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Science, ISSN 0036-8075, 1/2012, Volume 335, Issue 6064, pp. 85 - 88
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2011, Volume 108, Issue 52, pp. 21259 - 21264
Journal Article
JOURNAL OF BACTERIOLOGY, ISSN 0021-9193, 07/2019, Volume 201, Issue 14, p. 1
We characterized an operon in Mycobacterium tuberculosis, Rv3679-Rv3680, in which each open reading frame is annotated to encode "anion transporter ATPase"... 
Mycobacterium | CATALYTIC SUBUNIT | ATP HYDROLYSIS | PROTEOME | DNA MISMATCH | tuberculosis | PROTEASOME | RESISTANCE | MICROBIOLOGY | Get3 | ARSA ATPASE | GENOME | Membranes | Crystal defects | Pathogenesis | Homology | Nucleotides | Proteins | Anions | Eukaryotes | Tuberculosis | Clonal deletion | Endoplasmic reticulum | Transporter | Adenosine triphosphatase | Crystal structure
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2014, Volume 9, Issue 12, p. e113643
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2018, Volume 115, Issue 41, pp. E9560 - E9569
The protein disaggregase ClpB hexamer is conserved across evolution and has two AAA+-type nucleotide-binding domains, NBD1 and NBD2, in each protomer. In M.... 
AAA-ATPase | Proteostasis | Mycobacterium tuberculosis | Cryo-EM | Disaggregase | SYSTEM | HSP104 | HSP70 | MULTIDISCIPLINARY SCIENCES | proteostasis | DISAGGREGATION | disaggregase | DNAK | MOLECULAR CHAPERONE | PROTEINS | cryo-EM | CRYO-EM STRUCTURE | Physiological aspects | Genetic aspects | Translocation (Genetics) | Peptides | Observations | Biological Sciences | PNAS Plus
Journal Article
Nature, ISSN 0028-0836, 3/2018, Volume 555, Issue 7696, pp. 328 - 333
N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction... 
Journal Article