Evidence map›Paper›PMID 16505963›Full record

ArticleJournal of biomolecular NMR2006

PASA--a program for automated protein NMR backbone signal assignment by pattern-filtering approach.

Yizhuang Xu, Xiaoxia Wang, Jun Yang, Julia Vaynberg, Jun Qin

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Article in Journal of biomolecular NMR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

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0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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.

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3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

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  12. Structural mechanism of integrin inactivation by filamin.Nature structural & molecular biology · 2015
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  19. Automated structure determination from NMR spectra.European biophysics journal : EBJ · 2009
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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Yizhuang XuStructural Biology Program, NB20, The Lerner Research Institute, The Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195, USA.
Xiaoxia Wang
Jun Yang
Julia Vaynberg
Jun Qin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present a new program, PASA (Program for Automated Sequential Assignment), for assigning protein backbone resonances based on multidimensional heteronuclear NMR data. Distinct from existing programs, PASA emphasizes a per-residue-based pattern-filtering approach during the initial stage of the automated 13Calpha and/or 13Cbeta chemical shift matching. The pattern filter employs one or multiple constraints such as 13Calpha/Cbeta chemical shift ranges for different amino acid types and side-chain spin systems, which helps to rule out, in a stepwise fashion, improbable assignments as resulted from resonance degeneracy or missing signals. Such stepwise filtering approach substantially minimizes early false linkage problems that often propagate, amplify, and ultimately cause complication or combinatorial explosion of the automation process. Our program (http://www.lerner.ccf.org/moleccard/qin/) was tested on four representative small-large sized proteins with various degrees of resonance degeneracy and missing signals, and we show that PASA achieved the assignments efficiently and rapidly that are fully consistent with those obtained by laborious manual protocols. The results demonstrate that PASA may be a valuable tool for NMR-based structural analyses, genomics, and proteomics.

Indexed as

Nuclear Magnetic Resonance, BiomolecularSoftwareAlgorithmsAmino Acid SequenceMolecular Sequence DataProtein ConformationProteinsProteins

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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.