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Pesquisa : G02.111.570.060 [Categoria DeCS]
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  1 / 454298 MEDLINE  
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[PMID]:29447197
[Au] Autor:Fujita T; Kozuka-Hata H; Hori Y; Takeuchi J; Kubo T; Oyama M
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
[Ti] Título:Shotgun proteomics deciphered age/division of labor-related functional specification of three honeybee (Apis mellifera L.) exocrine glands.
[So] Source:PLoS One;13(2):e0191344, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The honeybee (Apis mellifera L.) uses various chemical signals produced by the worker exocrine glands to maintain the functioning of its colony. The roles of worker postcerebral glands (PcGs), thoracic glands (TGs), and mandibular glands (MGs) and the functional changes they undergo according to the division of labor from nursing to foraging are not as well studied. To comprehensively characterize the molecular roles of these glands in workers and their changes according to the division of labor of workers, we analyzed the proteomes of PcGs, TGs, and MGs from nurse bees and foragers using shotgun proteomics technology. We identified approximately 2000 proteins from each of the nurse bee or forager glands and highlighted the features of these glands at the molecular level by semiquantitative enrichment analyses of frequently detected, gland-selective, and labor-selective proteins. First, we found the high potential to produce lipids in PcGs and MGs, suggesting their relation to pheromone production. Second, we also found the proton pumps abundant in TGs and propose some transporters possibly related to the saliva production. Finally, our data unveiled candidate enzymes involved in labor-dependent acid production in MGs.
[Mh] Termos MeSH primário: Abelhas/genética
Glândulas Exócrinas/fisiologia
Proteômica/métodos
[Mh] Termos MeSH secundário: Fatores Etários
Sequência de Aminoácidos
Animais
Abelhas/metabolismo
Comportamento Animal/fisiologia
Glândulas Exócrinas/citologia
Glândulas Exócrinas/metabolismo
Proteínas de Insetos/metabolismo
Feromônios/metabolismo
Proteoma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Insect Proteins); 0 (Pheromones); 0 (Proteome)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191344


  2 / 454298 MEDLINE  
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[PMID]:29381770
[Au] Autor:Lin CY; Lin LY
[Ad] Endereço:Institute of Molecular and Cellular Biology and Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan, ROC.
[Ti] Título:The conserved basic residues and the charged amino acid residues at the α-helix of the zinc finger motif regulate the nuclear transport activity of triple C2H2 zinc finger proteins.
[So] Source:PLoS One;13(1):e0191971, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Zinc finger (ZF) motifs on proteins are frequently recognized as a structure for DNA binding. Accumulated reports indicate that ZF motifs contain nuclear localization signal (NLS) to facilitate the transport of ZF proteins into nucleus. We investigated the critical factors that facilitate the nuclear transport of triple C2H2 ZF proteins. Three conserved basic residues (hot spots) were identified among the ZF sequences of triple C2H2 ZF proteins that reportedly have NLS function. Additional basic residues can be found on the α-helix of the ZFs. Using the ZF domain (ZFD) of Egr-1 as a template, various mutants were constructed and expressed in cells. The nuclear transport activity of various mutants was estimated by analyzing the proportion of protein localized in the nucleus. Mutation at any hot spot of the Egr-1 ZFs reduced the nuclear transport activity. Changes of the basic residues at the α-helical region of the second ZF (ZF2) of the Egr-1 ZFD abolished the NLS activity. However, this activity can be restored by substituting the acidic residues at the homologous positions of ZF1 or ZF3 with basic residues. The restored activity dropped again when the hot spots at ZF1 or the basic residues in the α-helix of ZF3 were mutated. The variations in nuclear transport activity are linked directly to the binding activity of the ZF proteins with importins. This study was extended to other triple C2H2 ZF proteins. SP1 and KLF families, similar to Egr-1, have charged amino acid residues at the second (α2) and the third (α3) positions of the α-helix. Replacing the amino acids at α2 and α3 with acidic residues reduced the NLS activity of the SP1 and KLF6 ZFD. The reduced activity can be restored by substituting the α3 with histidine at any SP1 and KLF6 ZFD. The results show again the interchangeable role of ZFs and charge residues in the α-helix in regulating the NLS activity of triple C2H2 ZF proteins.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
Núcleo Celular/metabolismo
Dedos de Zinco
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191971


  3 / 454298 MEDLINE  
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[PMID]:29381737
[Au] Autor:Wang Y; Zhang T; Song X; Zhang J; Dang Z; Pei X; Long Y
[Ad] Endereço:MOA Key Laboratory on Safety Assessment (Molecular) of Agri-GMO, Institute of Biotechnology, Chinese Academy of Agricultural Sciences, Beijing, China.
