Filters
Results 1 - 10 of 6694
Results 1 - 10 of 6694.
Search took: 0.03 seconds
Sort by: date | relevance |
Pfannes, H.D.; Martins, M.D. Delany; Bill, E.; Winkler, H.; Trautwein, A.X.
Proceedings of the 17. national meeting on condensed matter physics. Abstracts1994
Proceedings of the 17. national meeting on condensed matter physics. Abstracts1994
AbstractAbstract
[en] Short communication
Original Title
Estudo de hemoglobina nitrosilada por EPR e espectroscopia Moessbauer
Source
Sociedade Brasileira de Fisica, Sao Paulo, SP (Brazil); 427 p; 1994; p. 40-41; 17. Brazilian meeting on condensed matter physics; 17. Encontro nacional de fisica da materia condensada; Caxambu, MG (Brazil); 7-11 Jun 1994; Available from the Library of Brazilian Nuclear Energy Commission, Rio de Janeiro (BR)
Record Type
Miscellaneous
Literature Type
Conference
Country of publication
LanguageLanguage
Reference NumberReference Number
Related RecordRelated Record
INIS VolumeINIS Volume
INIS IssueINIS Issue
Alves, O.C.; Wajnberg, E.
Proceedings of the 17. national meeting on condensed matter physics. Abstracts1994
Proceedings of the 17. national meeting on condensed matter physics. Abstracts1994
AbstractAbstract
[en] Short communication
Original Title
Tempo de relaxacao spin-rede de hemoproteinas desnaturadas
Source
Sociedade Brasileira de Fisica, Sao Paulo, SP (Brazil); 427 p; 1994; p. 41; 17. Brazilian meeting on condensed matter physics; 17. Encontro nacional de fisica da materia condensada; Caxambu, MG (Brazil); 7-11 Jun 1994; Available from the Library of Brazilian Nuclear Energy Commission, Rio de Janeiro (BR)
Record Type
Miscellaneous
Literature Type
Conference
Country of publication
LanguageLanguage
Reference NumberReference Number
Related RecordRelated Record
INIS VolumeINIS Volume
INIS IssueINIS Issue
Tavanti, Michele; Porter, Joanne L.; Levy, Colin W.; Gómez Castellanos, J. Rubén; Flitsch, Sabine L.; Turner, Nicholas J., E-mail: sabine.flitsch@manchester.ac.uk, E-mail: nicholas.turner@manchester.ac.uk2018
AbstractAbstract
[en] Highlights: • The crystal structure of CYP116B45 (P450-TT) from T. thermophilus has been solved. • P450-TT crystal structure is the first example of a class VII P450 structure. • P450-TT adopts the typical P450-fold. • Structural deviation of regions involved in substrate recognition is observed. • Analysis of 96 class VII sequences revealed conservation of active site residues. The first crystal structure of a class VII P450, CYP116B46 from Tepidiphilus thermophilus, has been solved at 1.9 Å resolution. The structure reveals overall conservation of the P450-fold and a water conduit around the I-helix. Active site residues have been identified and sequence comparisons have been made with other class VII enzymes. A structure similarity search demonstrated that the P450-TT structure is similar to enzymes capable of oxy-functionalization of fatty acids, terpenes, macrolides, steroids and statins. The insight gained from solving this structure will provide a guideline for future engineering and modelling studies on this catalytically promiscuous class of enzymes.
