Rapid Single-Step Induction of Functional Neurons from Human Pluripotent Stem Cells
- Yingsha Zhang, ChangHui Pak, T. Südhof
- BiologyNeuron
- 5 June 2013
Exosomal PD-L1 Contributes to Immunosuppression and is Associated with anti-PD-1 Response
It is reported that metastatic melanomas release extracellular vesicles, mostly in the form of exosomes, that carry PD-L1 on their surface, suggesting a mechanism by which tumours could evade the immunesystem, and the potential application ofExosomal PD- L1 to monitor patient responses to checkpoint therapies.
aph-1 and pen-2 Are Required for Notch Pathway Signaling, γ-Secretase Cleavage of βAPP, and Presenilin Protein Accumulation
- R. Francis, G. Mcgrath, D. Curtis
- Biology
- 1 July 2002
Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors.
- Mengtao Xiao, Hui Yang, K. Guan
- Biology, ChemistryGenes & Development
- 15 June 2012
This study suggests that tumor-derived FH and SDH mutations accumulate fumarate and succinate, leading to enzymatic inhibition of multiple α-KG-dependent dioxygenases and consequent alterations of genome-wide histone and DNA methylation.
A Neural Circuit for Memory Specificity and Generalization
It is proposed that the nucleus reuniens (NR), a thalamic nucleus of largely unknown function, determines the specificity and generalization of memory attributes for a particular context by processing information from the medial prefrontal cortex en route to the hippocampus.
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
- S. Demarest, M. Martinez-Yamout, P. Wright
- BiologyNature
- 31 January 2002
This study uncovers a unique mechanism, called ‘synergistic folding’, through which p160 coactivators recruit CBP/p300 to allow transmission of the hormonal signal to the transcriptional machinery.
Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
It is shown that Uch37 is responsible for the ubiquitin isopeptidase activity in the PA700 (19S) proteasome regulatory complex, which facilitates processing of polyubiquitin chains.
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
- Y. Lam, Wei Xu, G. Demartino, R. Cohen
- BiologyNature
- 20 February 1997
A bovine isopeptidase is described that is well suited to such an editing function because of its unique localization and specificity and can selectively rescue poorly ubiquitinated or slowly degraded Ub-protein conjugates from proteolysis.
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