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[PMID]:28457955
[Au] Autor:Tapadiya A; Vasanthan N
[Ad] Endereço:Department of Chemistry and Biochemistry, Long Island University, One University Plaza, Brooklyn, NY 11201, United States.
[Ti] Título:Crystallization and alkaline hydrolysis of poly(3- hydroxybutyrate) films probed by thermal analysis and infrared spectroscopy.
[So] Source:Int J Biol Macromol;102:1130-1137, 2017 Sep.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Poly(3-hydroxybutyrate) (PHB) is a microbially synthesized polymer, which is often purified by alkaline treatment. The effect of microstructure on alkaline hydrolysis has been studied by varying concentration of base and the temperature. The morphologies of PHB films before and after degradation were evaluated using DSC and FTIR spectroscopy. The hydrolytic degradation study by weight loss measurement revealed that the crystallinity of PHB greatly decreased the hydrolytic ability of PHB. The crystallization of PHB and the effect of base on hydrolysis was investigated by time dependent FTIR spectroscopy. The normalized absorbance of 3010cm and 1183cm were used to characterize the crystalline and the amorphous phases of PHB. FTIR spectroscopy reveal that the extent of hydrolysis decreased with increasing crystallinity. The crotonic acid was detected as a major product after hydrolysis, confirmed by UV/Visible and proton NMR spectroscopy. The normalized absorbance of the crystalline band at 3010cm band remained constant, suggesting that there is no significant change in crystallinity with degradation. The normalized amorphous band at 1183cm showed a decrease in absorbance ratio, suggesting degradation of the amorphous phase. Our data suggests that alkaline hydrolysis depends on concentration of base and the crystallinity of PHB.
[Mh] Termos MeSH primário: Ácido 3-Hidroxibutírico/química
Temperatura Ambiente
[Mh] Termos MeSH secundário: Cristalização
Concentração de Íons de Hidrogênio
Hidrólise
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
TZP1275679 (3-Hydroxybutyric Acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  2 / 47845 MEDLINE  
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[PMID]:29416037
[Au] Autor:Zabara A; Chong JTY; Martiel I; Stark L; Cromer BA; Speziale C; Drummond CJ; Mezzenga R
[Ad] Endereço:Department of Health Sciences and Technology, ETH Zurich, Schmelzbergstrasse 9 LFO E23, 8092, Zürich, Switzerland.
[Ti] Título:Design of ultra-swollen lipidic mesophases for the crystallization of membrane proteins with large extracellular domains.
[So] Source:Nat Commun;9(1):544, 2018 02 07.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In meso crystallization of membrane proteins from lipidic mesophases is central to protein structural biology but limited to membrane proteins with small extracellular domains (ECDs), comparable to the water channels (3-5 nm) of the mesophase. Here we present a strategy expanding the scope of in meso crystallization to membrane proteins with very large ECDs. We combine monoacylglycerols and phospholipids to design thermodynamically stable ultra-swollen bicontinuous cubic phases of double-gyroid (Ia3d), double-diamond (Pn3m), and double-primitive (Im3m) space groups, with water channels five times larger than traditional lipidic mesophases, and showing re-entrant behavior upon increasing hydration, of sequences Ia3d→Pn3m→Ia3d and Pn3m→Im3m→Pn3m, unknown in lipid self-assembly. We use these mesophases to crystallize membrane proteins with ECDs inaccessible to conventional in meso crystallization, demonstrating the methodology on the Gloeobacter ligand-gated ion channel (GLIC) protein, and show substantial modulation of packing, molecular contacts and activation state of the ensued proteins crystals, illuminating a general strategy in protein structural biology.
[Mh] Termos MeSH primário: Membrana Celular
Proteínas de Membrana/química
Fosfatidilgliceróis/química
[Mh] Termos MeSH secundário: Cristalização/métodos
Ácidos Graxos Monoinsaturados/química
Canais Iônicos
Transição de Fase
Domínios Proteicos
Termodinâmica
Água
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids, Monounsaturated); 0 (Ion Channels); 0 (Membrane Proteins); 0 (Phosphatidylglycerols); 059QF0KO0R (Water); 4271ZA8WXO (distearoyl phosphatidylglycerol)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180209
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02996-5


  3 / 47845 MEDLINE  
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[PMID]:29439228
[Au] Autor:Chen Y; Popko B
[Ad] Endereço:Department of Neurology, Center for Peripheral Neuropathy, University of Chicago, Chicago, IL 60637, USA.
[Ti] Título:Cholesterol crystals impede nerve repair.
[So] Source:Science;359(6376):635-636, 2018 02 09.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Colesterol/química
Cristalização
Regeneração Nervosa
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; COMMENT
[Nm] Nome de substância:
97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180214
[St] Status:MEDLINE
[do] DOI:10.1126/science.aar7369


