49 results on '"Chubatsu, Leda S."'
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2. Crystal structure of the GlnZ-DraG complex reveals a different form of P II -target interaction
3. 2-Oxoglutarate levels control adenosine nucleotide binding by Herbaspirillum seropedicae PII proteins
4. Role of conserved cysteine residues in Herbaspirillum seropedicae NifA activity
5. Search for novel targets of the PII signal transduction protein in Bacteria identifies the BCCP component of acetyl-CoA carboxylase as a PII binding partner
6. The Protein-Protein Interaction Network Reveals a Novel Role of the Signal Transduction Protein PII in the Control of c-di-GMP Homeostasis in Azospirillum brasilense
7. Genome structure of the genus Azospirillum
8. Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria
9. ADP-ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB-dependent membrane sequestration of DraG
10. GlnB is specifically required for Azospirillum brasilense NifA activity in Escherichia coli
11. Genome Analysis of Entomopathogenic Bacillus sp. ABP14 Isolated from a Lignocellulosic Compost
12. Identification and characterization of PhbF: A DNA binding protein with regulatory role in the PHB metabolism of Herbaspirillum seropedicae SmR1
13. Role of PII proteins in nitrogen fixation control of Herbaspirillum seropedicae strain SmR1
14. The NtrY-NtrX two-component system is involved in controlling nitrate assimilation inHerbaspirillum seropedicaestrain SmR1
15. Fnr is involved in oxygen control of Herbaspirillum seropedicae N-truncated NifA protein activity in Escherichaia coli
16. Backup Expression of the PhaP2 Phasin Compensates for phaP1 Deletion in Herbaspirillum seropedicae, Maintaining Fitness and PHB Accumulation
17. Complete Genome Sequence of Herbaspirillum hiltneri N3 (DSM 17495), Isolated from Surface-Sterilized Wheat Roots
18. 2-Oxoglutarate levels control adenosine nucleotide binding byHerbaspirillum seropedicaePII proteins
19. The NtrY-NtrX two-component system is involved in controlling nitrate assimilation in Herbaspirillum seropedicae strain SmR1.
20. Dual RNA-seq transcriptional analysis of wheat roots colonized by Azospirillum brasilense reveals up-regulation of nutrient acquisition and cell cycle genes
21. Search for novel targets of the PIIsignal transduction protein in Bacteria identifies the BCCP component of acetyl-CoA carboxylase as a PIIbinding partner
22. Identification of Proteins Associated with Polyhydroxybutyrate Granules from Herbaspirillum seropedicae SmR1 - Old Partners, New Players
23. Draft Genome Sequence of Herbaspirillum huttiense subsp. putei IAM 15032, a Strain Isolated from Well Water
24. Influence of the ADP/ATP ratio, 2-oxoglutarate and divalent ions on Azospirillum brasilense PII protein signalling
25. Genomic comparison of the endophyte Herbaspirillum seropedicaeSmR1 and the phytopathogen Herbaspirillum rubrisubalbicansM1 by suppressive subtractive hybridization and partial genome sequencing
26. PII signal transduction proteins: pivotal players in post-translational control of nitrogenase activity
27. Identification and characterization of PhbF: A DNA binding protein with regulatory role in the PHB metabolism of Herbaspirillum seropedicae SmR1
28. Genome of Herbaspirillum seropedicae Strain SmR1, a Specialized Diazotrophic Endophyte of Tropical Grasses
29. Role of PII proteins in nitrogen fixation control of Herbaspirillum seropedicae strain SmR1
30. In Vitro Interactions between the PII Proteins and the Nitrogenase Regulatory Enzymes Dinitrogenase Reductase ADP-ribosyltransferase (DraT) and Dinitrogenase Reductase-activating Glycohydrolase (DraG) in Azospirillum brasilense
31. Expression, purification and DNA-binding activities of two putative ModE proteins of Herbaspirillum seropedicae (Burkholderiales, Oxalobacteraceae)
32. Interactions between PII proteins and the nitrogenase regulatory enzymes DraT and DraG in Azospirillum brasilense
33. ADP‐ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB‐dependent membrane sequestration of DraG
34. Repressor Mutant Forms of the Azospirillum brasilense NtrC Protein
35. Interactions between P II proteins and the nitrogenase regulatory enzymes DraT and DraG in Azospirillum brasilense
36. Comparative molecular analysis of Herbaspirillum strains by RAPD, RFLP, and 16S rDNA sequencing
37. Endophytic Herbaspirillum seropedicae expresses nif genes in gramineous plants
38. Inter-domain cross-talk controls the NifA protein activity ofHerbaspirillum seropedicae
39. Search for novel targets of the PII signal transduction protein in Bacteria identifies the BCCP component of acetyl- CoA carboxylase as a PII binding partner.
40. Implication of Mammalian Ribosomal Protein S3 in the Processing of DNA Damage
41. Identification of Proteins Associated with Polyhydroxybutyrate Granules from Herbaspirillum seropedicae SmR1 - Old Partners, New Players.
42. Glutathione is the antioxidant responsible for resistance to oxidative stress in V79 Chinese hamster fibroblasts rendered resistant to cadmium
43. Genomic comparison of the endophyte Herbaspirillum seropedicae Sm R1 and the phytopathogen Herbaspirillum rubrisubalbicans M1 by suppressive subtractive hybridization and partial genome sequencing.
44. Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction.
45. Interactions between PII proteins and the nitrogenase regulatory enzymes DraT and DraG in Azospirillum brasilense
46. Inter‐domain cross‐talk controls the NifA protein activity of Herbaspirillum seropedicae
47. In Vitro Interactions between the PII Proteins and the Nitrogenase Regulatory Enzymes Dinitrogenase Reductase ADP-ribosyltransferase (DraT) and Dinitrogenase Reductase-activating Glycohydrolase (DraG) in Azospirillum brasiIense.
48. Genomic comparison of the endophyte Herbaspirillum seropedicae SmR1 and the phytopathogen Herbaspirillum rubrisubalbicans M1 by suppressive subtractive hybridization and partial genome sequencing.
49. Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction.
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