Pernilla Wittung-Stafshede

About

Pernilla Wittung-Stafshede is a Professor of Chemistry and BioSciences at Rice University, holding the Charles W. Duncan Jr.-Welch Chair in Chemistry and serving as a CPRIT Scholar in Cancer Research. Her research group employs biophysical and biochemical tools to investigate the (dys)functionality of proteins and biological pathways at the molecular level, with a focus on understanding the role of metal ions, particularly copper, in health and disease. Her work explores how human cells regulate copper, how imbalances contribute to diseases such as cancer and neurodegenerative disorders, and the mechanisms by which proteins, including amyloids, interact with metals and catalyze reactions. Her pioneering discoveries include insights into the role of metals in protein folding, macromolecular crowding effects, and mechanisms of copper-transport proteins. Wittung-Stafshede's research integrates biophysics, biochemistry, and bioinorganic chemistry, often in collaboration with other groups, to advance fundamental knowledge aimed at improving human health. She has made significant contributions to understanding the molecular mechanisms underlying diseases like Alzheimer's, Parkinson's, and cancer, and her work includes exploring the emerging roles of amyloids in these conditions. Her academic career spans positions at Tulane University, Umeå University, Chalmers University of Technology, and Rice University, with notable achievements including election to the Royal Swedish Academy…

Selected publications

• ATP7A-Regulated Enzyme Metalation and Trafficking in the Menkes Disease Puzzle

  Biomedicines · 2021-04-06 · 76 citations

  reviewOpen accessSenior author

  Copper is vital for numerous cellular functions affecting all tissues and organ systems in the body. The copper pump, ATP7A is critical for whole-body, cellular, and subcellular copper homeostasis, and dysfunction due to genetic defects results in Menkes disease. ATP7A dysfunction leads to copper deficiency in nervous tissue, liver, and blood but accumulation in other tissues. Site-specific cellular deficiencies of copper lead to loss of function of copper-dependent enzymes in all tissues, and t…

  PublisherOA PDFDOI

• Metal ions control amyloid catalysis

  Journal of Inorganic Biochemistry · 2025-10-15

  articleSenior authorCorresponding
  PublisherDOI

• ATP Hydrolysis by α‐Synuclein Amyloids is Mediated by Enclosing β‐Strand

  Advanced Science · 2025-10-16

  articleOpen accessSenior authorCorresponding

  Pathological amyloids, like those formed by α-synuclein in Parkinson's disease, are recently found to catalyze the hydrolysis of model substrates in vitro. Here it is reported that the universal energy molecule ATP is another substrate for α-synuclein amyloid chemical catalysis. To reveal the underlying mechanism, the high-resolution cryo-EM structure of the amyloids in the presence of ATP is solved. The structure reveals a type 1A amyloid fold with an additional β-strand involving residues 16-2…

  PublisherOA PDFDOI

• <scp>CAPIM</scp> : Catalytic activity and site prediction and analysis tool in multimer proteins

  Protein Science · 2025-10-18

  articleOpen accessSenior authorCorresponding

  Enzymes play a fundamental role in living organisms by catalyzing vital chemical reactions. While much is known about enzyme function, a substantial portion of the proteome remains uncharacterized. Computational tools have become indispensable in this field, yet most focus exclusively on either enzymatic activity prediction or active site detection, creating a gap between residue-level annotation and functional characterization. To bridge this gap, we present Catalytic Activity and Site Predicti…

  PublisherOA PDFDOI

Awards & honors

• Royal Swedish Academy of Sciences (2016)
• Royal Swedish Academy of Engineering Sciences (2020)
• Honorary Fellow of the Royal Society of Chemistry (2024)
• European Academy of Sciences (2024)
• Finnish Society of Sciences and Letters (2024)

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