase with an unusual second coordination sphere.

• Authors : Munzone A; Aix Marseille Univ, CNRS, Centrale Marseille, iSm2, Marseille, France.; El Kerdi B

Subjects: Bacterial Proteins/Bacterial Proteins/Bacterial Proteins/*chemistry ; Bacterial Proteins/Bacterial Proteins/Bacterial Proteins/*metabolism ; Copper/Copper/Copper/*metabolism

• Source: The FEBS journal [FEBS J] 2020 Aug; Vol. 287 (15), pp. 3298-3314. Date of Electronic Publication: 2020 Jan 24.Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication

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