Per O. Ljungdahl (0000-0002-6625-3540)

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Professional Preparation:
1980 B.A. (Microbiology), Cornell University, Ithaca, NY, USA
1987 Ph.D. (Biochemistry), Dartmouth Medical School, Hanover, NH, USA
1987 – 1990 Research Fellow (Genetics/Cell Biology), Whitehead Institute for Biomedical Research, Cambridge, MA, USA
1990 –1993 Research Associate (Genetics/Cell Biology), Whitehead Institute for Biomedical Research, Cambridge, MA, USA
Appointments:
1993 – 2000 Assistant Member, Ludwig Institute for Cancer Research, Stockholm Branch, Sweden
2001 – 2006 Associate Member, Ludwig Institute for Cancer Research, Stockholm Branch, Sweden
2007 – Professor of Cell Biology, Stockholm University
2010 – 2013 Director, Wenner-Gren Institute for Experimenatal Biology, Stockholm University
2013 – 2019 Chair, Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University
2020 - Director, Campus Solna, SciLifeLab - Stockholm

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Diverse mechanisms control amino acid‐dependent environmental alkalization by <i>Candida albicans</i>

Molecular Microbiology

2024-01-04 | Journal article

DOI: 10.1111/mmi.15216

Part of ISSN: 0950-382X

Part of ISSN: 1365-2958

Contributors: Fitz Gerald Salazar Silao; Valerie Diane Valeriano; Erika Uddström; Emilie Falconer; Per O. Ljungdahl

Per O. Ljungdahl

https://orcid.org/0000-0002-6625-3540

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Works (50 of 80)

Diverse mechanisms control amino acid‐dependent environmental alkalization by <i>Candida albicans</i>

Proline catabolism is a key factor facilitating Candida albicans pathogenicity

ER-localized Shr3 is a selective co-translational folding chaperone necessary for amino acid permease biogenesis

Diverse mechanisms control amino acid-dependent environmental alkalization byCandida albicans

Glutamate dehydrogenase (Gdh2)-dependent alkalization is dispensable for escape from macrophages and virulence of Candida albicans

The ER membrane chaperone Shr3 acts in a progressive manner to assist the folding of related plasma membrane transport proteins

Glutamate dehydrogenase (Gdh2)-dependent alkalization is dispensable for escape from macrophages and virulence ofCandida albicans

Ssy1 functions at the plasma membrane as a receptor of extracellular amino acids independent of plasma membrane‐endoplasmic reticulum junctions

Mitochondrial proline catabolism activates Ras1/cAMP/PKA-induced filamentation in Candida albicans

Mitochondrial proline catabolism activates Ras1/cAMP/PKA-induced filamentation in Candida albicans

Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity

Cdc48 and Ubx1 participate in a pathway associated with the inner nuclear membrane that governs Asi1 degradation

Atypical Ubiquitylation in Yeast Targets Lysine-less Asi2 for Proteasomal Degradation

Diverse Nitrogen Sources in Seminal Fluid Act in Synergy To Induce Filamentous Growth of Candida albicans.

A nuclear ubiquitin-proteasome pathway targets the inner nuclear membrane protein Asi2 for degradation

Latency of transcription factor Stp1 depends on a modular regulatory motif that functions as cytoplasmic retention determinant and nuclear degron

Protein quality control at the inner nuclear membrane

Rts1-protein phosphatase 2A antagonizes Ptr3-mediated activation of the signaling protease Ssy5 by casein kinase I

SOMA: A Single Oligonucleotide Mutagenesis and Cloning Approach

Regulation of Amino Acid, Nucleotide, and Phosphate Metabolism in Saccharomyces cerevisiae

A phosphodegron controls nutrient-induced proteasomal activation of the signaling protease Ssy5

Wild-Type Drosophila melanogaster as a Model Host to Analyze Nitrogen Source Dependent Virulence of Candida albicans

The Prodomain of Ssy5 Protease Controls Receptor-Activated Proteolysis of Transcription Factor Stp1

Amino-acid-induced signalling via the SPS-sensing pathway in yeast

Dal81 enhances stp1- and stp2-dependent transcription necessitating negative modulation by inner nuclear membrane protein asil in Saccharomyces cerevisiae

Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert to maintain the latent properties of transcription factors Stp1 and Stp2

Membrane chaperone Shr3 assists in folding amino acid permeases preventing precocious ERAD

Ssh4, Rcr2 and Rcr1 affect plasma membrane transporter activity in Saccharomyces cerevisiae

Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors

Host-pathogen interactions and the pathological consequences of acute systemic Candida albicans infections in mice

Regulation of transcription factor latency by receptor-activated proteolysis

Divergence of Stp1 and Stp2 transcription factors in Candida albicans places virulence factors required for proper nutrient acquisition under amino acid control

Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER

Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER

An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans

Four permeases import proline and the toxic proline analogue azetidine-2-carboxylate into yeast

The N-terminal regulatory domain of Stp1p is modular and, fused to an artificial transcription factor, confers full Ssy1p-Ptr3p-Ssy5p sensor control

Characterization of potassium transport in wild-type and isogenic yeast strains carrying all combinations of trk1, trk2 and tok1 null mutations

Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-x (LNX)

Mrd1p is required for processing of pre-rRNA and for maintenance of steady-state levels of 40 S ribosomal subunits in yeast

Receptor-mediated endoproteolytic activation of two transcription factors in yeast

Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-Ssy5p sensor of extracellular amino acids

Sensors of extracellular nutrients in Saccharomyces cerevisiae

Suppressors of ssy1 and ptr3 null mutations define novel amino acid sensor-independent genes in Saccharomyces cerevisiae

Suppressors of ssy1 and ptr3 null mutations define novel amino acid sensor-independent genes in Saccharomyces cerevisiae

The role of the yeast plasma membrane SPS nutrient sensor in the metabolic response to extracellular amino acids

A method for determining the in vivo topology of yeast polytopic membrane proteins demonstrates that Gap1p fully integrates into the membrane independently of Shr3p

The SHR3 homologue from S-pombe demonstrates a conserved function of ER packaging chaperones

The SHR3 homologue from S-pombe demonstrates a conserved function of ER packaging chaperones

Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles

Peer review (4 reviews for 3 publications/grants)