Primary Subject
Source
S0006291X18310593; Available from http://dx.doi.org/10.1016/j.bbrc.2018.05.014; Copyright (c) 2018 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Biochemical and Biophysical Research Communications; ISSN 0006-291X;
; CODEN BBRCA9; v. 501(4); p. 846-850

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] The transcriptional factor Bach1 forms a heterodimer with small Maf family, and functions as a repressor of the Maf recognition element (MARE) in vivo. To investigate the involvement of Bach1 in the heme-dependent regulation of the expression of the α-globin gene, human erythroleukemia K562 cells were cultured with succinylacetone (SA), a heme biosynthetic inhibitor, and the level of α-globin mRNA was examined. A decrease of α-globin mRNA was observed in SA-treated cells, which was restored by the addition of hemin. The heme-dependent expression of α-globin occurred at the transcriptional level since the expression of human α-globin gene promoter-reporter gene containing hypersensitive site-40 (HS-40) was decreased when K562 cells were cultured with SA. Hemin treatment restored the decrease of the promoter activity by SA. The regulation of the HS-40 activity by heme was dependent on the NF-E2/AP-1 (NA) site, which is similar to MARE. The NA site-binding activity of Bach1 in K562 increased upon SA-treatment, and the increase was diminished by the addition of hemin. The transient expression of Bach1 and mutated Bach1 lacking CP motifs suppressed the HS-40 activity, and cancellation of the repressor activity by hemin was observed when wild-type Bach1 was expressed. The expression of NF-E2 strengthened the restoration of the Bach1-effect by hemin. Interestingly, nuclear localization of Bach1 increased when cells were treated with SA, while hemin induced the nuclear export of Bach1. These results indicated that heme plays an important role in the induction of α-globin gene expression through disrupting the interaction of Bach1 and the NA site in HS-40 enhancer in erythroid cells
Primary Subject
Source
S0006-291X(04)02065-0; Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Biochemical and Biophysical Research Communications; ISSN 0006-291X;
; CODEN BBRCA9; v. 324(1); p. 77-85

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] Expressions appropriate for the evaluation of the hyperfine splitting in ferric-hemoglobin hydroxide have been derived in the Hartree-Fock approximation using ''giant'' multielectron molecular-orbital wave functions formed as linear combinations of atomic orbitals of the constituent atoms and the molecular orbitals of the OH- complex incorporating overlap effects. Core orbitals as well as valence orbitals have been considered. The relevant multicenter matrix elements have been evaluated accurately by means of the analytical expressions which we have derived by employing a general closed-form expression developed previously for the coefficients of the expansion of a Slater orbital from one center onto the other. Various calculated electric field gradient components have been analyzed separately in terms of the valence and the core orbitals of the central ion (iron) interacting with the orbitals of the other constituent atoms and the complex OH-. One finds that the ''local'' and ''distant'' parts of the field gradient due to OH- nearly cancel one another and, consequently, produce negligible effect on the hyperfine splitting of iron. The nitrogens of the porphyrin plane contribute dominantly to the splitting. Other surrounding atoms contribute less and their influence decreases rapidly as their distance from the central ion increases. On combining various contributions, the calculated hyperfine splitting comes out to be 1.44 + 0.16 mm/sec, which agrees excellently with the experimental splitting 1.57 mm/sec observed by Lang and Marshall. The results from the present calculations have been compared with those obtained by Weissbluth and Maling employing semiempirical treatment on a porphyin-hydroxide model compound. Their estimate is found to give negative sign to the splitting in contrast with our result. Sources of disagreement have been pointed out. Positive hyperfine splitting in ferric-hemoglobin compounds is predicted
Primary Subject
Record Type
Journal Article
Journal
Physical Review. A; v. 18(2); p. 726-739
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] Recently, several members of a vertebrate protein family containing a six trans-membrane (6TM) domain and involved in apoptosis and cancer (e.g. STEAP, STAMP1, TSAP6), have been identified in Golgi and cytoplasmic membranes. The exact function of these proteins remains unknown. We related this 6TM domain to distant protein families using intermediate sequences and methods of iterative profile sequence similarity search. Here we show for the first time that this 6TM domain is homolog to the 6TM heme binding domain of both the NADPH oxidase (Nox) family and the YedZ family of bacterial oxidoreductases. This finding gives novel insights about the existence of a previously undetected electron transfer system involved in apoptosis and cancer, and suggests further steps in the experimental characterization of these evolutionarily related families
Primary Subject
Source
Available from http://dx.doi.org/10.1186/1471-2407-4-98; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC546010; PMCID: PMC546010; PUBLISHER-ID: 1471-2407-4-98; PMID: 15623366; OAI: oai:pubmedcentral.nih.gov:546010; Copyright (c) 2004 Sanchez-Pulido et al; licensee BioMed Central Ltd.; This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
BMC cancer (Online); ISSN 1471-2407;
; v. 4; p. 98

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
External URLExternal URL
Patterson, L.K.
