Literature DB >> 26367146

Correction: High Resolution Crystal Structure of Human β-Glucuronidase Reveals Structural Basis of Lysosome Targeting.

Md Imtaiyaz Hassan, Abdul Waheed, Jeffery H Grubb, Herbert E Klei, Sergey Korolev, William S Sly.   

Abstract

Entities:  

Year:  2015        PMID: 26367146      PMCID: PMC4569263          DOI: 10.1371/journal.pone.0138401

Source DB:  PubMed          Journal:  PLoS One        ISSN: 1932-6203            Impact factor:   3.240


× No keyword cloud information.
Fig 1 is incorrect. Please see the corrected Fig 1 here.
Fig 1

Multiple sequence alignment of human GUS with mouse and bacterial GUS.

The percent sequence identities are given in parentheses. Completely conserved residues and homologous residues are shaded in dark and light grey, respectively. The secondary structure elements are given on the top of sequences, where α-helices are represented by blue rectangles, β-strands by green arrows. Domains 1, 2 and 3 are indicated by yellow, green and red line respectively, below the sequence. Conserved active site residues are highlighted in green boxes. Potential glycosylation sites are in pink. Glycosylation sites are in magenta boxes. Amino acid sequences of GUS were taken from the Uniprot database with their primary accession number as: human, P08236; mouse P12265; and E. coli, P05804.

Multiple sequence alignment of human GUS with mouse and bacterial GUS.

The percent sequence identities are given in parentheses. Completely conserved residues and homologous residues are shaded in dark and light grey, respectively. The secondary structure elements are given on the top of sequences, where α-helices are represented by blue rectangles, β-strands by green arrows. Domains 1, 2 and 3 are indicated by yellow, green and red line respectively, below the sequence. Conserved active site residues are highlighted in green boxes. Potential glycosylation sites are in pink. Glycosylation sites are in magenta boxes. Amino acid sequences of GUS were taken from the Uniprot database with their primary accession number as: human, P08236; mouse P12265; and E. coli, P05804.
  1 in total

1.  High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting.

Authors:  Md Imtaiyaz Hassan; Abdul Waheed; Jeffery H Grubb; Herbert E Klei; Sergey Korolev; William S Sly
Journal:  PLoS One       Date:  2013-11-19       Impact factor: 3.240

  1 in total
  2 in total

1.  Structural and Biophysical Characterization of Cajanus cajan Protease Inhibitor.

Authors:  Tooba Naz Shamsi; Romana Parveen; Shahzaib Ahamad; Sadaf Fatima
Journal:  J Nat Sci Biol Med       Date:  2017 Jul-Dec

2.  First Report of a Patient with MPS Type VII, Due to Novel Mutations in GUSB, Who Underwent Enzyme Replacement and Then Hematopoietic Stem Cell Transplantation.

Authors:  Patricia Dubot; Frédérique Sabourdy; Geneviève Plat; Charlotte Jubert; Claude Cancès; Pierre Broué; Guy Touati; Thierry Levade
Journal:  Int J Mol Sci       Date:  2019-10-28       Impact factor: 5.923

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.