Literature DB >> 12865401

Ubiquitinated deiodinase: not dead yet.

Ronald J Koenig1.   

Abstract

Originating in the thyroid, the prohormone thyroxine is converted to triiodothyronine, which is essential in brain development, growth, and metabolism. A study in this issue reveals a novel mechanism for controlling triiodothyronine production that provides the first example of enzyme activity being restored by deubiquitination.

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Year:  2003        PMID： 12865401      PMCID： PMC164296          DOI： 10.1172/JCI19157

Source DB:  PubMed          Journal:  J Clin Invest        ISSN： 0021-9738            Impact factor:   14.808


  16 in total

1.  Selective proteolysis of human type 2 deiodinase: a novel ubiquitin-proteasomal mediated mechanism for regulation of hormone activation.

Authors:  B Gereben; C Goncalves; J W Harney; P R Larsen; A C Bianco
Journal:  Mol Endocrinol       Date:  2000-11

Review 2.  Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases.

Authors:  Antonio C Bianco; Domenico Salvatore; Balázs Gereben; Marla J Berry; P Reed Larsen
Journal:  Endocr Rev       Date:  2002-02       Impact factor: 19.871

3.  An analysis of the sources and quantity of 3,5,3'-triiodothyronine specifically bound to nuclear receptors in rat cerebral cortex and cerebellum.

Authors:  F R Crantz; J E Silva; P R Larsen
Journal:  Endocrinology       Date:  1982-02       Impact factor: 4.736

4.  Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein.

Authors:  Zaibo Li; Xi Na; Dakun Wang; Susan R Schoen; Edward M Messing; Guan Wu
Journal:  J Biol Chem       Date:  2001-12-05       Impact factor: 5.157

Review 5.  The von Hippel-Lindau tumour suppressor protein: new perspectives.

Authors:  M Ohh; W G Kaelin
Journal:  Mol Med Today       Date:  1999-06

6.  The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase.

Authors:  T Ravid; R Doolman; R Avner; D Harats; J Roitelman
Journal:  J Biol Chem       Date:  2000-11-17       Impact factor: 5.157

7.  Distinct subcellular localization of transiently expressed types 1 and 2 iodothyronine deiodinases as determined by immunofluorescence confocal microscopy.

Authors:  M M Baqui; B Gereben; J W Harney; P R Larsen; A C Bianco
Journal:  Endocrinology       Date:  2000-11       Impact factor: 4.736

8.  Intracellular conversion of thyroxine to triiodothyronine is required for the optimal thermogenic function of brown adipose tissue.

Authors:  A C Bianco; J E Silva
Journal:  J Clin Invest       Date:  1987-01       Impact factor: 14.808

9.  Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation.

Authors:  Cyntia Curcio-Morelli; Ann Marie Zavacki; Marcelo Christofollete; Balazs Gereben; Beatriz C G de Freitas; John W Harney; Zaibo Li; Guan Wu; Antonio C Bianco
Journal:  J Clin Invest       Date:  2003-07       Impact factor: 14.808

10.  Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor.

Authors:  Zaibo Li; Dakun Wang; Xi Na; Susan R Schoen; Edward M Messing; Guan Wu
Journal:  Biochem Biophys Res Commun       Date:  2002-06-14       Impact factor: 3.575
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  1 in total

1.  Increased sensitivity of thyroid hormone-mediated signaling despite prolonged fasting.

Authors:  Bridget Martinez; Michael Scheibner; José G Soñanez-Organis; John T Jaques; Daniel E Crocker; Rudy M Ortiz
Journal:  Gen Comp Endocrinol       Date:  2017-07-22       Impact factor: 2.822
  1 in total

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