  4 / 47845 MEDLINE  
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[PMID]:29384619
[Au] Autor:Zhao H; Wang YL; Peng JR; Zhang L; Qu Y; Chu BY; Dong ML; Tan LW; Qian ZY
[Ti] Título:Biodegradable Self-Assembled Micelles Based on MPEG-PTMC Copolymers: An Ideal Drug Delivery System for Vincristine.
[So] Source:J Biomed Nanotechnol;13(4):427-36, 2017 Apr.
[Is] ISSN:1550-7033
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite advantageous properties, micelles using methoxy poly(ethylene glycol)-poly(trimethylene carbonate) (MPEGPTMC) have not been widely studied. In this work, we aim to develop a novel vehicle for vincristine (VCR) based on a MPEG-PTMC micelle system. MPEG-PTMC with a series of molecular weights were synthesized and screened for the appropriate range for forming stable VCR micelles. The prepared micelles were then characterized in vitro and in vivo . VCR micelles presented high stability and ideal sustained release profile. The passive targeting effect was also enhanced compared with liposomal VCR. These results provide critical data to give the first clues regarding novel VCR micelles which exhibit potential for clinical application.
[Mh] Termos MeSH primário: Implantes Absorvíveis
Dioxanos/química
Implantes de Medicamento/química
Nanocápsulas/química
Polietilenoglicóis/química
Vincristina/administração & dosagem
Vincristina/química
[Mh] Termos MeSH secundário: Cristalização/métodos
Difusão
Composição de Medicamentos/métodos
Implantes de Medicamento/administração & dosagem
Micelas
Nanocápsulas/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dioxanes); 0 (Drug Implants); 0 (Micelles); 0 (Nanocapsules); 0 (monomethoxy poly(ethylene glycol)-block-poly(trimethylene carbonate)); 30IQX730WE (Polyethylene Glycols); 5J49Q6B70F (Vincristine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE


  5 / 47845 MEDLINE  
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[PMID]:29199986
[Au] Autor:Tarver CL; Pusey M
[Ad] Endereço:Department of Biological Science, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
[Ti] Título:A low-cost method for visible fluorescence imaging.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 12):657-663, 2017 Dec 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A wide variety of crystallization solutions are screened to establish conditions that promote the growth of a diffraction-quality crystal. Screening these conditions requires the assessment of many crystallization plates for the presence of crystals. Automated systems for screening and imaging are very expensive. A simple approach to imaging trace fluorescently labeled protein crystals in crystallization plates has been devised, and can be implemented at a cost as low as $50. The proteins ß-lactoglobulin B, trypsin and purified concanavalin A (ConA) were trace fluorescently labeled using three different fluorescent probes: Cascade Yellow (CY), Carboxyrhodamine 6G (CR) and Pacific Blue (PB). A crystallization screening plate was set up using ß-lactoglobulin B labeled with CR, trypsin labeled with CY, ConA labeled with each probe, and a mixture consisting of 50% PB-labeled ConA and 50% CR-labeled ConA. The wells of these plates were imaged using a commercially available macro-imaging lens attachment for smart devices that have a camera. Several types of macro lens attachments were tested with smartphones and tablets. Images with the highest quality were obtained with an iPhone 6S and an AUKEY Ora 10× macro lens. Depending upon the fluorescent probe employed and its Stokes shift, a light-emitting diode or a laser diode was used for excitation. An emission filter was used for the imaging of protein crystals labeled with CR and crystals with two-color fluorescence. This approach can also be used with microscopy systems commonly used to observe crystallization plates.
[Mh] Termos MeSH primário: Corantes Fluorescentes/química
Imagem Molecular/instrumentação
Imagem Molecular/métodos
Proteínas/química
[Mh] Termos MeSH secundário: Cor
Concanavalina A/química
Custos e Análise de Custo
Cristalização
Desenho de Equipamento
Fluorescência
Lactoglobulinas/química
Imagem Molecular/economia
Rodaminas/química
Smartphone/economia
Smartphone/instrumentação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (6-carboxyrhodamine-6G); 0 (Fluorescent Dyes); 0 (Lactoglobulins); 0 (Proteins); 0 (Rhodamines); 11028-71-0 (Concanavalin A)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17015941


