These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Journal Abstract Search
116 related items for PubMed ID: 7984101
1. Membrane association and role in DNA uptake of the Bacillus subtilis PriA analogue ComF1. Londoño-Vallejo JA, Dubnau D. Mol Microbiol; 1994 Jul; 13(2):197-205. PubMed ID: 7984101 [Abstract] [Full Text] [Related]
4. comF, a Bacillus subtilis late competence locus, encodes a protein similar to ATP-dependent RNA/DNA helicases. Londoño-Vallejo JA, Dubnau D. Mol Microbiol; 1993 Jul; 9(1):119-31. PubMed ID: 8412657 [Abstract] [Full Text] [Related]
5. The competence transcription factor of Bacillus subtilis recognizes short A/T-rich sequences arranged in a unique, flexible pattern along the DNA helix. Hamoen LW, Van Werkhoven AF, Bijlsma JJ, Dubnau D, Venema G. Genes Dev; 1998 May 15; 12(10):1539-50. PubMed ID: 9585513 [Abstract] [Full Text] [Related]
6. Role of ComEA in DNA uptake during transformation of competent Bacillus subtilis. Takeno M, Taguchi H, Akamatsu T. J Biosci Bioeng; 2012 Jun 15; 113(6):689-93. PubMed ID: 22398145 [Abstract] [Full Text] [Related]
7. Single-Molecule Dynamics of DNA Receptor ComEA, Membrane Permease ComEC, and Taken-Up DNA in Competent Bacillus subtilis Cells. Burghard-Schrod M, Kilb A, Krämer K, Graumann PL. J Bacteriol; 2022 Mar 15; 204(3):e0057221. PubMed ID: 34928178 [Abstract] [Full Text] [Related]
8. The contrahelicase activities of the replication terminator proteins of Escherichia coli and Bacillus subtilis are helicase-specific and impede both helicase translocation and authentic DNA unwinding. Sahoo T, Mohanty BK, Lobert M, Manna AC, Bastia D. J Biol Chem; 1995 Dec 08; 270(49):29138-44. PubMed ID: 7493939 [Abstract] [Full Text] [Related]
9. Mutation of the putative nucleotide binding site of the Bacillus subtilis membrane protein ComFA abolishes the uptake of DNA during transformation. Londoño-Vallejo JA, Dubnau D. J Bacteriol; 1994 Aug 08; 176(15):4642-5. PubMed ID: 8045895 [Abstract] [Full Text] [Related]
11. Cell surface localization and processing of the ComG proteins, required for DNA binding during transformation of Bacillus subtilis. Chung YS, Breidt F, Dubnau D. Mol Microbiol; 1998 Aug 08; 29(3):905-13. PubMed ID: 9723928 [Abstract] [Full Text] [Related]
12. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Provvedi R, Dubnau D. Mol Microbiol; 1999 Jan 08; 31(1):271-80. PubMed ID: 9987128 [Abstract] [Full Text] [Related]
13. Transformation proteins and DNA uptake localize to the cell poles in Bacillus subtilis. Hahn J, Maier B, Haijema BJ, Sheetz M, Dubnau D. Cell; 2005 Jul 15; 122(1):59-71. PubMed ID: 16009133 [Abstract] [Full Text] [Related]
15. Fluorescently Labeled DNA Interacts with Competence and Recombination Proteins and Is Integrated and Expressed Following Natural Transformation of Bacillus subtilis. Boonstra M, Vesel N, Kuipers OP. mBio; 2018 Sep 25; 9(5):. PubMed ID: 30254116 [Abstract] [Full Text] [Related]
16. DnaB, DnaD and DnaI proteins are components of the Bacillus subtilis replication restart primosome. Bruand C, Farache M, McGovern S, Ehrlich SD, Polard P. Mol Microbiol; 2001 Oct 25; 42(1):245-55. PubMed ID: 11679082 [Abstract] [Full Text] [Related]
17. A Conserved Metal Binding Motif in the Bacillus subtilis Competence Protein ComFA Enhances Transformation. Chilton SS, Falbel TG, Hromada S, Burton BM. J Bacteriol; 2017 Aug 01; 199(15):. PubMed ID: 28559293 [Abstract] [Full Text] [Related]
18. Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a lipoprotein as part of a binding protein-dependent transport system. Schneider R, Hantke K. Mol Microbiol; 1993 Apr 01; 8(1):111-21. PubMed ID: 8388528 [Abstract] [Full Text] [Related]
19. Mechanisms of Transforming DNA Uptake to the Periplasm of Bacillus subtilis. Hahn J, DeSantis M, Dubnau D. mBio; 2021 Jun 29; 12(3):e0106121. PubMed ID: 34126763 [Abstract] [Full Text] [Related]