N-glycosylation in isolated rat nerve terminals

Molecular Omics ◽

10.1039/d0mo00044b ◽

2021 ◽

Author(s):

Inga Matthies ◽

Jodie Louise Abrahams ◽

Pia Jensen ◽

Tiago Oliveira ◽

Daniel Kolarich ◽

...

Keyword(s):

Protein Structure ◽

Structure Function ◽

Protein Modification ◽

Nerve Terminals ◽

The Brain ◽

Rat Nerve ◽

Isolated Rat

N-linked glycosylation is a ubiquitous protein modification that is capable of modulating protein structure, function and interactions. Many proteins in the brain associated with the synapse and important for synaptic...

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Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure–Function

Methods in Enzymology - Energetics of Biological Macromolecules, Part D ◽

10.1016/s0076-6879(04)79011-4 ◽

2004 ◽

pp. 188-209 ◽

Cited By ~ 8

Author(s):

Liskin Swint-Kruse ◽

Kathleen S Matthews

Keyword(s):

Molecular Dynamics ◽

Protein Structure ◽

Structure Function ◽

Protein Modification ◽

Repressor Protein ◽

Lactose Repressor

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Platelets as potential peripheral markers to study functioning of the high-affinity sodium-dependent glutamate transporters in the nerve terminals of the brain

Kosmìčna nauka ì tehnologìâ ◽

10.15407/knit2007.02.080 ◽

2007 ◽

Vol 13 (2) ◽

pp. 80-85

Author(s):

T.A. Borisova ◽

◽

L.A. Kasatkina ◽

Keyword(s):

Glutamate Transporters ◽

Nerve Terminals ◽

High Affinity ◽

Sodium Dependent ◽

The Brain ◽

Peripheral Markers

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Clusters in ?/? barrel proteins: Implications for protein structure, function, and folding: A graph theoretical approach

Proteins Structure Function and Bioinformatics ◽

10.1002/1097-0134(20010501)43:2<103::aid-prot1022>3.0.co;2-x ◽

2001 ◽

Vol 43 (2) ◽

pp. 103-112 ◽

Cited By ~ 24

Author(s):

N. Kannan ◽

S. Selvaraj ◽

M. Michael Gromiha ◽

S. Vishveshwara

Keyword(s):

Protein Structure ◽

Structure Function ◽

Theoretical Approach ◽

Graph Theoretical Approach

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Intranasal insulin improves the structure–function of the brain mitochondrial ATP–sensitive Ca2+ activated potassium channel and respiratory chain activities under diabetic conditions

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease ◽

10.1016/j.bbadis.2021.166075 ◽

2021 ◽

Vol 1867 (4) ◽

pp. 166075

Author(s):

Nihad Torabi ◽

Elham Noursadeghi ◽

Farzad Shayanfar ◽

Maryam Nazari ◽

Javad Fahanik-babaei ◽

...

Keyword(s):

Potassium Channel ◽

Structure Function ◽

Respiratory Chain ◽

Intranasal Insulin ◽

The Brain

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Lanthanide-Protein Interactions and their Use in Determination of Protein Structure, Function, and Dynamics

Analytical Chemistry Letters ◽

10.1080/22297928.2021.1890638 ◽

2021 ◽

Vol 11 (3) ◽

pp. 315-342

Author(s):

Harsha E. Rajapakse ◽

Marni Goldstein

Keyword(s):

Protein Structure ◽

Structure Function ◽

Protein Interactions

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BECLIN1: Protein Structure, Function and Regulation

Cells ◽

10.3390/cells10061522 ◽

2021 ◽

Vol 10 (6) ◽

pp. 1522

Author(s):

Sharon Tran ◽

W. Douglas Fairlie ◽

Erinna F. Lee

Keyword(s):

Protein Structure ◽

Structure Function ◽

Membrane Trafficking ◽

Biochemical Properties ◽

Class Iii ◽

Form Class ◽

Protein Interactome ◽

Protein Functions ◽

Phosphoinositide 3 Kinase ◽

Shed Light

BECLIN1 is a well-established regulator of autophagy, a process essential for mammalian survival. It functions in conjunction with other proteins to form Class III Phosphoinositide 3-Kinase (PI3K) complexes to generate phosphorylated phosphatidylinositol (PtdIns), lipids essential for not only autophagy but other membrane trafficking processes. Over the years, studies have elucidated the structural, biophysical, and biochemical properties of BECLIN1, which have shed light on how this protein functions to allosterically regulate these critical processes of autophagy and membrane trafficking. Here, we review these findings and how BECLIN1’s diverse protein interactome regulates it, as well as its impact on organismal physiology.

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