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Plos Biology|March 16, 2007
The Sorcerer II Global Ocean Sampling expedition: expanding the universe of protein familiesShibu Yooseph, Granger Sutton, Douglas B Rusch, et al.
Emerging Infectious Diseases|April 13, 2023
US National Institutes of Health Prioritization of SARS-CoV-2 VariantsSam Turner, Arghavan Alisoltani, Debbie Bratt, et al.
Genome Medicine|December 20, 2017
Mapping genetic variations to three-dimensional protein structures to enhance variant interpretation: a proposed frameworkGustavo Glusman, Peter W Rose, Andreas Prlić, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|October 15, 2010
Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolutionQingping Xu, Daniel McMullan, Lukasz Jaroszewski, et al.
Plos Computational Biology|October 28, 2021
Crowdsourcing biocuration: The Community Assessment of Community Annotation with Ontologies (CACAO)Jolene Ramsey, Brenley McIntosh, Daniel Renfro, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|October 15, 2010
The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding roleS Sri Krishna, L Aravind, Constantina Bakolitsa, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|October 15, 2010
Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelationMitchell D Miller, L Aravind, Constantina Bakolitsa, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|October 15, 2010
Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolismHsiu Ju Chiu, Constantina Bakolitsa, Arne Skerra, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|October 15, 2010
The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymesHsiu Ju Chiu, Polat Abdubek, Tamara Astakhova, et al.
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