Add to ORKGThe LysM (lysin motif) domain is a small globular domain of 42-65 amino acids long that is widely distributed in nature, it can be found in procaryotes and eucaryotes in more than 4000 proteins. One to 12 LysM domains bind to N-acetylglucosamine residues of bacterial peptidoglycan (PG) in a non-covalently way. The binding between proteins with LysM domains and PG is strong and stable; it can only be separated under harsh reducing conditions. This can be useful for antigen display on the surface of bacterial PG for immunization purposes. It has been reported that the number of LysM motifs in proteins affects the efficiency of the binding of foreign proteins to the PG. Proteins with LysM domains can be difficult to express in a heterologous s...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner ...
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner ...
The lysin motif (LysM) is a ubiquitous motif across kingdoms, which in bacteria allows cell wall deg...
We characterized two LysM domains of Limosilactobacillus fermentum, belonging to proteins Acglu (Gen...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
Abstract We characterized two LysM domains of Limosilactobacillus fermentum, belonging to proteins A...
Abstract The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent stu...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
Lysin motif (LysM) domains are found in many bacterial peptidoglycan hydrolases. They can bind non-c...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner ...
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner ...
The lysin motif (LysM) is a ubiquitous motif across kingdoms, which in bacteria allows cell wall deg...
We characterized two LysM domains of Limosilactobacillus fermentum, belonging to proteins Acglu (Gen...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has...
Abstract We characterized two LysM domains of Limosilactobacillus fermentum, belonging to proteins A...
Abstract The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent stu...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
Lysin motif (LysM) domains are found in many bacterial peptidoglycan hydrolases. They can bind non-c...
A novel display system is described that allows highly efficient immobilization of heterologous prot...
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner ...
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner ...