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Lukasz Joachimiak, Ph.D.

Lukasz Joachimiak, Ph.D.

Titles and Appointments

Associate Professor

Endowed Title
Effie Marie Cain Scholar in Medical Research
Schools
Medical School | Graduate School
Departments
Center for Alzheimer's and Neurodegenerative Diseases | Biochemistry | Biophysics
Graduate Programs
Molecular Biophysics
  • Biography

    Download Curriculum Vitae

    Lukasz Joachimiak received his B.S. in Biochemistry from the University of Wisconsin-Madison in 2000.  He received his Ph.D. in 2007 working in the lab of David Baker at University of Washington where he established computational tools to define the energetic and structural principles that underlie protein-protein interactions.  He completed his postdoctoral work with Judith Frydman at Stanford University where he developed innovative approaches to understand the structure and mechanics of substrate interaction by the eukaryotic chaperonin TRiC/CCT.

    At UT Southwestern Medical Center, Dr. Joachimiak's laboratory utilizes structural and biochemical approaches to dissect the role of chaperones and protein misfolding in neurodegenerative diseases.  His group is also interested in integrating computational and experimental methods to design molecular interactions to control amyloid assembly.

    The Joachimiak Lab is a collaborative environment focused on uncovering the molecular origins of neurodegenerative disease. We value scientific rigor, creativity, and interdisciplinary thinking, and support trainees in taking ownership of their research to advance the field. 

     

     

  • Education
    Undergraduate
    Uni of Wisconsin-Madison (2001), Biochemistry
    Graduate School
    University of Washington (2007), Biochemistry
  • Research Interest
    • Chaperone structural biology
    • Design of molecular recognition and specificity
    • Protein (mis)folding in neurodegenerative diseases
  • Publications

    Star Featured Publications

    Featured Featured Featured Featured Featured
    NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.
    Muela-Zarzuela I, Alcocer-Gómez E, Suarez-Rivero JM, Low E, Ishaq A, Azkargorta M, Luque-Sierra A, Martin F, Elortza F, Astorga-Gamaza A, Antón R, Bali S, Tamargo-Azpilicueta J, Guerra-Castellano A, Díaz-Moreno I, Joachimiak LA, Oroz J, Ruiz-Cabello J, von Zglinicki T, Sanz A, Cordero MD, Sci Adv 2026 Jun 12 26 eaec9499
    Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.
    Jayan P, Rastogi S, Bommareddy V, Dashnaw CM, Vaquer-Alicea J, Nguyen BA, Saelices L, Shahmoradian S, White CL, Diamond MI, Joachimiak LA, bioRxiv 2026 Mar
    Amyloid-motif-dependent tau self-assembly is modulated by isoform sequence context.
    Bali S, Wydorski PM, Singh R, Van Nuland NE, Wosztyl A, Morgan N, Perez VA, Chen D, Chen J, Rizo J, Joachimiak LA, Structure 2025 Dec
    DnaJB1 chaperone inhibits tau aggregation by recognizing its N-terminus.
    Wydorski PM, Macierzynska P, Bali S, Vaquer-Alicea J, Joachimiak LA, bioRxiv 2025 Oct
    Select azo compounds post-translationally modulate HTRA1 abundance and activity potentially through interactions at the trimer interface.
    Hulleman JD, Jeon S, Bali S, DiCesare SM, Abbas A, Daniel S, Ortega AJ, Collier GE, Yang J, Bhattacharyaa A, McCoy MK, Joachimiak LA, Posner BA, bioRxiv 2025 May
  • Honors & Awards
    • Endowed Scholar Award
      (2016-2020)