The ENT family of eukaryote nucleoside and nucleobase transporters: recent advances in the investigation of structure/function relationships and the identification of novel isoforms

2001 ◽  
Vol 18 (1) ◽  
pp. 53-63 ◽  
Author(s):  
Ralph J. Hyde ◽  
Carol E. Cass ◽  
James D. Young ◽  
James D. Stephen A. Baldwin
2011 ◽  
Vol 39 (3) ◽  
pp. 703-706 ◽  
Author(s):  
J. Malcolm East ◽  
Francesco Michelangeli

This Biochemical Society Annual Symposium on Recent Advances in Membrane Biochemistry was organized to bring together experts from across the spectrum of biomembrane disciplines from the biological to the biophysical/structural, with the intention of promoting interactions and collaborations across the field. We were keen that the potential for improving human health that stems from a deeper understanding of membrane structure/function should be acknowledged, especially in the light of the increasing numbers of membrane protein structures that continue to be made available to the biomembrane community. This foreword provides an idea of what was communicated in the various sessions and, we hope, gives an impression of the excitement generated by the speakers and delegates at this over-subscribed Symposium.


2018 ◽  
Vol 234 (6) ◽  
pp. 7856-7873 ◽  
Author(s):  
Qiushuang Ji ◽  
Shuai Guo ◽  
Xuzhao Wang ◽  
Chunli Pang ◽  
Yong Zhan ◽  
...  

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 525 ◽  
Author(s):  
Vladimir N. Uversky

Despite attracting the close attention of multiple researchers for the past 25 years, α-synuclein continues to be an enigma, hiding sacred truth related to its structure, function, and dysfunction, concealing mechanisms of its pathological spread within the affected brain during disease progression, and, above all, covering up the molecular mechanisms of its multipathogenicity, i.e. the ability to be associated with the pathogenesis of various diseases. The goal of this article is to present the most recent advances in understanding of this protein and its aggregation and to show that the remarkable structural, functional, and dysfunctional multifaceted nature of α-synuclein can be understood using the proteoform concept.


2018 ◽  
Vol 47 (1) ◽  
pp. 433-440 ◽  
Author(s):  
Cristina Cecchetti ◽  
Euan Pyle ◽  
Bernadette Byrne

Abstract Oligomerisation is a key feature of integral membrane transporters with roles in structure, function and stability. In this review, we cover some very recent advances in our understanding of how oligomerisation affects these key transporter features, with emphasis on a few groups of transporters, including the nucleobase ascorbate transporters, neurotransmitter sodium symporters and major facilitator superfamily members.


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