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1. Measurement of Neuropeptide Y Using Aptamer-Modified Microelectrodes by Electrochemical Impedance Spectroscopy

   https://doi.org/10.1021/acs.analchem.0c03719  

   López, Luis ; Hernández, Nerika ; Reyes Morales, Joshua ; Cruz, John ; Flores, Krystal ; González-Amoretti, John ; Rivera, Vitmary ; Cunci, Lisandro ( January 2021 , Analytical Chemistry)

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2. In Silico Discovery and Validation of Neuropeptide-Y-Binding Peptides for Sensors

   https://doi.org/10.1021/acs.jpcb.9b09439  

   Xiao, Xingqing ; Kuang, Zhifeng ; Burke, B. J. ; Chushak, Yaroslav ; Farmer, Barry L. ; Mirau, Peter A. ; Naik, Rajesh R. ; Hall, Carol K. ( December 2019 , The Journal of Physical Chemistry B)
3. Hedonic eating, obesity, and addiction result from increased neuropeptide Y in the nucleus accumbens during human brain evolution

   https://doi.org/10.1073/pnas.2311118120  

   Raghanti, Mary Ann ; Miller, Elaine N. ; Jones, Danielle N. ; Smith, Heather N. ; Munger, Emily L. ; Edler, Melissa K. ; Phillips, Kimberley A. ; Hopkins, William D. ; Hof, Patrick R. ; Sherwood, Chet C. ; et al ( September 2023 , Proceedings of the National Academy of Sciences)

   The nucleus accumbens (NAc) is central to motivation and action, exhibiting one of the highest densities of neuropeptide Y (NPY) in the brain. Within the NAc, NPY plays a role in reward and is involved in emotional behavior and in increasing alcohol and drug addiction and fat intake. Here, we examined NPY innervation and neurons of the NAc in humans and other anthropoid primates in order to determine whether there are differences among these various species that would correspond to behavioral or life history variables. We quantified NPY-immunoreactive axons and neurons in the NAc of 13 primate species, including humans, great apes, and monkeys. Our data show that the human brain is unique among primates in having denser NPY innervation within the NAc, as measured by axon length density to neuron density, even after accounting for brain size. Combined with our previous finding of increased dopaminergic innervation in the same region, our results suggest that the neurochemical profile of the human NAc appears to have rendered our species uniquely susceptible to neurophysiological conditions such as addiction. The increase in NPY specific to the NAc may represent an adaptation that favors fat intake and contributes to an increased vulnerability to eating disorders, obesity, as well as alcohol and drug dependence. Along with our findings for dopamine, these deeply rooted structural attributes of the human brain are likely to have emerged early in the human clade, laying the groundwork for later brain expansion and the development of cognitive and behavioral specializations.

    

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4. Toward Subcutaneous Electrochemical Aptasensors for Neuropeptide Y

   https://doi.org/10.1109/SENSORS47087.2021.9639832  

   Richardson, Hayley ; Maddocks, Grace ; Peterson, Kaila ; Daniele, Michael ; Pavlidis, Spyridon ( January 2021 , 2021 IEEE Sensors)
5. Structural basis of neuropeptide Y signaling through Y1 receptor

   https://doi.org/10.1038/s41467-022-28510-6  

   Park, Chaehee ; Kim, Jinuk ; Ko, Seung-Bum ; Choi, Yeol Kyo ; Jeong, Hyeongseop ; Woo, Hyeonuk ; Kang, Hyunook ; Bang, Injin ; Kim, Sang Ah ; Yoon, Tae-Young ; et al ( February 2022 , Nature Communications)

   Neuropeptide Y (NPY) is highly abundant in the brain and involved in various physiological processes related to food intake and anxiety, as well as human diseases such as obesity and cancer. However, the molecular details of the interactions between NPY and its receptors are poorly understood. Here, we report a cryo-electron microscopy structure of the NPY-bound neuropeptide Y1 receptor (Y₁R) in complex with G_i1protein. The NPY C-terminal segment forming the extended conformation binds deep into the Y₁R transmembrane core, where the amidated C-terminal residue Y36 of NPY is located at the base of the ligand-binding pocket. Furthermore, the helical region and two N-terminal residues of NPY interact with Y₁R extracellular loops, contributing to the high affinity of NPY for Y₁R. The structural analysis of NPY-bound Y₁R and mutagenesis studies provide molecular insights into the activation mechanism of Y₁R upon NPY binding.

    

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