Notre Dame Univ., IN (USA). Radiation Lab1980
Notre Dame Univ., IN (USA). Radiation Lab1980
AbstractAbstract
[en] Studies of irradiation induced lipid peroxidation in fatty acid micelles, both from our own lab and others, are briefly summarized. Steady state measurements have shown the dependence of hydroperoxide yield on the state of aggregation in the lipid and the degree to which the reactive sites are close packed. Chromatographic measurements obeyed the square root dependence of yield on dose rate confirming the proposed chain mechanism. Application to antioxidant studies have demonstrated the highly efficient blockage of the peroxidation chain by α-tocopherol and the subsequent prooxidant effect of the product formed. Time resolved studies have been used to determine rate information for .OH-lipid interaction, radical transfer within the lipid, radical peroxidation, lipid radical movement across the micellar boundary, chain termination, and radical interaction with α-tocopherol. Complimentary laser studies have demonstrated, in contrast to .OH behavior, the comparatively high degree of selectively exhibited by alkoxy radicals toward allylic lipid sites
Primary Subject
Source
1980; 9 p; International conference on oxygen and oxy-radicals in chemistry and biology; Austin, TX, USA; 26 - 29 May 1980; CONF-800591--1; Available from NTIS., PC A02/MF A01
Record Type
Report
Literature Type
Conference
Report Number
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
Yukl, Erik T.; Jensen, Lyndal M. R.; Davidson, Victor L.; Wilmot, Carrie M., E-mail: wilmo004@umn.edu2013
AbstractAbstract
[en] Crystal structures of MauG in complexes with MADH with its TTQ cofactor in the quinone and quinol forms are reported. MauG has been cocrystallized with methylamine dehydrogenase (MADH) with its TTQ cofactor in the o-quinol (TTQOQ) and quinone (TTQOX) forms and the structures of the resulting complexes have been solved. The TTQOQ structure crystallized in either space group P21 or C2, while the TTQOX structure crystallized in space group P1. The previously solved structure of MauG in complex with MADH bearing an incompletely formed TTQ cofactor (preMADH) also crystallized in space group P1, although with different unit-cell parameters. Despite the changes in crystal form, the structures are virtually identical, with only very minor changes at the protein–protein interface. The relevance of these structures with respect to the measured changes in affinity between MauG and various forms of MADH is discussed
Source
S1744309113016539; Available from http://dx.doi.org/10.1107/S1744309113016539; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3702316; PMCID: PMC3702316; PMID: 23832199; PUBLISHER-ID: tb5059; OAI: oai:pubmedcentral.nih.gov:3702316; Copyright (c) International Union of Crystallography 2013; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
External URLExternal URL
AbstractAbstract
No abstract available
Primary Subject
Secondary Subject
Source
International Atomic Energy Agency, Vienna (Austria). Joint FAO/IAEA Div. of Atomic Energy in Food and Agriculture; Panel proceedings series; p. 121-139; 1972; IAEA; Vienna; Latin American study group meeting on induced mutations and plant improvement; Buenos Aires, Argentina; 16 Nov 1970
Record Type
Book
Literature Type
Conference
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] Effects of different levels of soil moisture on growth up to maturity of two cultivars of Pennisetum americanum L. i.e. Tiftlate synthate and IC-8206 were investigated in pots containing sandy clay loam soil. There were four treatments each with six replicates. The survival and appearance of plants was better in response to moderate moisture levels. This shows the sensitivity of the test cultivars to water logging and drought. However, variations were observed in response to these stresses. The cultivars Tiftlate synthate and IC-8206 were found to be truly drought sensitive. Both the cultivars were found to be intermediate in their tolerance to waterlogged conditions. (author)
Primary Subject
Record Type
Journal Article
Journal
Journal of Science and Technology (Peshawar); ISSN 0250-5339;
; v. 27(1-2); p. 31-34

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
1 | 2 | 3 | Next |