Structure of bacteriophage SPN1S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity
about
Breaking barriers: expansion of the use of endolysins as novel antibacterials against Gram-negative bacteria.Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue.Dissecting the structure-function relationship in lysozyme domain of mycobacteriophage D29-encoded peptidoglycan hydrolase.
P2860
Structure of bacteriophage SPN1S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity
description
2014 nî lūn-bûn
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2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
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2014年論文
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2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
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name
Structure of bacteriophage SPN ...... can lytic and binding activity
@ast
Structure of bacteriophage SPN ...... can lytic and binding activity
@en
Structure of bacteriophage SPN ...... can lytic and binding activity
@nl
type
label
Structure of bacteriophage SPN ...... can lytic and binding activity
@ast
Structure of bacteriophage SPN ...... can lytic and binding activity
@en
Structure of bacteriophage SPN ...... can lytic and binding activity
@nl
prefLabel
Structure of bacteriophage SPN ...... can lytic and binding activity
@ast
Structure of bacteriophage SPN ...... can lytic and binding activity
@en
Structure of bacteriophage SPN ...... can lytic and binding activity
@nl
P2093
P2860
P356
P1476
Structure of bacteriophage SPN ...... can lytic and binding activity
@en
P2093
Jeong-A Lim
Minsuk Kong
Sangkee Rhee
Sangryeol Ryu
Yangshin Park
P2860
P304
P356
10.1111/MMI.12555
P407
P577
2014-04-01T00:00:00Z