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Corinna Probst

Research Associate, Senior
Medicine, Infectious Diseases

Scholarly Works


A cysteine-rich domain of the Cryptococcus neoformans Cuf1 transcription factor is required for high copper stress sensing and fungal virulence.

Journal article mBio · July 8, 2026 UNLABELLED: The ability to sense, import, and detoxify copper (Cu) has been shown to be crucial for microbial pathogens to survive within an infected host. Previous studies conducted with the opportunistic human fungal pathogen Cryptococcus neoformans (Cn) ... Full text Link to item Cite

A broad-spectrum inhibitor of copper-exporting P<sub>1B</sub>-type ATPases.

Journal article Proceedings of the National Academy of Sciences of the United States of America · May 2026 Copper (Cu) transporting ATPases represent a highly conserved subclass of P-type ATPases with critical roles in Cu export and metalloenzyme synthesis. Despite their important biological roles and association with a wide range of human diseases, no high-aff ... Full text Cite

Rsp5-mediated ubiquitination of a functional analog of the Rim8 arrestin facilitates Rim pathway activation in Cryptococcus neoformans.

Journal article mBio · August 13, 2025 Pathogenic microorganisms use varied cellular processes to adapt to the particular stresses encountered in the infected host. These stresses include rapid alterations in ambient temperature, nutrient availability, and extracellular pH. Fungal pathogens, th ... Full text Link to item Cite

A cysteine-rich domain of the Cuf1 transcription factor is required for high copper stress sensing and fungal virulence.

Preprint · December 13, 2024 UNLABELLED: The ability to sense, import but also detoxify copper (Cu) has been shown to be crucial for microbial pathogens to survive within the host. Previous studies conducted with the opportunistic human fungal pathogen Cryptococcus neoformans ( Cn ) h ... Full text Link to item Cite

Interactions between copper homeostasis and the fungal cell wall affect copper stress resistance.

Journal article PLoS Pathog · June 2022 Copper homeostasis mechanisms are essential for microbial adaption to changing copper levels within the host during infection. In the opportunistic fungal pathogen Cryptococcus neoformans (Cn), the Cn Cbi1/Bim1 protein is a newly identified copper binding ... Full text Link to item Cite

Mechanism of molybdate insertion into pterin-based molybdenum cofactors.

Journal article Nature chemistry · August 2021 The molybdenum cofactor (Moco) is found in the active site of numerous important enzymes that are critical to biological processes. The bidentate ligand that chelates molybdenum in Moco is the pyranopterin dithiolene (molybdopterin, MPT). However, neither ... Full text Cite

Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace.

Journal article Scientific reports · October 2020 Lytic polysaccharide monooxygenase (LPMO) and copper binding protein CopC share a similar mononuclear copper site. This site is defined by an N-terminal histidine and a second internal histidine side chain in a configuration called the histidine brace. To ... Full text Cite

A lytic polysaccharide monooxygenase-like protein functions in fungal copper import and meningitis.

Journal article Nature chemical biology · March 2020 Infection by the fungal pathogen Cryptococcus neoformans causes lethal meningitis, primarily in immune-compromised individuals. Colonization of the brain by C. neoformans is dependent on copper (Cu) acquisition from the host, which drives critical virulenc ... Full text Cite

Genome-wide analysis of the regulation of Cu metabolism in Cryptococcus neoformans.

Journal article Mol Microbiol · June 2018 The ability of the human fungal pathogen Cryptococcus neoformans to adapt to variable copper (Cu) environments within the host is key for successful dissemination and colonization. During pulmonary infection, host alveolar macrophages compartmentalize Cu i ... Full text Link to item Cite

Dimerization of the plant molybdenum insertase Cnx1E is required for synthesis of the molybdenum cofactor.

Journal article The Biochemical journal · January 2017 The molybdenum cofactor (Moco) is a redox active prosthetic group, essentially required for numerous enzyme-catalyzed two electron transfer reactions. Moco is synthesized by an evolutionarily old and highly conserved multistep pathway. In the last step of ... Full text Cite

Linear Discriminant Analysis Identifies Mitochondrially Localized Proteins in Neurospora crassa.

Journal article Journal of proteome research · September 2015 Besides their role as powerhouses, mitochondria play a pivotal role in the spatial organization of numerous enzymatic functions. They are connected to the ER, and many pathways are organized through the mitochondrial membranes. Thus, the precise definition ... Full text Cite

Enzymatic characterization of recombinant nitrate reductase expressed and purified from Neurospora crassa.

Journal article Fungal genetics and biology : FG & B · July 2015 We established an expression and purification procedure for recombinant protein production in Neurospora crassa (N. crassa). This Strep-tagĀ® based system was successfully used for purifying recombinant N. crassa nitrate reductase (NR), whose enzymatic acti ... Full text Cite

Genetic characterization of the Neurospora crassa molybdenum cofactor biosynthesis.

Journal article Fungal genetics and biology : FG & B · May 2014 Molybdenum (Mo) is a trace element that is essential for important cellular processes. To gain biological activity, Mo must be complexed in the molybdenum cofactor (Moco), a pterin derivative of low molecular weight. Moco synthesis is a multi-step pathway ... Full text Cite