Results 101 to 110 of about 16,775,741 (374)

Aβ42 promotes the aggregation of α‐synuclein splice isoforms via heterogeneous nucleation

open access: yesFEBS Letters, EarlyView.
The aggregation of amyloid‐β (Aβ) and α‐synuclein (αSyn) is associated with Alzheimer's and Parkinson's diseases. This study reveals that Aβ aggregates serve as potent nucleation sites for the aggregation of αSyn and its splice isoforms, shedding light on the intricate interplay between these two pathogenic proteins.
Alexander Röntgen   +2 more
wiley   +1 more source

Effectiveness of Problem-Based Learning and Discovery Learning Models on Learning Outcomes of Social Science Students

open access: yesTarbiyah: Jurnal Ilmiah Kependidikan
Research will be conducted to determine the description of the problem-based learning and discovery learning models to improve student learning outcomes, the differences in cognitive and affective learning outcomes between experimental and control ...
Walipah Walipah   +2 more
doaj   +1 more source

ERBIN limits epithelial cell plasticity via suppression of TGF‐β signaling

open access: yesFEBS Letters, EarlyView.
In breast and lung cancer patients, low ERBIN expression correlates with poor clinical outcomes. Here, we show that ERBIN inhibits TGF‐β‐induced epithelial‐to‐mesenchymal transition in NMuMG breast and A549 lung adenocarcinoma cell lines. ERBIN suppresses TGF‐β/SMAD signaling and reduces TGF‐β‐induced ERK phosphorylation.
Chao Li   +3 more
wiley   +1 more source

Secondary social science teacher training in Papua New Guinea and secondary social studies teacher training in New Zealand : a comparative study : a thesis presented in partial fulfilment of the requirements for the degree of Masters in Education at Massey University [PDF]

open access: yes, 1982
This thesis is presented in a form of a report on a comparative documentary survey of secondary social science teacher training in Papua New Guinea and secondary social studies teacher training in New Zealand.
André, Elisabeth, Rist, Thomas
core   +1 more source

Mechanisms and kinetic assays of aminoacyl‐tRNA synthetases

open access: yes
FEBS Letters, EarlyView.
Igor Zivkovic   +2 more
wiley   +1 more source

Thermostable neutral metalloprotease from Geobacillus sp. EA1 does not share thermolysin's preference for substrates with leucine at the P1′ position

open access: yesFEBS Letters, EarlyView.
Knowing how proteases recognise preferred substrates facilitates matching proteases to applications. The S1′ pocket of protease EA1 directs cleavage to the N‐terminal side of hydrophobic residues, particularly leucine. The S1′ pocket of thermolysin differs from EA's at only one position (leucine in place of phenylalanine), which decreases cleavage ...
Grant R. Broomfield   +3 more
wiley   +1 more source

Sociology and Methodology of Historical Research. Ethnomethodology

open access: yesRespectus Philologicus, 2016
The article is taking issues of the social science methodology (with particular reference to sociology, with ethnomethodology at the head) in the context of the historical research methodology.
Sylwia Konarska-Zimnicka
doaj   +1 more source

Redox‐dependent binding and conformational equilibria govern the fluorescence decay of NAD(P)H in living cells

open access: yesFEBS Letters, EarlyView.
In this work, we reveal how different enzyme binding configurations influence the fluorescence decay of NAD(P)H in live cells using time‐resolved anisotropy imaging and fluorescence lifetime imaging microscopy (FLIM). Mathematical modelling shows that the redox states of the NAD and NADP pools govern these configurations, shaping their fluorescence ...
Thomas S. Blacker   +8 more
wiley   +1 more source

Research and Science Today Supplement No. 2/2015 [PDF]

open access: yesResearch and Science Today, 2015
RESEARCH AND SCIENCE TODAY is a biannual science journal established in 2011. The journal is an informational platform that publishes assessment articles and the results of various scientific research carried out by academics.
Tudor Cosmin CIOCAN   +14 more
doaj  

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