Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression.
about
Structural Characterizations of Glycerol Kinase: Unraveling Phosphorylation-Induced Long-Range Activation †Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operatorsEngineering of a glycerol utilization pathway for amino acid production by Corynebacterium glutamicumHigh- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysisTranscriptional activator YesS is stimulated by histidine-phosphorylated HPr of the Bacillus subtilis phosphotransferase system.A single mutation in enzyme I of the sugar phosphotransferase system confers penicillin tolerance to Streptococcus gordonii.The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Global transcriptome response in Lactobacillus sakei during growth on riboseGenetic and proteomic analysis of factors affecting serum cholesterol reduction by Lactobacillus acidophilus A4.Catabolite repression and activation in Bacillus subtilis: dependency on CcpA, HPr, and HprKA functional genomics approach to establish the complement of carbohydrate transporters in Streptococcus pneumoniae.Catabolite control protein A (CcpA) contributes to virulence and regulation of sugar metabolism in Streptococcus pneumoniae.Acetoin metabolism in bacteria.Identification and characterization of a fructose phosphotransferase system in Bifidobacterium breve UCC2003The Role of α-CTD in the Genome-Wide Transcriptional Regulation of the Bacillus subtilis Cells.Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent dihydroxyacetone kinase system connected to the pentose phosphate pathwayHow phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaThe phosphotransferase system of Lactobacillus casei: regulation of carbon metabolism and connection to cold shock response.Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose 6'-phosphate phosphatase (MapP).Glycerol metabolism and PrfA activity in Listeria monocytogenesCarbon catabolite repression by seryl phosphorylated HPr is essential to Streptococcus pneumoniae in carbohydrate-rich environments.Transcriptional Profile during Deoxycholate-Induced Sporulation in a Clostridium perfringens Isolate Causing Foodborne Illness.Basal levels of (p)ppGpp in Enterococcus faecalis: the magic beyond the stringent response.Nutritional control of antibiotic resistance via an interface between the phosphotransferase system and a two-component signaling system.The phosphoenolpyruvate phosphotransferase system in group A Streptococcus acts to reduce streptolysin S activity and lesion severity during soft tissue infection.In vivo activity of enzymatic and regulatory components of the phosphoenolpyruvate:sugar phosphotransferase system in Mycoplasma pneumoniaeThe Lactobacillus casei ptsHI47T mutation causes overexpression of a LevR-regulated but RpoN-independent operon encoding a mannose class phosphotransferase system.Glycerol metabolism is important for cytotoxicity of Mycoplasma pneumoniae.Glycerol is metabolized in a complex and strain-dependent manner in Enterococcus faecalisMultiple-mutation reaction: a method for simultaneous introduction of multiple mutations into the glpK gene of Mycoplasma pneumoniae.Determinants of interaction specificity of the Bacillus subtilis GlcT antitermination protein: functionality and phosphorylation specificity depend on the arrangement of the regulatory domains.The doubly phosphorylated form of HPr, HPr(Ser~P)(His-P), is abundant in exponentially growing cells of Streptococcus thermophilus and phosphorylates the lactose transporter LacS as efficiently as HPr(His~P).Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation. Elucidation of the phosphorylation chain leading to inactivation of GlcT.Glycerol metabolism of Lactobacillus rhamnosus ATCC 7469: cloning and expression of two glycerol kinase genes.Glycerol metabolism and its implication in virulence in Mycoplasma.Transcriptional adaptation of Shigella flexneri during adherence to epithelial cells.How seryl-phosphorylated HPr inhibits PrfA, a transcription activator of Listeria monocytogenes virulence genes.Improvement of glycerol catabolism in Bacillus licheniformis for production of poly-γ-glutamic acid.Rewiring glycerol metabolism for enhanced production of poly-γ-glutamic acid in
P2860
Q27653233-0DECE378-4F93-4898-8720-6FB2F0378824Q27666052-DFFBC472-E14B-44B2-A8A6-62BB288A22F7Q28756797-8C30DFB4-9411-435B-85AB-188E9377E7D0Q29346690-347CA514-F376-487E-9EBD-B65580E9D754Q33490034-206CEB9F-8483-4660-8770-51213D7F4006Q33559083-183C169D-4CD6-49E8-8D95-832AE473FB09Q33743505-37A8040E-E051-4900-88EB-E883A904C458Q33942335-6E398869-24F5-419A-95B4-46F156A3AA43Q33983528-8AFDB019-3C0C-4FF2-9D01-DBDA7E35B015Q34124360-E2BA5F33-037B-4396-A8A2-99A44405401FQ34200747-77DCD952-D54A-4AD8-BAB5-10A0A19A4C00Q34231050-E30FCE09-3E2E-4042-BFA3-43D44176A00FQ34635937-D87C4F09-B6C0-48D1-AFFC-563CDD64D23FQ35633450-D471E05E-D29A-46D2-B57F-E16F60FABD93Q35685980-F6362592-1096-4378-A88E-9F73DAD57E7EQ36197581-C135E72F-0FD7-4CCD-87A6-296856E5D49CQ36678721-E7D9659F-62B5-4EDD-B20A-869DE6791052Q36689766-3791BF72-07E7-417D-88B3-DA931F235A90Q36786340-EDBA6E60-6E99-44BF-A1F3-9C8649CBDFDAQ36804436-6F1F653A-BC7C-489F-9498-A09954021A26Q36813453-802F9429-AC71-4D4F-AD7D-11F485CC4DA6Q37121974-DC4A7C1E-36A1-46BD-85A2-832F4A29B4B2Q37194311-72EFF6AD-60E8-4E55-9A58-918C140B98B8Q37544839-D1182AD2-3AA4-40FB-BF3D-2E28FEAA5A6FQ37643839-3FC3B144-C4B2-4D2F-8BCC-9FDDBAAC05ECQ40420931-49327CF0-6E40-429F-975C-6D8CD8941345Q40993488-DAB54989-254F-452A-B293-035DF519A84AQ41825663-40A5559E-2200-45C5-8365-01B71870F5B8Q42139328-A2FEFD42-915F-4198-B0D3-607E240638D8Q42237879-E537133A-CF97-4233-9774-C92509FAF955Q42322238-54AFF4AA-76B8-460E-9D06-E1C0A8A4D246Q42705055-F63A5AD1-BF47-4D3B-935A-8AD6F92E9DFEQ44607657-A23E1846-A8F2-43B7-B7A2-CFA5F2F3AC50Q45071351-CDA428D9-0F65-4854-8B44-D67F31FB6CEFQ46298680-1D555057-5BC5-4F7E-821D-1F2D729BCDE1Q46431834-65CAD75A-1B3B-4272-9B5F-1AB8C46989F5Q46895959-FC0DA8AF-6F67-4EB6-BFF2-F521FDDB89DBQ47799091-1F26CDF5-CCFD-4A9B-9B6D-76696E32D82EQ59137016-5E604FD6-73DC-4D32-AB6E-1B890A8B52F9
P2860
Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Antitermination by GlpP, catab ...... lus subtilis glpFK expression.
@en
Antitermination by GlpP, catab ...... lus subtilis glpFK expression.
@nl
type
label
Antitermination by GlpP, catab ...... lus subtilis glpFK expression.
@en
Antitermination by GlpP, catab ...... lus subtilis glpFK expression.
@nl
prefLabel
Antitermination by GlpP, catab ...... lus subtilis glpFK expression.
@en
Antitermination by GlpP, catab ...... lus subtilis glpFK expression.
@nl
P2093
P2860
P1476
Antitermination by GlpP, catab ...... lus subtilis glpFK expression.
@en
P2093
Emmanuelle Darbon
Pascale Servant
Sandrine Poncet
P2860
P304
P356
10.1046/J.1365-2958.2002.02800.X
P407
P577
2002-02-01T00:00:00Z