  6 / 47845 MEDLINE  
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[PMID]:29342202
[Au] Autor:Mayorova TD; Smith CL; Hammar K; Winters CA; Pivovarova NB; Aronova MA; Leapman RD; Reese TS
[Ad] Endereço:Laboratory of Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, United States of America.
[Ti] Título:Cells containing aragonite crystals mediate responses to gravity in Trichoplax adhaerens (Placozoa), an animal lacking neurons and synapses.
[So] Source:PLoS One;13(1):e0190905, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Trichoplax adhaerens has only six cell types. The function as well as the structure of crystal cells, the least numerous cell type, presented an enigma. Crystal cells are arrayed around the perimeter of the animal and each contains a birefringent crystal. Crystal cells resemble lithocytes in other animals so we looked for evidence they are gravity sensors. Confocal microscopy showed that their cup-shaped nuclei are oriented toward the edge of the animal, and that the crystal shifts downward under the influence of gravity. Some animals spontaneously lack crystal cells and these animals behaved differently upon being tilted vertically than animals with a typical number of crystal cells. EM revealed crystal cell contacts with fiber cells and epithelial cells but these contacts lacked features of synapses. EM spectroscopic analyses showed that crystals consist of the aragonite form of calcium carbonate. We thus provide behavioral evidence that Trichoplax are able to sense gravity, and that crystal cells are likely to be their gravity receptors. Moreover, because placozoans are thought to have evolved during Ediacaran or Cryogenian eras associated with aragonite seas, and their crystals are made of aragonite, they may have acquired gravity sensors during this early era.
[Mh] Termos MeSH primário: Carbonato de Cálcio/metabolismo
Gravitação
Placozoa/metabolismo
[Mh] Termos MeSH secundário: Animais
Carbonato de Cálcio/química
Cristalização
Corantes Fluorescentes
Microscopia Eletrônica de Varredura
Microscopia Eletrônica de Transmissão
Neurônios
Placozoa/citologia
Análise Espectral/métodos
Sinapses
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Fluorescent Dyes); H0G9379FGK (Calcium Carbonate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190905


  7 / 47845 MEDLINE  
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[PMID]:28470596
[Au] Autor:Cooper CDO; Marsden BD
[Ad] Endereço:Department of Biological Sciences, School of Applied Sciences, University of Huddersfield, Queensgate, Huddersfield, West Yorkshire, HD1 3DH, UK. c.d.cooper@hud.ac.uk.
[Ti] Título:N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools.
[So] Source:Methods Mol Biol;1586:11-31, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Soluble protein expression is a key requirement for biochemical and structural biology approaches to study biological systems in vitro. Production of sufficient quantities may not always be achievable if proteins are poorly soluble which is frequently determined by physico-chemical parameters such as intrinsic disorder. It is well known that discrete protein domains often have a greater likelihood of high-level soluble expression and crystallizability. Determination of such protein domain boundaries can be challenging for novel proteins. Here, we outline the application of bioinformatics tools to facilitate the prediction of potential protein domain boundaries, which can then be used in designing expression construct boundaries for parallelized screening in a range of heterologous expression systems.
[Mh] Termos MeSH primário: Proteínas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Biologia Computacional
Cristalização
Bases de Dados de Proteínas
Seres Humanos
Cadeias de Markov
Modelos Biológicos
Modelos Moleculares
Conformação Proteica
Domínios Proteicos
Software
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_2


  8 / 47845 MEDLINE  
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[PMID]:29426296
[Au] Autor:Iu LPL; Fan MCY; Lam WC; Wong IYH
[Ad] Endereço:Department of Ophthalmology, The University of Hong Kong, Grantham Hospital, 125 Wong Chuk Hang Road, Aberdeen, Hong Kong, Hong Kong. lawipl@hku.hk.
[Ti] Título:Repeated intraocular crystallization of ganciclovir in one eye after bilateral intravitreal injections: a case report.
[So] Source:BMC Ophthalmol;18(1):36, 2018 Feb 09.
[Is] ISSN:1471-2415
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cytomegalovirus (CMV) retinitis is an opportunistic infection that primarily affects immunocompromised individuals. Intravitreal ganciclovir injection monotherapy or in combination with systemic anti-CMV therapy are effective treatments for CMV retinitis. Crystallization of ganciclovir after intravitreal injection is extremely rare. Only two cases had been reported in literature. Crystallization in only one eye after bilateral injections had not been reported before. We hereby report a case of intraocular ganciclovir crystallization in one eye after bilateral intravitreal injections, and repeated crystallization in the same eye after repeated injections. CASE PRESENTATION: A 79-year-old patient had bilateral cytomegalovirus retinitis and received bilateral intravitreal ganciclovir injections of 2.5 mg in 0.05 ml sterile water. Fundus examination after injection showed formation of needle-shaped, golden-yellow crystals in the vitreous of right eye but not in left eye. The crystals dissolved spontaneously. Repeated bilateral intravitreal ganciclovir injections 4 days later resulted in repeated crystallization of ganciclovir in right eye but not in left eye. The crystals dissolved spontaneously and completely after 5 minutes. Visual acuity remained unchanged and intraocular pressure was normal. CONCLUSIONS: Intraocular ganciclovir crystallization could occur after intravitreal injections. It is important to perform fundus examination after injection. The crystals may dissolve rapidly and vitrectomy may not be necessary. Our case suggested intraocular ganciclovir crystallization is an idiosyncratic phenomenon, subjects to distinctive intraocular environment which could be different between two eyes of the same patient. The susceptible intraocular environment could be persistent leading to repeated crystallization.
[Mh] Termos MeSH primário: Antivirais/química
Precipitação Química
Retinite por Citomegalovirus/tratamento farmacológico
Ganciclovir/química
Corpo Vítreo/efeitos dos fármacos
[Mh] Termos MeSH secundário: Idoso
Antivirais/uso terapêutico
Cristalização
Retinite por Citomegalovirus/diagnóstico
Evolução Fatal
Ganciclovir/uso terapêutico
Seres Humanos
Injeções Intravítreas
Masculino
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); P9G3CKZ4P5 (Ganciclovir)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180211
[St] Status:MEDLINE
[do] DOI:10.1186/s12886-018-0703-8


  9 / 47845 MEDLINE  
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[PMID]:29246762
[Au] Autor:Terrell JR; Gumpper RH; Luo M
[Ad] Endereço:Department of Chemistry, Georgia State University, Atlanta, GA 30302, USA; Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30302, USA.
[Ti] Título:Hemoglobin crystals immersed in liquid oxygen reveal diffusion channels.
[So] Source:Biochem Biophys Res Commun;495(2):1858-1863, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human hemoglobin (HbA) transports molecular oxygen (O ) from the lung to tissues where the partial pressure of O is lower. O binds to HbA at the heme cofactor and is stabilized by a distal histidine (HisE7). HisE7 has been observed to occupy opened and closed conformations, and is postulated to act as a gate controlling the binding/release of O . However, it has been suggested that HbA also contains intraprotein oxygen channels for entrances/exits far from the heme. In this study, we developed a novel method of crystal immersion in liquid oxygen prior to X-ray data collection. In the crystals immersed in liquid oxygen, the heme center was oxidized to generate aquomethemoglobin. Increases of structural flexibility were also observed in regions that are synonymous with previously postulated oxygen channels. These regions also correspond to medically relevant mutations which affect O affinity. The way HbA utilizes these O channels could have a profound impact on understanding the relationship of HbA O transport within these disease conditions. Finally, the liquid oxygen immersion technique can be utilized as a new tool to crystallographically examine proteins and protein complexes which utilize O for enzyme catalysis or transport.
[Mh] Termos MeSH primário: Cristalização/métodos
Hemoglobinas/química
Hemoglobinas/ultraestrutura
Simulação de Dinâmica Molecular
Oxigênio/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Difusão
Porosidade
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hemoglobins); S88TT14065 (Oxygen)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE


  10 / 47845 MEDLINE  
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[PMID]:29199979
[Au] Autor:Quirnheim Pais D; Rathmann B; Koepke J; Tomova C; Wurzinger P; Thielmann Y
[Ad] Endereço:Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.
[Ti] Título:A standardized technique for high-pressure cooling of protein crystals.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 12):997-1006, 2017 Dec 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cryogenic temperatures slow down secondary radiation damage during data collection from macromolecular crystals. In 1973, cooling at high pressure was identified as a method for cryopreserving crystals in their mother liquor [Thomanek et al. (1973). Acta Cryst. A29, 263-265]. Results from different groups studying different crystal systems indicated that the approach had merit, although difficulties in making the process work have limited its widespread use. Therefore, a simplified and reliable technique has been developed termed high-pressure cooling (HPC). An essential requirement for HPC is to protect crystals in capillaries. These capillaries form part of new sample holders with SPINE standard dimensions. Crystals are harvested with the capillary, cooled at high pressure (220 MPa) and stored in a cryovial. This system also allows the usage of the standard automation at the synchrotron. Crystals of hen egg-white lysozyme and concanavalin A have been successfully cryopreserved and yielded data sets to resolutions of 1.45 and 1.35 Å, respectively. Extensive work has been performed to define the useful working range of HPC in capillaries with 250 µm inner diameter. Three different 96-well crystallization screens that are most frequently used in our crystallization facility were chosen to study the formation of amorphous ice in this cooling setup. More than 89% of the screening solutions were directly suitable for HPC. This achievement represents a drastic improvement for crystals that suffered from cryoprotection or were not previously eligible for cryoprotection.
[Mh] Termos MeSH primário: Cristalização
Cristalografia por Raios X/instrumentação
Síncrotrons
[Mh] Termos MeSH secundário: Animais
Galinhas
Temperatura Baixa
Concanavalina A/química
Criopreservação
Crioprotetores/química
Muramidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cryoprotective Agents); 11028-71-0 (Concanavalin A); EC 3.2.1.- (hen egg lysozyme); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317016357



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