Functional and structural characterization of parathyroid hormone receptors in health and disease

1989 ◽  
Author(s):  
Kin-kee Pun
Keyword(s):  
Parathyroid Hormone ◽  
Structural Characterization ◽  
Hormone Receptors ◽  
Health And Disease

Expression and characterization of parathyroid hormone receptors on fetal rat calvaria cells in culture

1994 ◽  
Vol 12 (S1) ◽  
pp. S33-S37 ◽  
Author(s):  
Noriyuki Yamauchi ◽  
Keiji Ohishi ◽  
Seiji Nishikawa ◽  
Toshihiko Nagata ◽  
Masatoshi Kataoka ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Receptors ◽  
Cells In Culture ◽  
Rat Calvaria ◽  
Fetal Rat

Synthesis of fully active biotinylated analogs of parathyroid hormone and parathyroid hormone-related protein as tools for the characterization of parathyroid hormone receptors

Biochemistry ◽  
1992 ◽  
Vol 31 (16) ◽  
pp. 4026-4033 ◽  
Author(s):  
Eliahu Roubini ◽  
Le T. Duong ◽  
Susan W. Gibbons ◽  
Chih T. Leu ◽  
Michael P. Caulfield ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Receptors ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

Structural characterization of amyloid fibrils from the human parathyroid hormone

2015 ◽  
Vol 1854 (4) ◽  
pp. 249-257 ◽  
Author(s):  
Mohanraj Gopalswamy ◽  
Amit Kumar ◽  
Juliane Adler ◽  
Monika Baumann ◽  
Mathias Henze ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Structural Characterization ◽  
Amyloid Fibrils ◽  
Human Parathyroid Hormone

scholarly journals Structural Characterization of Human Parathyroid Hormone 1 Receptor

2012 ◽  
Vol 28 (07) ◽  
pp. 1783-1789 ◽  
Author(s):  
LIN Ke-Jiang ◽  
◽  
ZHU Dong-Ji ◽  
LENG Yong-Gan ◽  
YOU Qi-Dong
Keyword(s):  
Parathyroid Hormone ◽  
Structural Characterization ◽  
Human Parathyroid Hormone ◽  
Parathyroid Hormone 1 Receptor

Molecular, chemical, and structural characterization of prostaglandin A2 as a novel agonist for Nur77

2019 ◽  
Vol 476 (19) ◽  
pp. 2757-2767 ◽  
Author(s):  
Sowmya P. Lakshmi ◽  
Aravind T. Reddy ◽  
Asoka Banno ◽  
Raju C. Reddy
Keyword(s):  
Structural Characterization ◽  
Hormone Receptors ◽  
Target Genes ◽  
Unsaturated Fatty Acids ◽  
Biological Effects ◽  
Chemical Properties ◽  
Orphan Receptor ◽  
Dynamic Simulations ◽  
Prostaglandin A2

Abstract Nur77 is a transcription factor belonging to the NR4A subfamily of nuclear hormone receptors. Upon induction, Nur77 modulates the expression of its target genes and controls a variety of biological and pathophysiological processes. Prior research that revealed a structurally atypical ligand-binding domain (LBD) and failed to locate an endogenous ligand had led to a classification of Nur77 as an orphan receptor. However, several more recent studies indicate that small synthetic molecules and unsaturated fatty acids can bind to Nur77. Discovery of additional endogenous ligands will facilitate our understanding of the receptor's functions and regulatory mechanisms. Our data have identified prostaglandin A2 (PGA2), a cyclopentenone prostaglandin (PG), as such a ligand. Cyclopentenone PGs exert their biological effects primarily by forming protein adducts via the characteristic electrophilic β-carbon(s) located in their cyclopentenone rings. Our data show that PGA2 induces Nur77 transcriptional activity by forming a covalent adduct between its endocyclic β-carbon, C9, and Cys566 in the receptor's LBD. The importance of this endocyclic β-carbon was substantiated by the failure of PGs without such electrophilic properties to react with Nur77. Calculated chemical properties and data from reactive molecular dynamic simulations, intrinsic reaction co-ordinate modeling, and covalent molecular docking also corroborate the selectivity of PGA2's C9 β-carbon towards Nur77's Cys. In summary, our molecular, chemical, and structural characterization of the PGA2–Nur77 interaction provides the first evidence that PGA2 is an endogenous Nur77 agonist.

Identification and characterization of parathyroid hormone receptors in rat renal cortical plasma membranes using radioligand binding

2009 ◽  
Vol 4 (4) ◽  
pp. 615-623 ◽  
Author(s):  
G. Allen Nickols ◽  
Maureen A. Metz-Nickols ◽  
M. Scot Roberts ◽  
Cary W. Cooper ◽  
Peter K.T. Pang
Keyword(s):  
Parathyroid Hormone ◽  
Plasma Membranes ◽  
Hormone Receptors ◽  
Radioligand Binding ◽  
Identification And Characterization

New ultrastructural findings about Borrelia burgdorferi by cryofixation, negative staining, thin sectioning and scanning techniques

1990 ◽  
Vol 48 (3) ◽  
pp. 582-583
Author(s):  
S. F. Hayes ◽  
M. D. Corwin ◽  
T. G. Schwan ◽  
D. W. Dorward ◽  
W. Burgdorfer
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Structural Characterization ◽  
Negative Staining ◽  
Low Speed ◽  
Thin Sectioning ◽  
Ultrastructural Findings

Characterization of Borrelia burgdorferi strains by means of negative staining EM has become an integral part of many studies related to the biology of the Lyme disease organism. However, relying solely upon negative staining to compare new isolates with prototype B31 or other borreliae is often unsatisfactory. To obtain more satisfactory results, we have relied upon a correlative approach encompassing a variety EM techniques, i.e., scanning for topographical features and cryotomy, negative staining and thin sectioning to provide a more complete structural characterization of B. burgdorferi.For characterization, isolates of B. burgdorferi were cultured in BSK II media from which they were removed by low speed centrifugation. The sedimented borrelia were carefully resuspended in stabilizing buffer so as to preserve their features for scanning and negative staining. Alternatively, others were prepared for conventional thin sectioning and for cryotomy using modified procedures. For thin sectioning, the fixative described by Ito, et al.

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