Structural insights into protein regulation by phosphorylation and substrate recognition of protein kinases/phosphatases

SH Seok - Life, 2021 - mdpi.com
Protein phosphorylation is one of the most widely observed and important post-translational
modification (PTM) processes. Protein phosphorylation is regulated by protein kinases, each …

Allosteric regulation of phenylalanine hydroxylase

PF Fitzpatrick - Archives of biochemistry and biophysics, 2012 - Elsevier
The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess
phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by …

First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer

EC Arturo, K Gupta, A Héroux, L Stith… - Proceedings of the …, 2016 - National Acad Sciences
Improved understanding of the relationship among structure, dynamics, and function for the
enzyme phenylalanine hydroxylase (PAH) can lead to needed new therapies for …

10-20 Joules as a neuromolecular quantum in medicinal chemistry: an alternative approach to myriad molecular pathways?

MA Persinger - Current Medicinal Chemistry, 2010 - ingentaconnect.com
The myriads of molecular pathways that have been measured to understand the physical
bases of neuronal and other cellular functions have exceeded classical comprehension. In …

Molecular dynamics simulations to decipher the role of phosphorylation of SARS-CoV-2 nonstructural proteins (nsps) in viral replication

L Alomair, S Mustafa, MS Jafri, W Alharbi, A Aljouie… - Viruses, 2022 - mdpi.com
Protein phosphorylation is a post-translational modification that enables various cellular
activities and plays essential roles in protein interactions. Phosphorylation is an important …

Random coil chemical shifts for serine, threonine and tyrosine phosphorylation over a broad pH range

R Hendus-Altenburger, CB Fernandes, K Bugge… - Journal of biomolecular …, 2019 - Springer
Phosphorylation is one of the main regulators of cellular signaling typically occurring in
flexible parts of folded proteins and in intrinsically disordered regions. It can have distinct …

[HTML][HTML] A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins–Lessons from the sodium proton exchanger 1 (NHE1)

R Hendus-Altenburger, M Lambrughi, T Terkelsen… - Cellular …, 2017 - Elsevier
Intrinsically disordered proteins (IDPs) are involved in many pivotal cellular processes
including phosphorylation and signalling. The structural and functional effects of …

Discovery of novel cyclic salt bridge in thermophilic bacterial protease and study of its sequence and structure

D Mitra, PK Das Mohapatra - Applied Biochemistry and Biotechnology, 2021 - Springer
The plausible explanation behind the stability of thermophilic protein is still yet to be defined
more clearly. Here, an in silico study has been undertaken by investigating the sequence …

Protein kinase‐A affects sorting and conformation of the sodium‐dependent glucose co‐transporter SGLT1

S Subramanian, P Glitz, H Kipp… - Journal of cellular …, 2009 - Wiley Online Library
In Chinese hamster ovary cells expressing rabbit sodium‐dependent glucose transporter
(rbSGLT1) protein kinase A (PKA) activators (forskolin and 8‐Br‐cAMP) stimulated α‐methyl …

Rescuing proteins of low kinetic stability by chaperones and natural ligands: phenylketonuria, a case study

A Martinez, AC Calvo, K Teigen, AL Pey - Progress in Molecular Biology …, 2008 - Elsevier
Publisher Summary Phenylketonuria (PKU) is a disease caused by deleterious mutations in
phenylalanine hydroxylase (PAH) and constitutes a paradigm for misfolding diseases …