GlobPlot protocols

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GlobPlot specifications


Unique identifier OMICS_03622
Name GlobPlot
Interface Web user interface
Restrictions to use None
Computer skills Basic
Version 2.0
Stability Stable
Maintained No

Publication for GlobPlot

GlobPlot in pipelines

PMCID: 5472282
PMID: 28617832
DOI: 10.1371/journal.pone.0179173

[…] defined as the negative of a sum of the products of amino acid frequencies in a typical repeat sequence (pi) and binary logarithms of those frequencies (log2(pi))., globularity was predicted using globplot []. the program identifies regions of globularity (order) and disorder within protein sequences. its approach is based on a running sum of the propensity for amino acids to be in an ordered […]

PMCID: 4756128
PMID: 26925067
DOI: 10.3389/fpls.2016.00097

[…] thérapeutique” université de lorraine) was appreciated., , href=" , , href=" , , , , , href=" […]

PMCID: 4756128
PMID: 26925067
DOI: 10.3389/fpls.2016.00097

[…] the phytozome portal (version 2.2, currently v3 assembly). sequence alignments were performed using the online programs multalin and clustalw. intrinsically disordered regions were predicted using globplot online. protein signal peptides were predicted on the signalp 3.0 server and protein parameters were calculated with the protparam program. disulfide bonds were predicted using the dianna […]

PMCID: 4817252
PMID: 27048799
DOI: 10.1128/mBio.00252-16

[…] acid sequence of agd3 from aspergillus fumigatus was obtained from the aspergillus genome database () and analyzed using a number of different web-based servers, including phyre2, signalp v3.0, globplot, netoglyc 4.0, and smart (, , ). the full-length sequence of agd3 was initially used for the bioinformatic analysis. as analysis of full-length agd3 using phyre2 failed to predict […]

PMCID: 4917548
PMID: 27445802
DOI: 10.3389/fphar.2016.00153

[…] vp4.bioedit v7.2.3 sequence alignment editor (hall, ) was used through multiple-sequence alignment (msa) with clustalw (thompson et al., ) to identify conserved sequences of different strains., globplot 2.3 ( was used to identify the protein disorder region of the vp4 protein of human rotavirus a., the automated protein modeling program modeller 9v11 (šali et al., ) […]

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GlobPlot in publications

PMCID: 5895634
PMID: 29643398
DOI: 10.1038/s41598-018-23969-0

[…] q8jux5]. previously, for disorder analysis, several specialized predictors have been developed, for example, pondr® pool [pondr® fit, pondr® vls2, pondr® vlxt], as well as iupred, disopred, disembl, globplot, spritz, and much more. to evaluate the precision of disorder predictors, several aforementioned tools were compared within the frames of the critical assessment of protein structure […]

PMCID: 5855623
PMID: 29385704
DOI: 10.3390/ijms19020401

[…] have been successfully achieved through bioinformatics, which is coping with a rapidly increasing number of genome sequences. examples of prediction tools in this category include disembl [], globplot [], pondr vsl1 [], disopred [], dispro [], and vsl2 []. we also developed different idp predictors, dichot [,], and a series of web applications named poodle [,,]. in this study, we designed […]

PMCID: 5793193
PMID: 29342086
DOI: 10.3390/genes9010042

[…] software [] to construct a phylogenetic tree., homologous construction of the tertiary structure of the sox6 proteins was carried out by swiss model []. the sox6 amino acid sequence was analyzed by globplot online software [] to predict the disordered region., both accucopy® (based on multiplex competitive amplification) [] and cnvplex® (based on the multiplex ligation-dependent probe […]

PMCID: 5747437
PMID: 29287083
DOI: 10.1371/journal.pone.0189905

[…] []. the results suggested that this protein is rich in β-turns in the region between 80 to 175 residues, which is the region where β-strands are oriented in anti-parallel to form β-sheets ()., globplot server (http://globplot.embl.deis) was used in order to predict the disordered and ordered (globular) regions within arabian camel hspb-1 protein. in this program, ordered regions […]

PMCID: 5753338
PMID: 29136216
DOI: 10.1093/nar/gkx1077

[…] is likely to generate many false positive predictions. any motifs likely to be non-functional are deprecated by applying structure and domain architecture filters based on protein disorder (from globplot () and iupred ()), protein secondary structure () and protein domains (from smart () and pfam ()). the result contains putative slims located in disordered regions that are accessible […]

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GlobPlot institution(s)
European Molecular Biology Laboratory, Biocomputing Unit, Heidelberg, Germany

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