Selected Publications

  • Martins A, Pfirrmann T, Heessen S, Sundqvist G, Bulone V, Andréasson C and Ljunggdahl PO (2018):  
     Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specifity.  
    J Biol Chem. 293(22), 8362-8378 
  • Klaus A, Pfirrmann T, Glomb MA (2017):  
     Transketolase A from E.coli Significantly Suppresses Protein Glycation by Glycoaldehyde and Glyoxal in Vitro. 
    J Agric Food Chem. doi: 10.1021/acs.jafc.7b03183 
  • Jennek S, Mittag S, Reiche J, Westphal JK, Seelk S, Dörfel MJ, Pfirrmann T, Friedrich K, Schütz A, Heinemann U and Huber O (2017):  
     Tricellulin is a target of the ubiquitin ligase Itch.  
    Ann N Y Acad Sci. doi: 10.1111/nyas.13349
  • Pfirrmann T, Jandt E, Ranft S, Lokapally A, Neuhaus H, Perron M and Hollemann T (2016):  
     Hedgehog-dependent E3-ligase Midline1 regulates ubiquitin-mediated proteasomal degradation of Pax6 during visual system development.  
    Proc Natl Acad Sci U S A. 113(36), 10103-8
  • Pfirrmann T, Villavicencio-Lorini P, Subudhi AK, Menssen R, Wolf DH and Hollemann T (2015):  
     RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development.  
    PLoS One. 10(3), e0120342
  • Pfirrmann T, Emmerich D, Ruokonen P, Quandt D, Buchen R, Fischer-Zirnsak B, Hecht J, Krawitz P, Meyer P, Klopocki E, Stricker S, Lausch E, Seliger B, Hollemann T, Reinhard T, Auw-Haedrich C, Zabel B, Hoffmann K and Villavicencio-Lorini P (2015):  
     Molecular mechanism of CHRDL1-mediated X-linked megalocornea in humans and in Xenopus model.  
    Hum Mol Genet. 24(11), 3119-32
  • Pfirrmann T, Lokapally A, Andreasson C, Ljungdahl P and Hollemann T (2013):  
     SOMA: a single oligonucleotide mutagenesis and cloning approach.  
    PloS one. 8(6), e64870
  • Zhao B, Velasco K, Sompallae R, Pfirrmann T, Masucci MG and Lindsten K (2012):  
     The ubiquitin specific protease-4 (USP4) interacts with the S9/Rpn6 subunit of the proteasome.  
    Biochemical and biophysical research communications. 427(3), 490-6
  • Omnus DJ, Pfirrmann T, Andreasson C and Ljungdahl PO (2011):  
     A phosphodegron controls nutrient-induced proteasomal activation of the signaling protease Ssy5.  
    Molecular biology of the cell. 22, 2754-2765 
  • Braun B, Pfirrmann T, Menssen R, Hofmann K, Scheel H and Wolf DH (2011):  
     Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation.  
    FEBS letters. 585, 3856-3861 
  • Basseres E, Coppotelli G, Pfirrmann T, Andersen JB, Masucci M and Frisan T (2010):  
      The ubiquitin C-terminal hydrolase UCH-L1 promotes bacterial invasion by altering the dynamics of the actin cytoskeleton.  
    Cellular microbiology. 12, 1622-1633 
  • Pfirrmann T, Heessen S, Omnus DJ, Andreasson C and Ljungdahl PO (2010): 
     The prodomain of Ssy5 protease controls receptor-activated proteolysis of transcription factor Stp1.  
    Molecular and cellular biology. 30, 3299-3309 
  • Rolen U, Freda E, Xie J, Pfirrmann T, Frisan T and Masucci MG (2009):  
     The ubiquitin C-terminal hydrolase UCH-L1 regulates B-cell proliferation and integrin activation.  
    Journal of cellular and molecular medicine. 13, 1666-1678 
  • Santt O, Pfirrmann T, Braun B, Juretschke J, Kimmig P, Scheel H, Hofmann K, Thumm M and Wolf DH (2008):  
     The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism.  
    Molecular biology of the cell. 19, 3323-3333 
  • Eisele F, Braun B, Pfirrmann T and Wolf DH (2006):  
     Mutants of the deubiquitinating enzyme Ubp14 decipher pathway diversity of ubiquitin-proteasome linked protein degradation.  
    Biochemical and biophysical research communications. 350, 329-333 




Prof. Dr. Guido Posern

Abt. Ubiquitination: 
Leiter: Thorsten Pfirrmann 
Telefon: (0345) 557-3802 
Fax:        (0345) 557-3804 
Email:    Thorsten Pfirrmann

Institut für Physiologische Chemie
Hollystrasse 1
06114 Halle (Saale)

Frau Ines Knipping
Telefon: (0345) 557-3812 
Fax:        (0345) 557-3811
Email:   Sekretariat