Ligand‐stereoselective allosteric activation of cold‐sensing TRPM8 channels by an H‐bonded homochiral menthol dimer with head‐to‐head or head‐to‐tail

Chirality ◽  
2021 ◽  
Author(s):  
Guangyu Wang
Keyword(s):  
Allosteric Activation ◽  
Cold Sensing

Chinese Scientists Made Breakthrough Progresses in Studies on Cold Sensing and Signaling in Plants

2015 ◽  
Vol 50 (2) ◽  
pp. 145
Author(s):  
Zuo Jianru ◽  
Chen Fan
Keyword(s):  
Cold Sensing

Dynamical Basis of Allosteric Activation for the Plasmodium falciparum Protein Kinase G

2021 ◽  
Author(s):  
Jinfeng Huang ◽  
Jung Ah Byun ◽  
Bryan VanSchouwen ◽  
Philipp Henning ◽  
Friedrich W. Herberg ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Kinase ◽  
Protein Kinase G ◽  
Allosteric Activation ◽  
Falciparum Protein

scholarly journals Odontoblast TRPC5 channels signal cold pain in teeth

2021 ◽  
Vol 7 (13) ◽  
pp. eabf5567
Author(s):  
Laura Bernal ◽  
Pamela Sotelo-Hitschfeld ◽  
Christine König ◽  
Viktor Sinica ◽  
Amanda Wyatt ◽  
...  
Keyword(s):  
Relative Sensitivity ◽  
Cellular Component ◽  
Sensory Transduction ◽  
Cold Sensation ◽  
Cold Pain ◽  
Sensing System ◽  
Cold Sensitive ◽  
Cellular Components ◽  
Cold Sensor ◽  
Cold Sensing

Teeth are composed of many tissues, covered by an inflexible and obdurate enamel. Unlike most other tissues, teeth become extremely cold sensitive when inflamed. The mechanisms of this cold sensation are not understood. Here, we clarify the molecular and cellular components of the dental cold sensing system and show that sensory transduction of cold stimuli in teeth requires odontoblasts. TRPC5 is a cold sensor in healthy teeth and, with TRPA1, is sufficient for cold sensing. The odontoblast appears as the direct site of TRPC5 cold transduction and provides a mechanism for prolonged cold sensing via TRPC5’s relative sensitivity to intracellular calcium and lack of desensitization. Our data provide concrete functional evidence that equipping odontoblasts with the cold-sensor TRPC5 expands traditional odontoblast functions and renders it a previously unknown integral cellular component of the dental cold sensing system.

scholarly journals Exploring the “minimal” structure of a functional ADAMTS13 by mutagenesis and small-angle X-ray scattering

Blood ◽  
2019 ◽  
Vol 133 (17) ◽  
pp. 1909-1918 ◽  
Author(s):  
Jian Zhu ◽  
Joshua Muia ◽  
Garima Gupta ◽  
Lisa A. Westfield ◽  
Karen Vanhoorelbeke ◽  
...  
Keyword(s):  
Small Angle ◽  
Columba Livia ◽  
Allosteric Activation ◽  
Complement Components ◽  
X Ray ◽  
X Ray Scattering ◽  
Morphogenetic Protein ◽  
Minimal Structure ◽  
Von Willebrand ◽  
Ray Scattering

Abstract Human ADAMTS13 is a multidomain protein with metalloprotease (M), disintegrin-like (D), thrombospondin-1 (T), Cys-rich (C), and spacer (S) domains, followed by 7 additional T domains and 2 CUB (complement components C1r and C1s, sea urchin protein Uegf, and bone morphogenetic protein-1) domains. ADAMTS13 inhibits the growth of von Willebrand factor (VWF)–platelet aggregates by cleaving the cryptic Tyr1605-Met1606 bond in the VWF A2 domain. ADAMTS13 is regulated by substrate-induced allosteric activation; without shear stress, the distal T8-CUB domains markedly inhibit VWF cleavage, and binding of VWF domain D4 or selected monoclonal antibodies (MAbs) to distal ADAMTS13 domains relieves this autoinhibition. By small angle X-ray scattering (SAXS), ADAMTS13 adopts a hairpin-like conformation with distal T7-CUB domains close to the proximal MDTCS domains and a hinge point between T4 and T5. The hairpin projects like a handle away from the core MDTCS and T7-CUB complex and contains distal T domains that are dispensable for allosteric regulation. Truncated constructs that lack the T8-CUB domains are not autoinhibited and cannot be activated by VWF D4 but retain the hairpin fold. Allosteric activation by VWF D4 requires T7, T8, and the 58–amino acid residue linker between T8 and CUB1. Deletion of T3 to T6 produced the smallest construct (delT3-6) examined that could be activated by MAbs and VWF D4. Columba livia (pigeon) ADAMTS13 (pADAMTS13) resembles human delT3-6, retains normal activation by VWF D4, and has a SAXS envelope consistent with amputation of the hairpin containing the dispensable T domains of human ADAMTS13. Our findings suggest that human delT3-6 and pADAMTS13 approach a “minimal” structure for allosterically regulated ADAMTS13.

Allosteric Activation off Brain Mitochondrial Ca2+Uptake by Spermine and by Ca2+: Developmental Changes

1989 ◽  
Vol 53 (4) ◽  
pp. 1173-1181 ◽  
Author(s):  
John R. Jensen ◽  
Gary Lynch ◽  
Michel Baudry
Keyword(s):  
Developmental Changes ◽  
Allosteric Activation

scholarly journals Allosteric Activation of a Bacterial Stress Sensor

Cell ◽  
2007 ◽  
Vol 131 (3) ◽  
pp. 441-443 ◽  
Author(s):  
Nieng Yan ◽  
Yigong Shi
Keyword(s):  
Allosteric Activation ◽  
Stress Sensor
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