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[PMID]:29429181
[Au] Autor:Chen T; Zhang W; Liang Y; Li Q; Yang C; Yuan YX; Ban ML
[Ad] Endereço:Department of Otorhinolaryngology, Nanfang Hospital, Southern Medical University, Guangzhou 510515, China.
[Ti] Título:[Effect of melatonin on expression of Prestin protein in the inner ear of mice following radiotherapy].
[So] Source:Zhonghua Er Bi Yan Hou Tou Jing Wai Ke Za Zhi;53(2):118-123, 2018 Feb 07.
[Is] ISSN:1673-0860
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To investigate the effect of melatonin on the expression of prestin protein in the inner ear of mice following a single dose radiation therapy, so as to provide the basis for the mechanism study of radiation induced inner ear injury and its prevention. Sixty 4-week-old male mice were randomly divided into six groups, including the control group (A group), 50 mg/kg MLT group (B group), 5 mg/kg MLT group (C group), 50 mg/kg MLT + radiotherapy group (D group), 5 mg/kg MLT+ radiotherapy group (E group), and 16 Gy radiotherapy group (F group). Each experimental group was randomly subdivided into two subgroups, which were killed to harvest the cochlea on the 3rd and 7th days following 16 Gy radiation. The specimens were used for immunostaining and Western blot to detect the expression of prestin protein. SPSS 19.0 software was used for statistical analysis. Prestin protein mainly distributed in the lateral membrane above the outer hair cell nucleus. When compared with A, B and C group, the expression of prestin protein in the inner ear was significantly up-regulated in F group ( <0.05). However, D and E group reduced the abnormal expression of prestin following radiotherapy when compared with F group, the difference was statistically significant ( <0.05), and the effect of D group was more significant than E group ( <0.05). The prestin protein of cochlea is mainly distributed in the lateral membrane above the outer hair cell nucleus. Following the high-dose radiotherapy, the prestin expression is upregulated, and melatonin can control the abnormal expression of prestin protein induced by radiotherapy with dose dependent.
[Mh] Termos MeSH primário: Orelha Interna/metabolismo
Orelha Interna/efeitos da radiação
Células Ciliadas Auditivas Externas/metabolismo
Melatonina/farmacologia
Proteínas Motores Moleculares/metabolismo
[Mh] Termos MeSH secundário: Animais
Cóclea/efeitos dos fármacos
Cóclea/efeitos da radiação
Células Ciliadas Auditivas Externas/efeitos dos fármacos
Células Ciliadas Auditivas Externas/efeitos da radiação
Masculino
Camundongos
Distribuição Aleatória
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Molecular Motor Proteins); 0 (Pres protein, mouse); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180213
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1673-0860.2018.02.007


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[PMID]:29197577
[Au] Autor:Liew CW; Hynson RM; Ganuelas LA; Shah-Mohammadi N; Duff AP; Kojima S; Homma M; Lee LK
[Ad] Endereço:School of Medical Sciences, The University of New South Wales, Australia.
[Ti] Título:Solution structure analysis of the periplasmic region of bacterial flagellar motor stators by small angle X-ray scattering.
[So] Source:Biochem Biophys Res Commun;495(2):1614-1619, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bacterial flagellar motor drives the rotation of helical flagellar filaments to propel bacteria through viscous media. It consists of a dynamic population of mechanosensitive stators that are embedded in the inner membrane and activate in response to external load. This entails assembly around the rotor, anchoring to the peptidoglycan layer to counteract torque from the rotor and opening of a cation channel to facilitate an influx of cations, which is converted into mechanical rotation. Stator complexes are comprised of four copies of an integral membrane A subunit and two copies of a B subunit. Each B subunit includes a C-terminal OmpA-like peptidoglycan-binding (PGB) domain. This is thought to be linked to a single N-terminal transmembrane helix by a long unstructured peptide, which allows the PGB domain to bind to the peptidoglycan layer during stator anchoring. The high-resolution crystal structures of flagellar motor PGB domains from Salmonella enterica (MotB ) and Vibrio alginolyticus (PomB ) have previously been elucidated. Here, we use small-angle X-ray scattering (SAXS). We show that unlike MotB , the dimeric conformation of the PomB in solution differs to its crystal structure, and explore the functional relevance by characterising gain-of-function mutants as well as wild-type constructs of various lengths. These provide new insight into the conformational diversity of flagellar motor PGB domains and experimental verification of their overall topology.
[Mh] Termos MeSH primário: Proteínas da Membrana Bacteriana Externa/química
Proteínas de Bactérias/química
Flagelos/química
Proteínas Motores Moleculares/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas da Membrana Bacteriana Externa/genética
Proteínas de Bactérias/genética
Modelos Moleculares
Proteínas Motores Moleculares/genética
Domínios Proteicos
Estrutura Quaternária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Salmonella enterica/química
Salmonella enterica/genética
Espalhamento a Baixo Ângulo
Homologia de Sequência de Aminoácidos
Soluções
Vibrio alginolyticus/química
Vibrio alginolyticus/genética
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (Molecular Motor Proteins); 0 (MotB protein, Bacteria); 0 (PomB protein, bacteria); 0 (Recombinant Proteins); 0 (Solutions)
[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:171204
[St] Status:MEDLINE


