geneworks v2.5.1 (GeneWorks)
90
Structured Review
GeneWorks
geneworks v2.5.1

Geneworks V2.5.1, supplied by GeneWorks, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pmc02174577-60-6-5?v=GeneWorks
Average 90 stars, based on 1 article reviews

Geneworks V2.5.1, supplied by GeneWorks, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pmc02174577-60-6-5?v=GeneWorks
Average 90 stars, based on 1 article reviews
geneworks v2.5.1 - by Bioz Stars,
2026-08
90/100 stars
Images
1) Product Images from "Caenorhabditis elegans β-G Spectrin Is Dispensable for Establishment of Epithelial Polarity, but Essential for Muscular and Neuronal Function"
Article Title: Caenorhabditis elegans β-G Spectrin Is Dispensable for Establishment of Epithelial Polarity, but Essential for Muscular and Neuronal Function
Journal: The Journal of Cell Biology
doi:
Figure Legend Snippet: Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks v2.5.1 software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Techniques Used: Software