Lukasz A Joachimiak
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Explore the profile of Lukasz A Joachimiak including associated specialties, affiliations and a list of published articles.
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46
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1325
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Recent Articles
1.
Westphal K, Michalska K, Joachimiak A, Joachimiak L
FEBS Open Bio
. 2025 Feb;
PMID: 39992796
Molecular machines from the AAA+ (ATPases Associated with diverse cellular Activity) superfamily of protein disaggregases play important roles in protein folding, disaggregation and DNA processing. Recent cryo-EM structures of AAA+...
2.
Vaquer-Alicea J, Manon V, Bommareddy V, Kunach P, Gupta A, Monistrol J, et al.
Sci Adv
. 2025 Jan;
11(4):eadp5978.
PMID: 39841851
Distinct tau amyloid assemblies underlie diverse tauopathies but defy rapid classification. Cell and animal experiments indicate tau functions as a prion, as different strains propagated in cells cause unique, transmissible...
3.
Wang J, Fendler N, Shukla A, Wu S, Challa A, Lee J, et al.
Mol Cell
. 2024 Nov;
84(23):4538-4557.e12.
PMID: 39532099
The polymerase associated factor 1 (PAF1) complex (PAF1c) promotes RNA polymerase II (RNA Pol II) transcription at the elongation step; however, how PAF1c transcription activity is selectively regulated during cell...
4.
Sari L, Bali S, Joachimiak L, Lin M
Nat Commun
. 2024 Mar;
15(1):2756.
PMID: 38553453
Protein fibril self-assembly is a universal transition implicated in neurodegenerative diseases. Although fibril structure/growth are well characterized, fibril nucleation is poorly understood. Here, we use a computational-experimental approach to resolve...
5.
Ryder B, Ustyantseva E, Boyer D, Mendoza-Oliva A, Kuska M, Wydorski P, et al.
Structure
. 2024 Mar;
32(6):662-678.e8.
PMID: 38508190
J-domain protein (JDP) molecular chaperones have emerged as central players that maintain a healthy proteome. The diverse members of the JDP family function as monomers/dimers and a small subset assemble...
6.
Rios M, Bagnucka M, Ryder B, Ferreira Gomes B, Familiari N, Yaguchi K, et al.
J Cell Biol
. 2024 Mar;
223(4).
PMID: 38456967
The outermost layer of centrosomes, called pericentriolar material (PCM), organizes microtubules for mitotic spindle assembly. The molecular interactions that enable PCM to assemble and resist external forces are poorly understood....
7.
Marszalek J, De Los Rios P, Cyr D, Mayer M, Adupa V, Andreasson C, et al.
Cell Stress Chaperones
. 2024 Feb;
29(1):21-33.
PMID: 38320449
J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is...
8.
Bali S, Singh R, Wydorski P, Wosztyl A, Perez V, Chen D, et al.
Res Sq
. 2024 Feb;
PMID: 38313287
The microtubule-associated protein tau is implicated in neurodegenerative diseases characterized by amyloid formation. Mutations associated with frontotemporal dementia increase tau aggregation propensity and disrupt its endogenous microtubule-binding activity. The structural...
9.
Bali S, Singh R, Wydorski P, Van Nuland N, Wosztyl A, Perez V, et al.
bioRxiv
. 2024 Jan;
PMID: 38168322
Abstract Figure:
10.
Chlebowicz J, Russ W, Chen D, Vega A, Vernino S, White 3rd C, et al.
Sci Adv
. 2023 Oct;
9(43):eadh3457.
PMID: 37889966
α-Synuclein (aSyn) aggregation underlies neurodegenerative synucleinopathies. aSyn seeds are proposed to replicate and propagate neuronal pathology like prions. Seeding of aSyn can be recapitulated in cellular systems of aSyn aggregation;...