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[PMID]:29294326
[Au] Autor:Kinoshita M; Furukawa Y; Uchiyama S; Imada K; Namba K; Minamino T
[Ad] Endereço:Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadoaka, Suita, Osaka 565-0871, Japan.
[Ti] Título:Insight into adaptive remodeling of the rotor ring complex of the bacterial flagellar motor.
[So] Source:Biochem Biophys Res Commun;496(1):12-17, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bacterial flagellar motor rotates in both counterclockwise (CCW) and clockwise (CW) directions. FliG, FliM and FliN form the C ring on the cytoplasmic face of the MS ring made of a transmembrane protein, FliF. The C ring acts not only as a rotor but also as a switch of the direction of motor rotation. FliG consists of three domains: FliG , FliG and FliG . FliG directly binds to FliF. Intermolecular interactions between FliG and FliG drive FliG ring formation. FliG is responsible for the interaction with FliM. FliG is involved in the interaction with the stator protein MotA. Adaptive remodeling of the C ring occurs when the motor switches between the CCW and CW states. However, it remained unknown how. Here, we report the effects of a CW-locked deletion mutation (ΔPEV) in FliG of Thermotaoga maritia (Tm-FliG) on FliG-FliG and FliG-FliM interactions. The PEV deletion stabilized the intramolecular interaction between FliG and FliG , thereby suppressing the oligomerization of Tm-FliG in solution. This deletion also induced a conformational change of Helix connecting FliG and FliG to reduce the binding affinity of Tm-FliG for FliM. We will discuss adaptive remodeling of the C ring responsible for flagellar motor switching.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Flagelos/química
Proteínas Motores Moleculares/química
Movimento (Física)
[Mh] Termos MeSH secundário: Proteínas de Bactérias/ultraestrutura
Sítios de Ligação
Proteínas Motores Moleculares/ultraestrutura
Ligação Proteica
Conformação Proteica
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (FliN protein, Bacteria); 0 (Molecular Motor Proteins); 134548-59-7 (FliM protein, Bacteria)
[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:180103
[St] Status:MEDLINE


