ReviewInternational journal of molecular sciences2012
Structural analysis of hypothetical proteins from Helicobacter pylori: an approach to estimate functions of unknown or hypothetical proteins.
Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 24 citations in OpenAlex.
- HP0953 - hypothetical virulence factor overexpresion and localization duringWorld journal of gastroenterology · 2022Article
- Identification of Phytoconstituents as Potent Inhibitors of Casein Kinase-1 Alpha Using Virtual Screening and Molecular Dynamics Simulations.Pharmaceutics · 2021Article
- Protein-Coding Genes ofGenes · 2021Article
- Deciphering the functional role of hypothetical proteins fromMolecular biology research communications · 2020Article
- Crystal structure of the MSMEG_4306 gene product from Mycobacterium smegmatis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Genome scale identification, structural analysis, and classification of periplasmic binding proteins from Mycobacterium tuberculosis.Current genetics · 2017Article
- Structure-based functional annotation of putative conserved proteins having lyase activity from Haemophilus influenzae.3 Biotech · 2015Article
- Analysis of spatial and temporal protein expression in the cerebral cortex after ischemia-reperfusion injury.Journal of clinical neurology (Seoul, Korea) · 2014Article
- NMR study on small proteins from Helicobacter pylori for antibiotic target discovery: a review.Molecules (Basel, Switzerland) · 2013Review
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Helicobacter pylori (H. pylori) have a unique ability to survive in extreme acidic environments and to colonize the gastric mucosa. It can cause diverse gastric diseases such as peptic ulcers, chronic gastritis, mucosa-associated lymphoid tissue (MALT) lymphoma, gastric cancer, etc. Based on genomic research of H. pylori, over 1600 genes have been functionally identified so far. However, H. pylori possess some genes that are uncharacterized since: (i) the gene sequences are quite new; (ii) the function of genes have not been characterized in any other bacterial systems; and (iii) sometimes, the protein that is classified into a known protein based on the sequence homology shows some functional ambiguity, which raises questions about the function of the protein produced in H. pylori. Thus, there are still a lot of genes to be biologically or biochemically characterized to understand the whole picture of gene functions in the bacteria. In this regard, knowledge on the 3D structure of a protein, especially unknown or hypothetical protein, is frequently useful to elucidate the structure-function relationship of the uncharacterized gene product. That is, a structural comparison with known proteins provides valuable information to help predict the cellular functions of hypothetical proteins. Here, we show the 3D structures of some hypothetical proteins determined by NMR spectroscopy and X-ray crystallography as a part of the structural genomics of H. pylori. In addition, we show some successful approaches of elucidating the function of unknown proteins based on their structural information.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.