Pawel A Penczek
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Explore the profile of Pawel A Penczek including associated specialties, affiliations and a list of published articles.
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3803
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Recent Articles
1.
Penczek P
IUCrJ
. 2020 Nov;
7(Pt 6):995-1008.
PMID: 33209314
A modified Fourier shell correlation (mFSC) methodology is introduced that is aimed at addressing two fundamental problems that mar the use of the FSC: the strong influence of mask-induced artifacts...
2.
Moncrieffe M, Bollschweiler D, Li B, Penczek P, Hopkins L, Bryant C, et al.
Structure
. 2020 Jan;
28(3):281-289.e3.
PMID: 31995744
Toll-like receptors (TLRs) are pivotal in triggering the innate immune response to pathogen infection. Ligand binding induces receptor dimerization which facilitates the recruitment of other post-receptor signal transducers into a...
3.
Hattne J, Martynowycz M, Penczek P, Gonen T
IUCrJ
. 2019 Oct;
6(Pt 5):921-926.
PMID: 31576224
Microcrystal electron diffraction (MicroED) combines crystallography and electron cryo-microscopy (cryo-EM) into a method that is applicable to high-resolution structure determination. In MicroED, nanosized crystals, which are often intractable using other...
4.
Schubert E, Vetter I, Prumbaum D, Penczek P, Raunser S
Elife
. 2018 Jul;
7.
PMID: 30010541
α-Xenorhabdolysins (Xax) are α-pore-forming toxins (α-PFT) that form 1-1.3 MDa large pore complexes to perforate the host cell membrane. PFTs are used by a variety of bacterial pathogens to attack...
5.
Brignole E, Tsai K, Chittuluru J, Li H, Aye Y, Penczek P, et al.
Elife
. 2018 Feb;
7.
PMID: 29460780
Ribonucleotide reductases (RNRs) convert ribonucleotides into deoxyribonucleotides, a reaction essential for DNA replication and repair. Human RNR requires two subunits for activity, the α subunit contains the active site, and...
6.
Moriya T, Saur M, Stabrin M, Merino F, Voicu H, Huang Z, et al.
J Vis Exp
. 2017 Jun;
(123).
PMID: 28570515
SPHIRE (SPARX for High-Resolution Electron Microscopy) is a novel open-source, user-friendly software suite for the semi-automated processing of single particle electron cryo-microscopy (cryo-EM) data. The protocol presented here describes in...
7.
Fu T, Li Y, Lu A, Li Z, Vajjhala P, Cruz A, et al.
Mol Cell
. 2016 Oct;
64(2):236-250.
PMID: 27746017
Caspase-8 activation can be triggered by death receptor-mediated formation of the death-inducing signaling complex (DISC) and by the inflammasome adaptor ASC. Caspase-8 assembles with FADD at the DISC and with...
8.
Blok N, Tan D, Wang R, Penczek P, Baker D, DiMaio F, et al.
Proc Natl Acad Sci U S A
. 2015 Jul;
112(30):E4017-25.
PMID: 26170309
Members of the AAA family of ATPases assemble into hexameric double rings and perform vital functions, yet their molecular mechanisms remain poorly understood. Here, we report structures of the Pex1/Pex6...
9.
Behrmann E, Loerke J, Budkevich T, Yamamoto K, Schmidt A, Penczek P, et al.
Cell
. 2015 May;
161(4):845-57.
PMID: 25957688
Macromolecular machines, such as the ribosome, undergo large-scale conformational changes during their functional cycles. Although their mode of action is often compared to that of mechanical machines, a crucial difference...
10.
Cheng Y, Grigorieff N, Penczek P, Walz T
Cell
. 2015 Apr;
161(3):438-449.
PMID: 25910204
Cryo-electron microscopy (cryo-EM) of single-particle specimens is used to determine the structure of proteins and macromolecular complexes without the need for crystals. Recent advances in detector technology and software algorithms...