Results 101 to 110 of about 564,515 (340)

CRISPR-Cas9 screens in human cells and primary neurons identify modifiers of C9ORF72 dipeptide-repeat-protein toxicity. [PDF]

open access: yes, 2018
Hexanucleotide-repeat expansions in the C9ORF72 gene are the most common cause of amyotrophic lateral sclerosis and frontotemporal dementia (c9ALS/FTD).
A Berson   +95 more
core   +1 more source

Targeted modulation of IGFL2‐AS1 reveals its translational potential in cervical adenocarcinoma

open access: yesMolecular Oncology, EarlyView.
Cervical adenocarcinoma patients face worse outcomes than squamous cell carcinoma counterparts despite similar treatment. The identification of IGFL2‐AS1's differential expression provides a molecular basis for distinguishing these histotypes, paving the way for personalized therapies and improved survival in vulnerable populations globally.
Ricardo Cesar Cintra   +6 more
wiley   +1 more source

Population structure-guided profiling of antibiotic resistance patterns in clinical Listeria monocytogenes isolates from Germany identifies pbpB3 alleles associated with low levels of cephalosporin resistance

open access: yesEmerging Microbes and Infections, 2020
Numbers of listeriosis illnesses have been increasing in Germany and the European Union during the last decade. In addition, reports on the occurrence of antibiotic resistance in Listeria monocytogenes in clinical and environmental isolates are ...
Martin A. Fischer   +5 more
doaj   +1 more source

COMP–PMEPA1 axis promotes epithelial‐to‐mesenchymal transition in breast cancer cells

open access: yesMolecular Oncology, EarlyView.
This study reveals that cartilage oligomeric matrix protein (COMP) promotes epithelial‐to‐mesenchymal transition (EMT) in breast cancer. We identify PMEPA1 (protein TMEPAI) as a novel COMP‐binding partner that mediates EMT via binding to the TSP domains of COMP, establishing the COMP–PMEPA1 axis as a key EMT driver in breast cancer.
Konstantinos S. Papadakos   +6 more
wiley   +1 more source

A Langmuir approach on monolayer interactions to investigate surface active peptides [PDF]

open access: yes, 2010
The Langmuir Blodgett apparatus provides a versatile system for studying the interfacial properties of peptides and peptide-membrane interactions under controlled conditions.
Dennison, Sarah Rachel   +2 more
core  

Identification of Treponema pallidum penicillin-binding proteins [PDF]

open access: yesJournal of Bacteriology, 1987
Penicillin-binding proteins of 180, 89, 80, 68, 61, 41, and 38 kilodaltons were identified in Treponema pallidum (Nichols) by their covalent binding of [35S]benzylpenicillin. Penicillin-binding proteins are localized in the plasma membranes of many bacterial species and may serve as useful markers for determining plasma membrane intactness in T ...
T M, Cunningham   +2 more
openaire   +2 more sources

IMPDH inhibition enhances cytarabine efficacy in SAMHD1‐expressing leukaemia cells via guanine nucleotide depletion

open access: yesMolecular Oncology, EarlyView.
Cytarabine is a key therapy for acute myeloid leukaemia (AML), but its efficacy is limited by the dNTPase SAMHD1, which hydrolyses its active metabolite. Screening nucleotide biosynthesis inhibitors revealed that IMPDH inhibitors selectively sensitise SAMHD1‐proficient AML cells to cytarabine.
Miriam Yagüe‐Capilla   +9 more
wiley   +1 more source

Francisella tularensis D-Ala D-Ala Carboxypeptidase DacD Is Involved in Intracellular Replication and It Is Necessary for Bacterial Cell Wall Integrity

open access: yesFrontiers in Cellular and Infection Microbiology, 2018
D-alanyl-D-alanine carboxypeptidase, product of dacD gene in Francisella, belongs to penicillin binding proteins (PBPs) and is involved in remodeling of newly synthetized peptidoglycan. In E.
Petra Spidlova   +8 more
doaj   +1 more source

Altering Enzymatic Activity: Recruitment of Carboxypeptidase Activity into an RTEM β-Lactamase/Penicillin-Binding Protein 5 Chimera [PDF]

open access: yes, 1990
The D-Ala-D-Ala carboxypeptidases/transpeptidases (penicillin-binding proteins, PBPs) share considerable structural homology with class A β-lactamases (EC 3.5.2.6), although these β-lactamases have no observable D-Ala-D-Ala carboxypeptidase activity ...
Chang, Yie-Hwa   +2 more
core  

Peptidoglycan recruitment by a penicillin binding protein

open access: yesNature Communications
Abstract The cell wall is essential for bacterial survival. Its core component is peptidoglycan (PG), a polymer comprised of disaccharide-peptides (stem peptides) that are cross-linked to one another via transpeptidation by penicillin-binding proteins (PBPs). While much is known about how PBPs are inactivated by β-
Yamanappa Hunashal   +11 more
openaire   +2 more sources

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