about
SMART: a web-based tool for the study of genetically mobile domains.Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotesMultiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potentialAn Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands.Determinants of the Src Homology Domain 3-Like FoldStructural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid EndopeptidaseStructure ofStenotrophomonas maltophiliaFeoA complexed with zinc: a unique prokaryotic SH3-domain protein that possibly acts as a bacterial ferrous iron-transport activating factorThe C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motifSH3 domains: modules of protein-protein interactions.Functional and structural characterization of a novel putative cysteine protease cell wall-modifying multi-domain enzyme selected from a microbial metagenome.Immunogenicity and Protective Response Induced by Recombinant Plasmids Based on the BAB1_0267 and BAB1_0270 Open Reading Frames of Brucella abortus 2308 in BALB/c Mice.Insights into Substrate Specificity of NlpC/P60 Cell Wall Hydrolases Containing Bacterial SH3 DomainsX-ray structure of a novel endolysin encoded by episomal phage phiSM101 of Clostridium perfringens.Expression, purification and preliminary crystallographic studies of the C-terminal SH3 domain of human Tks4.Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges.The structure and function of proline recognition domains.Adaptability in protein structures: structural dynamics and implications in ligand design.Peptidoglycan hydrolase fusions maintain their parental specificitiesStaphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'Genetic characterization of mycobacterial L,D-transpeptidases.Analysis of the peptidoglycan hydrolase complement of Lactobacillus casei and characterization of the major γ-D-glutamyl-L-lysyl-endopeptidaseThe YARHG domain: an extracellular domain in search of a function.Bacteriophage endolysins as novel antimicrobials.Deletion of the gene encoding p60 in Listeria monocytogenes leads to abnormal cell division and loss of actin-based motility.Endopeptidase and glycosidase activities of the bacteriophage B30 lysinEvolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection.Discovery of novel S. aureus autolysins and molecular engineering to enhance bacteriolytic activity.Synergistic streptococcal phage λSA2 and B30 endolysins kill streptococci in cow milk and in a mouse model of mastitis.RETRACTED: Identification of Peptidoglycan Hydrolase Constructs with Synergistic Staphylolytic Activity in Cow's Milk.Competence-induced fratricide in streptococci.Bacterial peptidoglycan (murein) hydrolases.Combination therapy with lysin CF-301 and antibiotic is superior to antibiotic alone for treating methicillin-resistant Staphylococcus aureus-induced murine bacteremia.ABC transporters involved in export of cell surface glycoconjugates.The structure and function of mammalian membrane-attack complex/perforin-like proteins.Delineation of the Salmonella enterica serovar Typhimurium HilA regulon through genome-wide location and transcript analysisA J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri.Streptococcus mutans murein hydrolase.The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain.
P2860
Q24515301-650F4C51-AD31-41A9-B421-734A12BBB215Q24814988-96CB3007-350A-4A3C-A7D8-573492EC521FQ27346739-0BD7BF4D-408B-4A11-867B-B57D88269D35Q27636252-0AB06B3D-3366-4602-BA24-7C3E195D84BAQ27639901-D782923F-1291-4965-9A04-94C8BEEB595AQ27641586-97026D7F-1E0C-43C3-ABD4-7F0A95E29837Q27653800-E805A63F-109F-4C25-B777-67C5B792B508Q27662083-710217F3-58D4-4EC2-9E1B-26AE679010B7Q28213947-1C719F97-B5B0-4A57-8DDF-060CD418F88CQ30008731-6806F51F-8CEE-4CDB-A4B6-F4106A098163Q30008807-4645C71A-7598-40C4-8590-41E06F3284E1Q30008850-C9DDA136-B367-4E80-AFE6-D95CA31F5B20Q30009099-748F042B-C74D-42D8-9704-CA1297F400BAQ30009441-8AAC5B10-54E4-4F7F-BB75-5CE8DB12326CQ30009477-B40132E1-AF12-443C-8B1E-C24097EFACFDQ30160087-074946D2-B8C3-46FD-81BB-561AAEB9167CQ30164765-4C87302F-8F12-4EBE-A61A-5FC627321B18Q30357974-54C5BF56-65B2-4517-B308-AE6FD1CFAA3BQ30446323-B447D735-2107-4556-BF37-A118548D01CAQ33775374-9B674798-4275-4301-B993-9F34083AE2E2Q33980489-5C2EE068-3F22-4BDB-B1F6-4862A0FABAC6Q34182492-1C9D08B8-4A32-4F72-867A-6DEA1A03D1CCQ34277178-D0EB03F9-1B96-4AE5-8ABA-87B79E701A14Q34303439-7A267BB7-7927-4BD2-9FCC-2785F24859D6Q35011378-722A6CCD-F8D2-4E89-912D-E8583F915C8EQ35091838-C2CEC75C-3DFB-46EC-AD5B-A8C99CF4FB3AQ35432724-6F73AA5E-027F-4642-AC0E-975C38CB92ADQ35842148-77C241A2-5392-4EAE-936D-37774ED4A74DQ36070204-B75BC387-2D72-432E-8A78-2C3CFF8F95C3Q36270490-4839F255-2862-42D8-87D4-E98B8DAFC4A0Q36842820-730B62F7-019F-445F-8546-1EE93D56F4E4Q37081704-DEDAFBDD-E6C3-424F-B66C-785A152545A5Q37696606-7B2F7CA4-D32B-4A29-AE21-67768FF7818AQ37784106-F5CF831A-C958-4DD7-8746-B463604CFD14Q37791183-BBA0D1A0-D90E-451D-A6D7-FCD6FA2B48C9Q38302051-EB6B3387-BA6C-47A6-A361-0E42724D7081Q39187608-D434110F-3DA5-4F8D-9532-F41527368122Q39603320-6EF6863F-532D-428C-9056-30567805F960Q39614597-901CB351-6B87-434F-B980-684CBE3CC240Q41487168-445530E9-71C9-4C81-ABAA-C4E3563895B9
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
SH3 domains in prokaryotes.
@ast
SH3 domains in prokaryotes.
@en
type
label
SH3 domains in prokaryotes.
@ast
SH3 domains in prokaryotes.
@en
prefLabel
SH3 domains in prokaryotes.
@ast
SH3 domains in prokaryotes.
@en
P1476
SH3 domains in prokaryotes.
@en
P2093
Whisstock JC
P304
P356
10.1016/S0968-0004(99)01366-3
P577
1999-04-01T00:00:00Z