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Crystallographic and microcalo...
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Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
Show other versions (1)
Bibliografiske detaljer
Main Authors:
Stamp, A
,
Owen, P
,
El Omari, K
,
Lockyer, M
,
Lamb, H
,
Charles, I
,
Hawkins, A
,
Stammers, D
Format:
Journal article
Sprog:
English
Udgivet:
2011
Beholdninger
Beskrivelse
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Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein...
af
Stamp, A
,
Owen, P
,
El Omari, K
,
Lockyer, M
,
Lamb, H
,
Charles, I
,
Hawkins, A
,
Stammers, D
Udgivet 2011
Journal article
Show all versions (2)
Lignende værker
Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351
af: Stamp, A, et al.
Udgivet: (2011)
Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: an unusual Type II glyoxalase.
af: Stamp, A, et al.
Udgivet: (2010)
Genomic comparison of Salmonella enterica serovars and Salmonella bongori by use of an S. enterica serovar typhimurium DNA microarray.
af: Chan, K, et al.
Udgivet: (2003)
Changes in Antimicrobial Resistance in Salmonella enterica Serovar Typhimurium
af: Frederick J. Angulo, et al.
Udgivet: (2000-08-01)
Salmonella enterica Serovar Typhimurium Strategies for Host Adaptation
af: Christopher J. Anderson, et al.
Udgivet: (2017-10-01)