Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
about
Staphylococcus aureus biofilms: properties, regulation, and roles in human diseaseStructure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaSIntegral and peripheral association of proteins and protein complexes with Yersinia pestis inner and outer membranesSystems-wide temporal proteomic profiling in glucose-starved Bacillus subtilisA proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.Identification of Staphylococcus aureus proteins recognized by the antibody-mediated immune response to a biofilm infection.LocateP: genome-scale subcellular-location predictor for bacterial proteins.Proteomics-based identification of anchorless cell wall proteins as vaccine candidates against Staphylococcus aureusProteomic analysis of iron acquisition, metabolic and regulatory responses of Yersinia pestis to iron starvation.Proteomic analysis of Staphylococcus aureus biofilm cells grown under physiologically relevant fluid shear stress conditions.Identification of a novel Staphylococcus aureus two-component leukotoxin using cell surface proteomics.Using chemical derivatization and mass spectrometric analysis to characterize the post-translationally modified Staphylococcus aureus surface protein GEnzymatic activities and functional interdependencies of Bacillus subtilis lipoteichoic acid synthesis enzymesRecombinant expression and functional analysis of proteases from Streptococcus pneumoniae, Bacillus anthracis, and Yersinia pestis.Vaccine development in Staphylococcus aureus: taking the biofilm phenotype into consideration.saeRS and sarA act synergistically to repress protease production and promote biofilm formation in Staphylococcus aureus.Extracellular proteases are key mediators of Staphylococcus aureus virulence via the global modulation of virulence-determinant stability.The Shigella dysenteriae serotype 1 proteome, profiled in the host intestinal environment, reveals major metabolic modifications and increased expression of invasive proteins.Identification of peptidoglycan-associated proteins as vaccine candidates for enterococcal infections.Immunorelevant proteins for the diagnosis of bovine staphylococcal mastitis.Staphylococcus aureus seroproteomes discriminate ruminant isolates causing mild or severe mastitisGenome transplantation in bacteria: changing one species to another.Proteome analysis and serological characterization of surface-exposed proteins of Rickettsia heilongjiangensisProteolytic cleavage inactivates the Staphylococcus aureus lipoteichoic acid synthaseEpidemic MRSA clone ST22-IV is more resistant to multiple host- and environment-related stresses compared with ST228-I.Surface-exposed proteins of Ehrlichia chaffeensis.Characterization of Early-Phase Neutrophil Extracellular Traps in Urinary Tract InfectionsEffect of Substance P in Staphylococcus aureus and Staphylococcus epidermidis Virulence: Implication for Skin HomeostasisTwo-dimensional gel electrophoresis in bacterial proteomics.Multiple genome comparison within a bacterial species reveals a unit of evolution spanning two adjacent genes in a tandem paralog cluster.Comparison of two label-free global quantitation methods, APEX and 2D gel electrophoresis, applied to the Shigella dysenteriae proteome.The Spl Serine Proteases Modulate Staphylococcus aureus Protein Production and Virulence in a Rabbit Model of Pneumonia.Analysis of the proteome of intracellular Shigella flexneri reveals pathways important for intracellular growth.Membrane proteins and proteomics: love is possible, but so difficult.Biofilm matrix exoproteins induce a protective immune response against Staphylococcus aureus biofilm infection.Identification of commonly expressed exoproteins and proteolytic cleavage events by proteomic mining of clinically relevant UK isolates of Staphylococcus aureus.Identifying potential therapeutic targets of methicillin-resistant Staphylococcus aureus through in vivo proteomic analysis.The cell surface proteome of Staphylococcus aureus.Current methodologies for proteomics of bacterial surface-exposed and cell envelope proteins.Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and alpha-(1->3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans.
P2860
Q27006715-F7BEB5A9-8570-4F18-90E3-90457CEEEA4AQ27653515-4BCF3EF9-6676-4641-8A5B-E3ED117B28FCQ30157353-D495CCA7-9513-4A94-B50A-49AC187BF072Q30500770-FC969390-53FB-4981-9BC2-6594B714C25FQ30974252-730A937C-E03B-46CE-816B-D8DFDE48F032Q33244198-348CCABF-951D-49CC-A9DC-9A38BE28D1D5Q33316216-06559E2C-5936-4050-8E27-A89CDAB46696Q33429774-E8891EEB-47B5-4E75-872D-9DD78A79CEC4Q33527554-DCAF1471-F4B1-43AC-8ABA-CF6507CF0FB7Q33578359-5D6F9BF7-FEEF-4180-A395-AD243B79728CQ33641315-68120A3B-F342-4414-84B4-A3F3EDAB5970Q33771587-A201659B-EB5B-46EF-A9F7-37138772236BQ33799750-02B3BF75-E2EF-4591-B827-76EC2BDAE3E4Q33890598-D10D343B-0390-4170-B589-4C6F5899EE03Q34113328-BAEE6F5D-B1DB-45F8-91D5-E72A6151200AQ34299637-A9EAE348-0AE0-40C1-B683-FA2C0A2560E4Q34317076-63640E13-6CB5-4527-B8A6-1F3BA87465D9Q34402880-2A17D103-1A18-41D1-82AF-6087D5F9F3F0Q34450707-E1FD1B6D-B162-4889-A235-295BC112CA7EQ34578080-C4693380-B701-4D3B-98EE-96107141D367Q34639298-B02F350A-A4B3-48CB-B4F5-B4C1EE5DB695Q34643428-56D82D86-D733-48C7-859C-EFA2BE8BD567Q34876423-BAD109AD-96AF-4B90-A1A2-0B77D5ADC6B4Q35274055-E727D921-38DE-4E14-B0F8-A06B3E326D6DQ35454113-4FAF4082-BD18-4334-9684-885E6356969AQ35949683-93897529-9B8F-4C36-B18C-F364C188748FQ36262668-9A6AB529-29E1-4BDD-B9DE-3194181C5B01Q36799709-3CE66B53-E9FE-4D4E-9D72-AF248F2AF586Q36923034-59A03FE2-B7F1-43A8-B718-0479C20E4AF3Q36938929-6F18DECB-EC7F-4E22-AF77-F1246EA7610CQ37276634-A801DF66-8B19-443C-B6C2-A928BBCFEE29Q37335319-8844A662-8E41-4620-A1D1-3E1F806A0412Q37336082-CB24C12F-5A6B-4656-BD19-4EF16DDE36DDQ37515143-AB71E473-B199-4763-A380-F595FA5EDE85Q37643833-3FED9D08-9456-4B6C-A67A-36AB8E1B77E0Q37658080-DBAD03EF-E1CD-416D-9E61-35E2401EFA10Q37719739-5D9A1355-EEB5-46FC-847F-B4F7D99CF609Q37883257-C1B69496-23EB-4521-A560-4B8EC9703B06Q37897206-4C14FD7D-B148-488B-86C7-1E33F1B188BCQ38354334-1C8A6433-0773-4B6D-86D4-68FB685CEFA2
P2860
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
@ast
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
@en
type
label
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
@ast
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
@en
prefLabel
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
@ast
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
@en
P2093
P356
P1433
P1476
Proteomic profiling of cell envelope-associated proteins from Staphylococcus aureus.
@en
P2093
Christine L Gatlin
Elizabeth Gebregeorgis
Emmanuel Mongodin
Hamid Alami
Leka Papazisi
Prashanth P Parmar
Rembert Pieper
Robert D Fleischmann
Scott N Peterson
Shih-Ting Huang
P2860
P304
P356
10.1002/PMIC.200500253
P577
2006-03-01T00:00:00Z