[Ti] Título:Identification and functional analysis of two alternatively spliced transcripts of ABSCISIC ACID INSENSITIVE3 (ABI3) in linseed flax (Linum usitatissimum L.).
[So] Source:PLoS One;13(1):e0191910, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alternative splicing is a popular phenomenon in different types of plants. It can produce alternative spliced transcripts that encode proteins with altered functions. Previous studies have shown that one transcription factor, ABSCISIC ACID INSENSITIVE3 (ABI3), which encodes an important component in abscisic acid (ABA) signaling, is subjected to alternative splicing in both mono- and dicotyledons. In the current study, we identified two homologs of ABI3 in the genome of linseed flax. We screened two alternatively spliced flax LuABI3 transcripts, LuABI3-2 and LuABI3-3, and one normal flax LuABI3 transcript, LuABI3-1. Sequence analysis revealed that one of the alternatively spliced transcripts, LuABI3-3, retained a 6 bp intron. RNA accumulation analysis showed that all three transcripts were expressed during seed development, while subcellular localization and transgene experiments showed that LuABI3-3 had no biological function. The two normal transcripts, LuABI3-1 and LuABI3-2, are the important functional isoforms in flax and play significant roles in the ABA regulatory pathway during seed development, germination, and maturation.
[Mh] Termos MeSH primário: Processamento Alternativo
Linho/genética
Genes de Plantas
Proteínas de Plantas/genética
RNA Mensageiro/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arabidopsis/genética
Germinação/genética
Proteínas de Plantas/química
Plantas Geneticamente Modificadas
Homologia de Sequência de Aminoácidos
Frações Subcelulares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plant Proteins); 0 (RNA, Messenger)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191910


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[PMID]:29355528
[Au] Autor:Zhu J; Li S; Ramelot TA; Kennedy MA; Liu M; Yang Y
[Ad] Endereço:State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan 430071, China.
[Ti] Título:Structural insights into the impact of two holoprosencephaly-related mutations on human TGIF1 homeodomain.
[So] Source:Biochem Biophys Res Commun;496(2):575-581, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human protein TGIF1 is an essential regulator of cell fate with broad roles in different tissues, and has been implicated in holoprosencephaly (HPE) and many cancers. The function of TGIF1 in transcriptional regulation depends on its three-amino acid loop extension (TALE) type of homeodomain (HD). Two missense mutations that led to P192A and R219C substitutions in TGIF1-HD were previously found in HPE patients and suggested to be the causes for these cases. However, how these mutations affected TGIF1 function has not been investigated from a structural view. Here, we investigated the roles of P192 and R219 in TGIF1-HD structure packing through determining the NMR structure of TGIF1-HD. Surprisingly, P192 and R219 were found to play roles in packing α1 and α2 to α3 together with A190 and F215 through side-chain interactions. Circular dichroism (CD) showed that P192A and R219C mutants displayed structural change and less folding compared with wild-type TGIF1-HD, and H- N HSQC spectrum of P192A mutant exhibited chemical shift perturbations in all three helices of TGIF1-HD. Thus, it is suggested that P192A and R219C mutations led to structure disturbances of TGIF1-HD, which subsequently reduced the DNA-binding affinity of TGIF1-HD by 23-fold and 10-fold respectively, as revealed by the isothermal titration calorimetry (ITC) experiments. Our study provides structural insights of the probable pathogenesis mechanism of two TGIF1-related HPE cases, and evidences for the roles of P192 and R219 in HD folding.
