Evidence map›Paper›PMID 33368013›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Ab Initio Determination of Peptide Structures by MicroED.

Chih-Te Zee, Ambarneil Saha, Michael R Sawaya, Jose A Rodriguez

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Chih-Te ZeeDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA, USA.
Ambarneil SahaDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA, USA.
Michael R SawayaHoward Hughes Medical Institute, UCLA-DOE Institute, Departments of Biological Chemistry, Chemistry & Biochemistry, and Molecular Biology Institute, UCLA, Los Angeles, CA, USA. sawaya@mbi.ucla.edu.
Jose A RodriguezDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA, USA. jrodriguez@mbi.ucla.edu.

Funding

Micro Electron Diffraction of Toxic and/or Infectious Macromolecular NanoassembliesR35GM128867 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Jose Alfonso Rodriguez · 2018 to 2026
$3.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM128867
6 · The paper itself

Abstract

Structural elucidation of small macromolecules such as peptides has recently been facilitated by a growing number of technological advances to existing crystallographic methods. The emergence of electron micro-diffraction (MicroED) of protein nanocrystals under cryogenic conditions has enabled the interrogation of crystalline peptide assemblies only hundreds of nanometers thick. Collection of atomic or near-atomic resolution data by these methods has permitted the ab initio determination of structures of various amyloid-forming peptides, including segments derived from prions and ice-nucleating proteins. This chapter focuses on the process of ab initio structural determination from nano-scale peptide assemblies and other similar molecules.

Indexed as

AmyloidMicroscopy, Electron, TransmissionNanoparticlesPeptidesAmyloidPeptidesAb initioAmyloidDirect methodsNanocrystalPeptide

Identifiers

PMID33368013
PMCPMC8726681

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.