ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization of Saccharomyces cerevisiae alpha-mannosidase, a cargo protein of the Cvt pathway.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Genomic Landscape Underlying Biofilm Formation Diversity in Nakaseomyces glabratus Clinical Isolates.MicrobiologyOpen · 2026Article
- Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.FEBS open bio · 2020Article
- Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.EMBO reports · 2016Article
- Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34.The Journal of biological chemistry · 2010Article
- Structure and kinetic investigation of Streptococcus pyogenes family GH38 alpha-mannosidase.PloS one · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saccharomyces cerevisiae alpha-mannosidase (Ams1) is a cargo protein that is transported to the vacuole by the cytoplasm-to-vacuole targeting (Cvt) pathway during conditions of growth and by autophagy during conditions of starvation. After transport to the vacuole, Ams1 functions as a resident hydrolase. Ams1 has been overexpressed in the methylotrophic yeast Pichia pastoris, purified and crystallized in two crystal forms. Form I belongs to space group P2(1), with unit-cell parameters a = 145.7, b = 127.7, c = 164.0 A, beta = 101.5 degrees . Form II belongs to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 127.9, b = 163.7, c = 291.5 A. Diffraction data were collected from these crystals to a resolution of 3.3 A for form I and of 2.6 A for form II using synchrotron radiation.
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Registered trials
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