Optimization of a β-Lactam Scaffold for Antibacterial Activity via the Inhibition of Bacterial Type I Signal Peptidase.

about

Optimization of a β-Lactam Scaffold for Antibacterial Activity via the Inhibition of Bacterial Type I Signal Peptidase.

Item

http://www.wikidata.org/entity/Q52579064

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Optimization of a β-Lactam Sca ...... erial Type I Signal Peptidase.

@en

Optimization of a β-Lactam Sca ...... erial Type I Signal Peptidase.

@nl

type

Item

label

Optimization of a β-Lactam Sca ...... erial Type I Signal Peptidase.

@en

Optimization of a β-Lactam Sca ...... erial Type I Signal Peptidase.

@nl

prefLabel

Optimization of a β-Lactam Sca ...... erial Type I Signal Peptidase.

@en

Optimization of a β-Lactam Sca ...... erial Type I Signal Peptidase.

@nl

P1476

Optimization of a β-Lactam Sca ...... terial Type I Signal Peptidase

@en

P2093

Ana-Florina Voica

http://www.w3.org/2001/XMLSchema#string

Arryn Craney

http://www.w3.org/2001/XMLSchema#string

M Greg Tabor

http://www.w3.org/2001/XMLSchema#string

Shawn I Walsh

http://www.w3.org/2001/XMLSchema#string

Sydney E Morris

http://www.w3.org/2001/XMLSchema#string

P2860

Evolution of a family of metazoan active-site-serine enzymes from penicillin-binding proteins: a novel facet of the bacterial legacy

Crystal Structures of Covalent Complexes of β-Lactam Antibiotics with Escherichia coli Penicillin-Binding Protein 5: Toward an Understanding of Antibiotic Specificity

Crystal Structures of Penicillin-Binding Protein 3 from Pseudomonas aeruginosa: Comparison of Native and Antibiotic-Bound Forms

The Role of the β5–α11 Loop in the Active-Site Dynamics of Acylated Penicillin-Binding Protein A from Mycobacterium tuberculosis

Crystal Structures of Bifunctional Penicillin-Binding Protein 4 from Listeria monocytogenes

Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases

Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor

Signal peptidases

Redefining penems

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration

P304

376-380

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/ACSMEDCHEMLETT.8B00064

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Floyd E Romesberg

Ramkrishna Adhikary

Chien-Hung Yeh

P577

2018-03-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29670704

http://www.w3.org/2001/XMLSchema#string

P932

5900324

http://www.w3.org/2001/XMLSchema#string