Duyệt theo

Hồ sơ tác giả

Tìm kiếm theo: Chủ đề Cơ sở cấu trúc

Duyệt theo: 0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
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  • OER000002722.pdf.jpg
  • Journal article

  • A structural basis for prion strain diversity

    • Tác giả : Manka, Szymon W. (2023)

  • Recent cryo-EM studies of infectious, ex vivo, prion fibrils from hamster 263K and mouse RML prion strains revealed a comparable, parallel in-register intermolecular β-sheet (PIRIBS) amyloid architecture. Rungs of the fibrils are composed of individual prion protein (PrP) monomers that fold to create distinct N- and C-terminal lobes. However, disparity in the hamster/mouse PrP sequence precludes understanding how divergent prion strains emerge ...
  • OER000002682.pdf.jpg
  • Journal article

  • Structural and biochemical basis of FANCI-FANCD2 interdependent ubiquitination

    • Tác giả : Lemonidis, Kimon (2023)

  • The Fanconi Anaemia pathway operates for the repair of interstrand crosslinks and the maintenance 11 of genomic stability upon replication stalling. Di‐monoubiquitination of the FANCI‐FANCD2 (ID2) 12 complex is a central and crucial step in this pathway. Evidence suggests that FANCD2 ubiquitination 13 precedes FANCI ubiquitination, and that both the FANCD2‐ubiquitinated (ID2Ub) and the di14 monoubiquitinated (IUbD2Ub) complex clamp on DNA. However, FANCD2...
  • OER000002388.pdf.jpg
  • Journal Article

  • Structural Basis for Autoinhibition by the Dephosphorylated Regulatory Domain of Ycf1

    • Tác giả : Khandelwal, Nitesh Kumar (2023)

  • Yeast Cadmium Factor 1 (Ycf1) sequesters glutathione and glutathione-heavy metal conjugates into yeast vacuoles as a cellular detoxification mechanism. Ycf1 belongs to the C subfamily of ATP Binding Cassette (ABC) transporters characterized by long flexible linkers, notably the regulatory domain (R-domain). R-domain phosphorylation is necessary for activity, whereas dephosphorylation induces autoinhibition through an undefined mechanism. Because of its transient and dynamic nature,&#...
  • OER000002615.pdf.jpg
  • Journal article

  • Structural basis for binding of Smaug to the GPCR Smoothened and to the germline inducer Oskar

    • Tác giả : Kubíková, Jana (2023)

  • Drosophila Smaug and its orthologs comprise a family of mRNA repressor proteins that exhibit various functions during animal development. Smaug proteins contain a characteristic RNA-binding sterile-a motif (SAM) domain and a conserved but uncharacterized N-terminal domain (NTD). Here, we resolved the crystal structure of the NTD of the human SAM domain-containing protein 4A (SAMD4A, a.k.a. Smaug1) to 2.0 Å resolution, which revealed its composi...
  • OER000002688.pdf.jpg
  • Journal article

  • Structural basis for RNA-mediated assembly of type V CRISPR-associated transposons

    • Tác giả : Schmitz, Michael (2023)

  • CRISPR systems have been co-opted by Tn7-like elements to direct RNA-guided transposition. Type V-K CRISPR-associated transposons rely on the concerted activities of the pseudonuclease Cas12k, the AAA+ ATPase TnsC, the Zn-finger protein TniQ, and the transposase TnsB. Here we present a cryo-electron microscopic structure of a target DNA-bound Cas12k-transposon recruitment complex comprising RNA-guided Cas12k, TniQ, TnsC and, unexpectedly, the ribosomal protein ...
  • OER000002309.pdf.jpg
  • Journal Article

  • Structural Basis for the Phase Separation of the Chromosome Passenger Complex

    • Tác giả : Bryan, Nikaela W. (2023)

  • Membraneless intracellular compartmentalization is central to a long and growing list of biochemical transactions at diverse sub-cellular locations 1. Proteins are by-and-large the drivers of the formation of these compartments, but there is debate about whether their underpinnings are either low-affinity/low-specificity interactions yielding phase separation 2 or multivalent site-specific interactions 3. By its very nature, ascertaining the former type of &#x...
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  • Ebooks (Sách điện tử)

  • Structural Basis for the transmembrane signaling and antidepressant-induced activation of the receptor tyrosine kinase TrkB

    • Tác giả : Kot, Erik F. (2023)

  • Neurotrophin receptors of the Trk family are involved in the regulation of brain development and neuroplasticity, and therefore can serve as targets for anti-cancer and stroke-recovery drugs, antidepressants, and many others. The structures of Trk protein domains in various states upon activation need to be elucidated to allow rational drug design. However, little is known about the conformations of the transmembrane and juxtamembrane domains of Trk receptors...
  • OER000002776.pdf.jpg
  • Journal article

  • Structural basis of actin filament assembly and aging

    • Tác giả : Oosterheert, Wout (2023)

  • The dynamic turnover of actin filaments (F-actin) controls cellular motility in eukaryotes and is coupled to changes in the F-actin nucleotide state. It remains unclear how F-actin hydrolyzes ATP and subsequently undergoes subtle conformational rearrangements that ultimately lead to filament depolymerization by actin-binding proteins. Here, we present cryo-EM structures of F-actin in all nucleotide states, polymerized in the presence of Mg2+ or Ca2+, ...
  • OER000002518.pdf.jpg
  • Journal article

  • Structural basis of LRPPRC-SLIRP-dependent translation by the mitoribosome

    • Tác giả : Singh, Vivek  (2023)

  • To explore the molecular basis for translation activation in human mitochondria, we used low 90 salt conditions to isolate a mitoribosome:LRPPRC-SLIRP-mRNA complex for cryo-EM. We available under aCC-BY-NC-ND 4.0 International license. was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made bioRxiv preprint doi: https://doi.org/10.1101/2022.06.20.496763; this...
  • OER000002676.pdf.jpg
  • Journal article

  • Structural basis of mitochondrial membrane bending by I-II-III2-IV2 supercomplex

    • Tác giả : Mühleip, Alexander (2023)

  • Mitochondrial energy conversion requires an intricate architecture of the inner 23 mitochondrial membrane1. Here we show that in ciliates, the membrane curvature is 24 provided by a supercomplex containing all four respiratory chain components. We report 25 cryo-electron microscopy and cryo-tomography structures of the supercomplex that 26 comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-megadalton 27 assembly. Due to ...
  • OER000002928.pdf.jpg
  • Journal article

  • Structural basis of polyamine transport by human ATP13A2 (PARK9)

    • Tác giả : Sim, Sue Im (2021)

  • Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transporters at endo-/lysosomes. Loss-of-function mutations of ATP13A2 in humans cause hereditary early-onset Parkinson’s disease. To understand the polyamine ...
  • OER000002677.pdf.jpg
  • Journal article

  • Structural basis of ubiquitin-independent PP1 complex disassembly by p97

    • Tác giả : Boom, Johannes van den (2023)

  • The AAA+ ATPase p97 (also called VCP, or Cdc48 in yeast) unfolds proteins and disassembles protein complexes in a myriad of cellular processes, but how a substrate complex needs to be loaded onto p97 by a dedicated substrate adapter and then disassembled by p97 has not been structurally visualized so far. Here we present cryo-EM structures of p97 in the process of disassembling a protein phosphatase-1 (PP1) complex by &#...
  • OER000002729.pdf.jpg
  • Journal article

  • Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms

    • Tác giả : Selvaraj, Muniyandi (2023)

  • The actin cytoskeleton is critical for cell migration, morphogenesis, endocytosis, organelle dynamics, and cytokinesis. To support diverse cellular processes, actin filaments form a variety of structures with specific architectures and dynamic properties. Key proteins specifying actin filaments are tropomyosins. Non-muscle cells express several functionally non-redundant tropomyosin isoforms, which differentially control the interactions of other proteins, including myosins ...