[Mh] Termos MeSH primário: Holoprosencefalia/genética
Proteínas de Homeodomínio/química
Proteínas de Homeodomínio/genética
Mutação Puntual
Proteínas Repressoras/química
Proteínas Repressoras/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
DNA/metabolismo
Holoprosencefalia/metabolismo
Proteínas de Homeodomínio/metabolismo
Seres Humanos
Modelos Moleculares
Mutação de Sentido Incorreto
Ressonância Magnética Nuclear Biomolecular
Conformação Proteica
Dobramento de Proteína
Proteínas Repressoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Homeodomain Proteins); 0 (Repressor Proteins); 0 (TGIF1 protein, human); 9007-49-2 (DNA)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180123
[St] Status:MEDLINE


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[PMID]:29346419
[Au] Autor:Holcomb J; Doughan M; Spellmon N; Lewis B; Perry E; Zhang Y; Nico L; Wan J; Chakravarthy S; Shang W; Miao Q; Stemmler T; Yang Z
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan, United States of America.
[Ti] Título:SAXS analysis of a soluble cytosolic NgBR construct including extracellular and transmembrane domains.
[So] Source:PLoS One;13(1):e0191371, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Nogo-B receptor (NgBR) is involved in oncogenic Ras signaling through directly binding to farnesylated Ras. It recruits farnesylated Ras to the non-lipid-raft membrane for interaction with downstream effectors. However, the cytosolic domain of NgBR itself is only partially folded. The lack of several conserved secondary structural elements makes this domain unlikely to form a complete farnesyl binding pocket. We find that inclusion of the extracellular and transmembrane domains that contain additional conserved residues to the cytosolic region results in a well folded protein with a similar size and shape to the E.coli cis-isoprenyl transferase (UPPs). Small Angle X-ray Scattering (SAXS) analysis reveals the radius of gyration (Rg) of our NgBR construct to be 18.2 Å with a maximum particle dimension (Dmax) of 61.0 Å. Ab initio shape modeling returns a globular molecular envelope with an estimated molecular weight of 23.0 kD closely correlated with the calculated molecular weight. Both Kratky plot and pair distribution function of NgBR scattering reveal a bell shaped peak which is characteristic of a single globularly folded protein. In addition, circular dichroism (CD) analysis reveals that our construct has the secondary structure contents similar to the UPPs. However, this result does not agree with the currently accepted topological orientation of NgBR which might partition this construct into three separate domains. This discrepancy suggests another possible NgBR topology and lends insight into a potential molecular basis of how NgBR facilitates farnesylated Ras recruitment.
[Mh] Termos MeSH primário: Receptores de Superfície Celular/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Membrana Celular/metabolismo
Dicroísmo Circular
Citosol/metabolismo
Peso Molecular
Estrutura Secundária de Proteína
Receptores de Superfície Celular/metabolismo
Espalhamento a Baixo Ângulo
Homologia de Sequência de Aminoácidos
Solubilidade
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NUS1 protein, human); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191371


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[PMID]:29324789
[Au] Autor:Choi JH; Shin KC; Oh DK
[Ad] Endereço:Department of Bioscience and Biotechnology, Konkuk University, Seoul, Republic of Korea.
[Ti] Título:An L213A variant of ß-glycosidase from Sulfolobus solfataricus with increased α-L-arabinofuranosidase activity converts ginsenoside Rc to compound K.
[So] Source:PLoS One;13(1):e0191018, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Compound K (C-K) is a crucial pharmaceutical and cosmetic component because of disease prevention and skin anti-aging effects. For industrial application of this active compound, the protopanaxadiol (PPD)-type ginsenosides should be transformed to C-K. ß-Glycosidase from Sulfolobus solfataricus has been reported as an efficient C-K-producing enzyme, using glycosylated PPD-type ginsenosides as substrates. ß-Glycosidase from S. solfataricus can hydrolyze ß-d-glucopyranoside in ginsenosides Rc, C-Mc1, and C-Mc, but not α-l-arabinofuranoside in these ginsenosides. To determine candidate residues involved in α-l-arabinofuranosidase activity, compound Mc (C-Mc) was docking to ß-glycosidase from S. solfataricus in homology model and sequence was aligned with ß-glycosidase from Pyrococcus furiosus that has α-l-arabinofuranosidase activity. A L213A variant ß-glycosidase with increased α-l-arabinofuranosidase activity was selected by substitution of other amino acids for candidate residues. The increased α-l-arabinofuranosidase activity of the L213A variant was confirmed through the determination of substrate specificity, change in binding energy, transformation pathway, and C-K production from ginsenosides Rc and C-Mc. The L213A variant ß-glycosidase catalyzed the conversion of Rc to Rd by hydrolyzing α-l-arabinofuranoside linked to Rc, whereas the wild-type ß-glycosidase did not. The variant enzyme converted ginsenosides Rc and C-Mc into C-K with molar conversions of 97%, which were 1.5- and 2-fold higher, respectively, than those of the wild-type enzyme. Therefore, protein engineering is a useful tool for enhancing the hydrolytic activity on specific glycoside linked to ginsenosides.
