About: Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation

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About: Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 1996

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1996 (uk) article scientifique publié en 1996 (fr) im Oktober 1996 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 1996 (ast) scientific article published on 01 October 1996 (en)
publication date	wds:Q71776975-BD366072-6F23-4CBC-A9F6-CE9450A17E61
publication date	1996-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71776975-D91045B5-C9E8-40A0-8771-EFAB0FAFB881
language of work or name	English
cites work	wds:Q71776975-01CE8420-DA39-4BFC-A017-787764D0A8BF wds:Q71776975-04F65C3A-6AC1-43DB-99E3-538105B68801 wds:Q71776975-07C1A8A9-9BF1-4A17-84A8-70DAF4EF9313 wds:Q71776975-0A2385CE-FBAD-468F-A86C-67E45D8AE054 wds:Q71776975-0DF51C91-5065-4E81-8BF3-71117079AE4D wds:Q71776975-17112DDF-A22A-453B-BF2E-9DF9453F6BFB wds:Q71776975-1B9FB3DF-ECED-4278-9D82-452E6E8FEB5D wds:Q71776975-31575448-5519-4E5E-A842-75558FB70D81 wds:Q71776975-3F2AD647-EE4A-4151-8007-98B747EA641B wds:Q71776975-4D90F034-2B6F-40B2-B2B5-38584FADBB7A wds:Q71776975-4E15ED67-40F0-4607-88BD-9B562CCC1EBA wds:Q71776975-5707A8AE-0B4B-40A9-9EA0-C0A28EBD56C5 wds:Q71776975-581E53E1-3B1B-4C0D-961A-697D3C659A79 wds:Q71776975-5B229EA6-DB28-4E8B-A2CF-8D5856E3EBB7 wds:Q71776975-6F5890D0-1E90-4927-A2A0-A8A405F874B6 wds:Q71776975-93F48ED3-FCA8-498D-9461-891C5233B4FC wds:Q71776975-9F7005EB-82ED-4572-8534-186255D4BA20 wds:Q71776975-A979801B-C44C-405F-A521-B1E4B2C3E752 wds:Q71776975-ABB1DDF5-DE96-468C-B609-692B698FC10E wds:Q71776975-B191DC3A-6297-49E3-AEEC-32E130B53FC0 wds:Q71776975-B1C0DA23-8646-45A0-92F0-222FD73A801E wds:Q71776975-B802DB8C-CD4D-4792-9CBF-A28848CD2277 wds:Q71776975-D488850B-4253-49A5-9CF1-53E987245C41 wds:Q71776975-DD6ADCFF-AA69-444F-9311-A097D7775EAA wds:Q71776975-DDC6A5D1-9739-4A6E-A00F-650544299148 wds:Q71776975-E601B460-586F-4717-A0C9-FEAA358F45B4
cites work	Characteristics of short-chain alcohol dehydrogenases and related enzymes Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Complete amino acid sequence of human placental 17 beta-hydroxysteroid dehydrogenase deduced from cDNA. Protein Denaturation Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution Determination and analysis of urea and guanidine hydrochloride denaturation curves The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites Multiphasic denaturation of glutathione transferase B1-1 by guanidinium chloride. Role of the dimeric structure on the flexibility of the active site A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of arc repressor The interconversion of estrone and estradiol by human tissue slices Solvent denaturation and stabilization of globular proteins Negative cooperativity in the binding of thyroxine to human serum prealbumin. Preparation of tritium-labeled 8-anilino-1-naphthalenesulfonic acid Estradiol 17 beta-dehydrogenase and 20 alpha-hydroxysteroid dehydrogenase from human placental cytosol: one enzyme with two activities? The unfolding and refolding of pig heart fumarase Inactivation before significant conformational change during denaturation of papain by guanidine hydrochloride Inactivation, subunit dissociation, aggregation, and unfolding of myosin subfragment 1 during guanidine denaturation Soluble 17β-hydroxysteroid dehydrogenase from human placenta. Evidence for a subunit structure Evidence for active half-molecules of alpha 2-macroglobulin formed by dissociation in urea A souble 17 beta-hydroxysteroid dehydrogenase from human placenta. The binding of pyridine nucleotides and steroids Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli A single step procedure for purification of estradiol 17 beta-dehydrogenase from human placenta Dissociation of the octameric bifunctional enzyme formiminotransferase-cyclodeaminase in urea. Isolation of two monofunctional dimers Denaturing behavior of glutathione reductase from cyanobacterium Spirulina maxima in guanidine hydrochloride. Dehydroepiandrosterone is a substrate for estradiol 17 β-dehydrogenase from human placenta
author name string	wds:Q71776975-11115181-D4A3-46E7-97D1-791AE60CF344 wds:Q71776975-2E4EF207-8995-4176-89BF-A926C4F8DBE7
author name string	G Mendoza-Hernández J L Rendón
rdfs:label	Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation (en) Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation (nl)
skos:prefLabel	Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation (en) Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation (nl)
name	Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation (en) Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation (nl)
title	wds:Q71776975-79B19F17-2AE2-4F31-9C4C-6FEB25EB8856
title	Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation (en)
page(s)	wds:Q71776975-C65E5E8B-48A2-4F5C-B9D6-2398E8DFCAF5
page(s)	219-227
instance of	wds:Q71776975-CB0E1828-51F6-499D-9691-B872B2E3BD2A
instance of	scholarly article
main subject	wds:Q71776975-DE6DD579-4F27-4E7F-B2F5-D423764E96D0
main subject	denaturation
PubMed ID	wds:Q71776975-0CD42694-6F20-4FBB-B160-480B5DCDDCB1
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8917625
PubMed ID	8917625
published in	wds:Q71776975-DD259009-35D9-4B33-AF7B-CDB2CB4E6555
published in	Biochimica et Biophysica Acta
issue	wds:Q71776975-F2D44AEE-D750-4E17-8BBD-DA47EE43AE3E
volume	wds:Q71776975-F0C9BF18-133F-41FF-B73A-F804C79EA0B2
issue	2
volume	1297
DOI	wds:Q71776975-89761F1D-036A-47FD-AF50-C4316365A435
DOI	http://dx.doi.org/10.1016/S0167-4838(96)00110-0
DOI	10.1016/S0167-4838(96)00110-0
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71776975
is cites work of	Aggregation, dissociation and unfolding of glucose dehydrogenase during urea denaturation
is cites work of	wds:Q73822384-4B8E438A-EF2D-4A39-B250-36508D7C79E4

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