Results 51 to 60 of about 68,403 (252)

Allosteric regulation of phenylalanine hydroxylase [PDF]

Archives of Biochemistry and Biophysics, 2012
The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin.
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Allosteric Regulation of E-Cadherin Adhesion [PDF]

Journal of Biological Chemistry, 2015
Cadherins are transmembrane adhesion proteins that maintain intercellular cohesion in all tissues, and their rapid regulation is essential for organized tissue remodeling. Despite some evidence that cadherin adhesion might be allosterically regulated, testing of this has been hindered by the difficulty of quantifying altered E-cadherin binding affinity
Nitesh, Shashikanth, Yuliya I, Petrova, Seongjin, Park, Jillian, Chekan, Stephanie, Maiden, Martha, Spano, Taekjip, Ha, Barry M, Gumbiner, Deborah E, Leckband   +8 more
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The energy landscape analysis of cancer mutations in protein kinases. [PDF]

PLoS ONE, 2011
The growing interest in quantifying the molecular basis of protein kinase activation and allosteric regulation by cancer mutations has fueled computational studies of allosteric signaling in protein kinases.
Anshuman Dixit, Gennady M Verkhivker
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Hairpin and allosteric regulation in ADAMTS13 [PDF]

Blood, 2019
In this issue of Blood , Muia et al 1 and Zhu et al, 2 using complementary approaches, provide important insights into the structure and function of ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin-1 repeats, member 13), identifying critical structural features and interactions that allosterically regulate its proteolytic activity ...
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Insights into Conformational Dynamics and Allostery in DNMT1-H3Ub/USP7 Interactions

Molecules, 2021
DNA methyltransferases (DNMTs) including DNMT1 are a conserved family of cytosine methylases that play crucial roles in epigenetic regulation. The versatile functions of DNMT1 rely on allosteric networks between its different interacting partners ...
Yu Zhu, Fei Ye, Ziyun Zhou, Wanlin Liu, Zhongjie Liang, Guang Hu   +5 more
doaj   +1 more source

Identification of Alternative Allosteric Sites in Glycolytic Enzymes for Potential Use as Species-Specific Drug Targets

Frontiers in Molecular Biosciences, 2020
Three allosteric glycolytic enzymes, phosphofructokinase, glyceraldehyde-3 phosphate dehydrogenase and pyruvate kinase, associated with bacterial, parasitic and human species, were explored to identify potential allosteric sites that would be used as ...
Merve Ayyildiz, Serkan Celiker, Fatih Ozhelvaci, E. Demet Akten   +3 more
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Integrative residue-intuitive machine learning and MD Approach to Unveil Allosteric Site and Mechanism for β2AR

Nature Communications
Allosteric drugs offer a new avenue for modern drug design. However, the identification of cryptic allosteric sites presents a formidable challenge. Following the allostery nature of residue-driven conformation transition, we propose a state-of-the-art ...
Xin Chen, Kexin Wang, Jianfang Chen, Chao Wu, Jun Mao, Yuanpeng Song, Yijing Liu, Zhenhua Shao, Xuemei Pu   +8 more
doaj   +1 more source

FimH as a scaffold for regulated molecular recognition

Journal of Biological Engineering, 2021
Background Recognition proteins are critical in many biotechnology applications and would be even more useful if their binding could be regulated. The current gold standard for recognition molecules, antibodies, lacks convenient regulation.
Shivani Gupta Ludwig, Casey L. Kiyohara, Laura A. Carlucci, Dagmara Kisiela, Evgeni V. Sokurenko, Wendy Evelyn Thomas   +5 more
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The structural basis of allosteric regulation in proteins [PDF]

FEBS Letters, 2009
Allosteric regulation of protein function occurs when the regulatory trigger, such as the binding of a small‐molecule effector or inhibitor, takes place some distance from the protein's, or protein complex's, active site. This distance can be a few Å, or tens of Å.
Laskowski, Roman A., Gerick, Fabian, Thornton, Janet M.   +2 more
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Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

FEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura, Shin‐ichi Tate, Kyota Yasuda   +2 more
wiley   +1 more source