[Mh] Termos MeSH primário: Ginsenosídeos/metabolismo
Glicosídeo Hidrolases/metabolismo
Sulfolobus solfataricus/enzimologia
beta-Glucosidase/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Genes Bacterianos
Mutagênese Sítio-Dirigida
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
beta-Glucosidase/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ginsenosides); 0 (ginsenoside M1); 0K83B0L786 (ginsenoside Rc); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.55 (alpha-N-arabinofuranosidase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191018


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[PMID]:29309431
[Au] Autor:Carmalt JL; Mortazavi S; McOnie RC; Allen AL; Unniappan S
[Ad] Endereço:Department of Large Animal Clinical Sciences, Western College of Veterinary Medicine, University of Saskatchewan, Saskatoon, SK, Canada.
[Ti] Título:Profiles of pro-opiomelanocortin and encoded peptides, and their processing enzymes in equine pituitary pars intermedia dysfunction.
[So] Source:PLoS One;13(1):e0190796, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Equine pituitary pars intermedia dysfunction (PPID) is characterized by hyperplasia of the pars intermedia (PI) melanotrophs of the pituitary gland (PG), and increased production of proopiomelanocortin (POMC). POMC is cleaved by prohormone convertase 1 (PC1) to produce adrenocorticotropic hormone (ACTH), and further processing of ACTH by PC2 to produce alpha-melanocyte stimulating hormone (α-MSH) and corticotropin-like intermediate peptide (CLIP). High plasma ACTH concentrations in horses with PPID might be related to reduced conversion of ACTH to α-MSH by PCs. The hypothesis of this study was that PC1 and PC2 expression in the pituitary gland are altered in PPID, resulting in an abnormal relative abundance of POMC derived proteins. The objectives of this study were to identify the partial sequences of equine POMC, PC1, and PC2 mRNAs; and to determine whether the expression of POMC, PC1, and PC2 mRNAs in whole pituitary extracts, and POMC-protein in the cavernous sinus blood of horses are altered in PPID. We confirmed (RT-PCR and sequencing) that the partial sequences obtained match the corresponding regions of predicted equine POMC, PC1 and PC2 sequences. The expression (quantification by RT-qPCR) of POMC, PC1 and PC2 mRNAs were found upregulated in the pituitary of horses with PPID. Plasma (measured using RIA/ELISA) ACTH and α-MSH were elevated in PPID horses. These results indicate distinct differences in gene and protein expression of POMC and its intermediates, and processing enzymes in PPID. It provides evidence to support the notion that local, pituitary-specific inadequacies in prohormone processing likely contribute to equine PPID.
[Mh] Termos MeSH primário: Peptídeos/metabolismo
Adeno-Hipófise Parte Intermédia/metabolismo
Pró-Opiomelanocortina/metabolismo
[Mh] Termos MeSH secundário: Hormônio Adrenocorticotrópico/sangue
Sequência de Aminoácidos
Animais
Ensaio de Imunoadsorção Enzimática
Cavalos
Adeno-Hipófise Parte Intermédia/enzimologia
Pró-Opiomelanocortina/sangue
Pró-Opiomelanocortina/química
Pró-Opiomelanocortina/genética
Pró-Proteína Convertase 1/genética
Pró-Proteína Convertase 1/metabolismo
Pró-Proteína Convertase 2/genética
Pró-Proteína Convertase 2/metabolismo
RNA Mensageiro/metabolismo
Homologia de Sequência de Aminoácidos
alfa-MSH/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 0 (RNA, Messenger); 581-05-5 (alpha-MSH); 66796-54-1 (Pro-Opiomelanocortin); 9002-60-2 (Adrenocorticotropic Hormone); EC 3.4.21.93 (Proprotein Convertase 1); EC 3.4.21.94 (Proprotein Convertase 2)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190796


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[PMID]:29272750
[Au] Autor:Galibert M; Wartenberg M; Lecaille F; Saidi A; Mavel S; Joulin-Giet A; Korkmaz B; Brömme D; Aucagne V; Delmas AF; Lalmanach G
[Ad] Endereço:CNRS UPR 4301, Centre de Biophysique Moléculaire, Rue Charles Sadron, Orléans, France.
