Hiten M. Patel - Publications
Affiliations: | 2003 | Harvard University, Cambridge, MA, United States |
Year | Citation | Score | |||
---|---|---|---|---|---|
2004 | Reimmann C, Patel HM, Walsh CT, Haas D. PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa. Journal of Bacteriology. 186: 6367-73. PMID 15375116 DOI: 10.1128/Jb.186.19.6367-6373.2004 | 0.585 | |||
2003 | Patel HM, Tao J, Walsh CT. Epimerization of an L-cysteinyl to a D-cysteinyl residue during thiazoline ring formation in siderophore chain elongation by pyochelin synthetase from Pseudomonas aeruginosa. Biochemistry. 42: 10514-27. PMID 12950179 DOI: 10.1021/Bi034840C | 0.522 | |||
2001 | Forbes AJ, Mazur MT, Patel HM, Walsh CT, Kelleher NL. Toward efficient analysis of >70 kDa proteins with 100% sequence coverage. Proteomics. 1: 927-33. PMID 11683509 DOI: 10.1255/Ejms.393 | 0.553 | |||
2001 | Walsh CT, Chen H, Keating TA, Hubbard BK, Losey HC, Luo L, Marshall CG, Miller DA, Patel HM. Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines. Current Opinion in Chemical Biology. 5: 525-34. PMID 11578925 DOI: 10.1016/S1367-5931(00)00235-0 | 0.516 | |||
2001 | Patel HM, Walsh CT. In vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities. Biochemistry. 40: 9023-31. PMID 11467965 DOI: 10.1021/Bi010519N | 0.569 | |||
2001 | Reimmann C, Patel HM, Serino L, Barone M, Walsh CT, Haas D. Essential PchG-dependent reduction in pyochelin biosynthesis of Pseudomonas aeruginosa. Journal of Bacteriology. 183: 813-20. PMID 11208777 DOI: 10.1128/Jb.183.3.813-820.2001 | 0.421 | |||
1999 | Quadri LE, Keating TA, Patel HM, Walsh CT. Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF. Biochemistry. 38: 14941-54. PMID 10555976 DOI: 10.1021/Bi991787C | 0.583 | |||
Show low-probability matches. |