Results 31 to 40 of about 558,213 (199)

Penicillin-binding proteins of protoplast and sporoplast membranes of Streptomyces griseus strains [PDF]

open access: yes, 1988
Membrane-bound penicillin-binding proteins (PBPs) of two Streptomyces griseus strains that sporulate well in liquid and solid medium have been investigated during the course of their life-cycle.
CE Buchanan   +14 more
core   +1 more source

Allosteric p97 inhibitors can overcome resistance to ATP-competitive p97 inhibitors for potential anti-cancer therapy [PDF]

open access: yes, 2020
A major challenge of targeted cancer therapy is the selection for drug‐resistant mutations in tumor cells leading to loss of treatment effectiveness. p97/VCP is a central regulator of protein homeostasis and a promising anti‐cancer target because of its ...
Chou, Tsui-Fen   +5 more
core   +1 more source

Penicillin-binding proteins in Borrelia burgdorferi [PDF]

open access: yesJournal of Bacteriology, 1990
Penicillin-binding proteins were identified in Borrelia burgdorferi membranes. A 94-kilodalton penicillin-binding protein was the first to be labeled with tritiated penicillin and was the first band to disappear in a competition experiment. Its binding ability was destroyed when membranes were preboiled. In addition, several of these penicillin-binding
C, Urban   +4 more
openaire   +2 more sources

Impacts of Penicillin Binding Protein 2 Inactivation on β-Lactamase Expression and Muropeptide Profile in Stenotrophomonas maltophilia

open access: yesmSystems, 2017
Penicillin binding proteins (PBPs) are involved in peptidoglycan synthesis, and their inactivation is linked to β-lactamase expression in ampR–β-lactamase module–harboring Gram-negative bacteria.
Yi-Wei Huang   +6 more
doaj   +1 more source

Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins. [PDF]

open access: yes, 2013
Of the membrane proteins of known structure, we found that a remarkable 67% of the water soluble domains are structurally similar to water soluble proteins of known structure. Moreover, 41% of known water soluble protein structures share a domain with an
Bowie, James U   +3 more
core   +3 more sources

Penicillin-binding proteins in Haemophilus influenzae [PDF]

open access: yesAntimicrobial Agents and Chemotherapy, 1981
The penicillin-binding proteins (PBPs) of Haemophilus influenzae were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Eight major PBPs, ranging in molecular weights from 90,000 to 27,000, were detected. The pattern of molecular weights was different from that determined fro Escherichia coli or Pseudomonas ...
S D, Makover, R, Wright, E, Telep
openaire   +2 more sources

Thrombospondin-3 augments injury-induced cardiomyopathy by intracellular integrin inhibition and sarcolemmal instability. [PDF]

open access: yes, 2019
Thrombospondins (Thbs) are a family of five secreted matricellular glycoproteins in vertebrates that broadly affect cell-matrix interaction. While Thbs4 is known to protect striated muscle from disease by enhancing sarcolemmal stability through increased
Brody, Matthew J   +11 more
core   +6 more sources

Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]

open access: yes, 2018
Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika   +3 more
core   +1 more source

Penicillin-binding proteins in Clostridium perfringens [PDF]

open access: yesAntimicrobial Agents and Chemotherapy, 1981
The penicillin-binding proteins (PBPs) of Clostridium perfringens were studied. Six PBPs ranging in molecular weight from approximately 42,000 to 100,000 were detected in the cytoplasmic membrane. The relative affinities of the PBPs for 16 beta-lactam antibiotics were determined.
T F, Murphy, M, Barza, J T, Park
openaire   +2 more sources

Structural and Regulatory Changes in PBP4 Trigger Decreased β-Lactam Susceptibility in Enterococcus faecalis

open access: yesmBio, 2018
Enterococcus faecalis strains resistant to penicillin and ampicillin are rare and have been associated with increases in quantities of low-affinity penicillin-binding protein 4 (PBP4) or with amino acid substitutions in PBP4. We report an E.
Louis B. Rice   +8 more
doaj   +1 more source

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