[Ti] Título:Substrate-derived triazolo- and azapeptides as inhibitors of cathepsins K and S.
[So] Source:Eur J Med Chem;144:201-210, 2018 Jan 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Cathepsin (Cat) K is a critical bone-resorbing protease and is a relevant target for the treatment of osteoporosis and bone metastasis, while CatS is an attractive target for drugs in autoimmune diseases (e.g. rheumatoid arthritis), emphysema or neuropathic pain. Despite major achievements, current pharmacological inhibitors are still lacking in safety and may have damaging side effects. A promising strategy for developing safer reversible and competitive inhibitors as new lead compounds could be to insert non-cleavable bonds at the scissile P1-P1' position of selective substrates of CatS and CatK. Accordingly, we introduced a 1,4-disubstituted 1,2,3-triazole heterocycle that mimics most of the features of a trans-amide bond, or we incorporated a semicarbazide bond (azaGly residue) by replacing the α-carbon of the glycyl residue at P1 by a nitrogen atom. AzaGly-containing peptidomimetics inhibited powerfully their respective target proteases in the nM range, while triazolopeptides were weaker inhibitors (Ki in the µM range). The selectivity of the azaGly CatS inhibitor (1b) was confirmed by using spleen lysates from wild-type vs CatS-deficient mice. Alternatively, the azaGly bradykinin-derived CatK inhibitor (2b) potently inhibited CatK (Ki = 9 nM) and impaired its kininase activity in vitro. Molecular modeling studies support that the semicarbazide bond of 2b is more favorable than the 1,2,3-triazole linkage of the bradykinin-derived pseudopeptide 2a to preserve an effective affinity towards CatK, its protease target.
[Mh] Termos MeSH primário: Catepsina K/antagonistas & inibidores
Catepsinas/antagonistas & inibidores
Inibidores de Proteases/química
Inibidores de Proteases/farmacologia
Triazóis/química
Triazóis/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Catepsina K/metabolismo
Catepsinas/metabolismo
Seres Humanos
Camundongos Endogâmicos C57BL
Simulação de Acoplamento Molecular
Peptídeos/química
Peptídeos/farmacologia
Peptidomiméticos/química
Peptidomiméticos/farmacologia
Relação Estrutura-Atividade
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Peptidomimetics); 0 (Protease Inhibitors); 0 (Triazoles); EC 3.4.- (Cathepsins); EC 3.4.22.27 (cathepsin S); EC 3.4.22.38 (Cathepsin K)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE


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[PMID]:29208012
[Au] Autor:Pereira A; Paro R
[Ad] Endereço:Department of Biosystems Science and Engineering, ETH Zurich, 4058, Basel, Switzerland.
[Ti] Título:Pho dynamically interacts with Spt5 to facilitate transcriptional switches at the hsp70 locus.
[So] Source:Epigenetics Chromatin;10(1):57, 2017 12 06.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Numerous target genes of the Polycomb group (PcG) are transiently activated by a stimulus and subsequently repressed. However, mechanisms by which PcG proteins regulate such target genes remain elusive. RESULTS: We employed the heat shock-responsive hsp70 locus in Drosophila to study the chromatin dynamics of PRC1 and its interplay with known regulators of the locus before, during and after heat shock. We detected mutually exclusive binding patterns for HSF and PRC1 at the hsp70 locus. We found that Pleiohomeotic (Pho), a DNA-binding PcG member, dynamically interacts with Spt5, an elongation factor. The dynamic interaction switch between Pho and Spt5 is triggered by the recruitment of HSF to chromatin. Mutation in the protein-protein interaction domain (REPO domain) of Pho interferes with the dynamics of its interaction with Spt5. The transcriptional kinetics of the heat shock response is negatively affected by a mutation in the REPO domain of Pho. CONCLUSIONS: We propose that a dynamic interaction switch between PcG proteins and an elongation factor enables stress-inducible genes to efficiently switch between ON/OFF states in the presence/absence of the activating stimulus.
[Mh] Termos MeSH primário: Proteínas Cromossômicas não Histona/metabolismo
Proteínas de Drosophila/metabolismo
Proteínas de Choque Térmico HSP70/genética
Proteínas do Grupo Polycomb/metabolismo
Fatores de Elongação da Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Cromatina/metabolismo
Proteínas de Drosophila/química
Drosophila melanogaster
Resposta ao Choque Térmico
Proteínas do Grupo Polycomb/química
Ligação Proteica
Homologia de Sequência de Aminoácidos
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Drosophila Proteins); 0 (HSP70 Heat-Shock Proteins); 0 (Polycomb-Group Proteins); 0 (Transcriptional Elongation Factors); 0 (pho protein, Drosophila); 138673-72-0 (SPT5 transcriptional elongation factor)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1186/s13072-017-0166-9


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[PMID]:28465230
[Au] Autor:Zhu F; Xiao S; Zhang Y; Shao Y; Tang F; Chen S; Bai X
[Ad] Endereço:Institute of Sericulture and Apiculture, Yunnan Academy of Agricultural Sciences, Mengzi 661101, Yunnan, China. Electronic address: 18287322700@163.com.
[Ti] Título:Molecular characterization and expression analysis of Turtle protein in silkworm that is associated with Nosema bombycis infection.
[So] Source:Infect Genet Evol;52:67-74, 2017 Aug.
[Is] ISSN:1567-7257
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In this report, we describe the cloning and characterization of a member of the immunoglobulin superfamily (IgSF); i.e., Turtle. The cDNA of Turtle was cloned from the silkworm Bombyx mori using the rapid amplification of cDNA ends (RACE) technique. Three isoforms of Bombyx Turtle were obtained, including Bmtutl-464, Bmtutl-519, and Bmtutl-810. The three isoforms had identical 27-amino acid signal peptides and four extracellular immunoglobulin (Ig) domains (IgI-IgIV). Sequence similarity and phylogenic analysis indicated that Bmtutl-810 belongs to the group of insect Turtle isoforms and shares 76.2% identity with Drosophila Turtle. Quantitative real-time PCR analysis revealed that the Bombyx Turtle isoforms were expressed throughout the entire development period, the highest levels of expression of Bmtutl-464 and Bmtutl-519 were observed at the second instar larvae stage, whereas that of Bmtutl-810 peaked at the embryonic stage. The ubiquitous expression of Bmtutl-464, Bmtutl-519, and Bmtutl-810 were observed in all studied tissues, except for Bmtutl-519 in the silk gland. The expression level of Bmtutl-464 was highest in the ovary, whereas that of Bmtutl-519 and Bmtutl-810 was highest in the hemolymph. Bmtutl-519 was upregulated in BmN cells infected by Nosema bombycis, We speculated that Bombyx Turtle was not only involved in neural development in silkworm, as well as Drosophila Turtle, but was also involved in the regulation of other biological functions. For example, Bmtutl-519 might be involved in N. bombycis infection and may play an important role in the immune response of silkworms to N. bombycis infection.
[Mh] Termos MeSH primário: Bombyx/crescimento & desenvolvimento
Clonagem Molecular/métodos
Expressão Gênica
Imunoglobulinas/genética
Imunoglobulinas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bombyx/genética
Bombyx/metabolismo
Linhagem Celular
Regulação da Expressão Gênica no Desenvolvimento
Imunoglobulinas/química
Proteínas de Insetos/química
Proteínas de Insetos/genética
Proteínas de Insetos/metabolismo
Filogenia
Domínios Proteicos
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulins); 0 (Insect Proteins); 0 (Protein Isoforms)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE



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