  4 / 3870 MEDLINE  
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[PMID]:29248727
[Au] Autor:Rula S; Suwa T; Kijima ST; Haraguchi T; Wakatsuki S; Sato N; Duan Z; Tominaga M; Uyeda TQP; Ito K
[Ad] Endereço:Department of Biology, Graduate School of Science, Chiba University, Inage-ku, Chiba 263-8522, Japan.
[Ti] Título:Measurement of enzymatic and motile activities of Arabidopsis myosins by using Arabidopsis actins.
[So] Source:Biochem Biophys Res Commun;495(3):2145-2151, 2018 01 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There are two classes of myosin, XI and VIII, in higher plants. Myosin XI moves actin filaments at high speed and its enzyme activity is also very high. In contrast, myosin VIII moves actin filaments very slowly with very low enzyme activity. Because most of these enzymatic and motile activities were measured using animal skeletal muscle α-actin, but not plant actin, they would not accurately reflect the actual activities in plant cells. We thus measured enzymatic and motile activities of the motor domains of two Arabidopsis myosin XI isoforms (MYA2, XI-B), and one Arabidopsis myosin VIII isoform (ATM1), by using three Arabidopsis actin isoforms (ACT1, ACT2, and ACT7). The measured activities were different from those measured by using muscle actin. Moreover, Arabidopsis myosins showed different enzymatic and motile activities when using different Arabidopsis actin isoforms. Our results suggest that plant actin should be used for measuring enzymatic and motile activities of plant myosins and that different actin isoforms in plant cells might function as different tracks along which affinities and velocities of each myosin isoform are modulated.
[Mh] Termos MeSH primário: Actinas/química
Proteínas de Arabidopsis/química
Proteínas Motores Moleculares/química
Movimento (Física)
Miosinas/química
[Mh] Termos MeSH secundário: Actinas/ultraestrutura
Proteínas de Arabidopsis/ultraestrutura
Ativação Enzimática
Proteínas Motores Moleculares/ultraestrutura
Miosinas/ultraestrutura
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Arabidopsis Proteins); 0 (Molecular Motor Proteins); EC 3.6.4.1 (Myosins)
[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:171218
[St] Status:MEDLINE


  5 / 3870 MEDLINE  
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[PMID]:29229393
[Au] Autor:Sakai T; Inoue Y; Terahara N; Namba K; Minamino T
[Ad] Endereço:Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadoaka, Suita, Osaka 565-0871, Japan.
[Ti] Título:A triangular loop of domain D1 of FlgE is essential for hook assembly but not for the mechanical function.
[So] Source:Biochem Biophys Res Commun;495(2):1789-1794, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bacterial flagellar hook is a short, curved tubular structure made of FlgE. The hook connects the basal body as a rotary motor and the filament as a helical propeller and functions as a universal joint to smoothly transmit torque produced by the motor to the filament. Salmonella FlgE consists of D0, Dc, D1 and D2 domains. Axial interactions between a triangular loop of domain D1 (D1-loop) and domain D2 are postulated to be responsible for hook supercoiling. In contrast, Bacillus FlgE lacks the D1-loop and domain D2. Here, to clarify the roles of the D1-loop and domain D2 in the mechanical function, we carried out deletion analysis of Salmonella FlgE. A deletion of the D1-loop conferred a loss-of-function phenotype whereas that of domain D2 did not. The D1-loop deletion inhibited hook polymerization. Suppressor mutations of the D1-loop deletion was located within FlgD, which acts as the hook cap to promote hook assembly. This suggests a possible interaction between the D1-loop of FlgE and FlgD. Suppressor mutant cells produced straight hooks, but retained the ability to form a flagellar bundle behind a cell body, suggesting that the loop deletion does not affect the bending flexibility of the Salmonella hook.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Flagelos/química
Flagelos/fisiologia
Flagelos/ultraestrutura
Genes Bacterianos
Modelos Moleculares
Proteínas Motores Moleculares/química
Proteínas Motores Moleculares/genética
Proteínas Motores Moleculares/metabolismo
Mutação
Domínios Proteicos
Multimerização Proteica
Salmonella/genética
Salmonella/fisiologia
Deleção de Sequência
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (FlgE protein, Bacteria); 0 (Molecular Motor Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE


  6 / 3870 MEDLINE  
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[PMID]:29253848
[Au] Autor:McFadden WM; McCall PM; Gardel ML; Munro EM
[Ad] Endereço:Biophysical Sciences Program, University of Chicago, Chicago, Illinois, United States of America.
[Ti] Título:Filament turnover tunes both force generation and dissipation to control long-range flows in a model actomyosin cortex.
[So] Source:PLoS Comput Biol;13(12):e1005811, 2017 12.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Actomyosin-based cortical flow is a fundamental engine for cellular morphogenesis. Cortical flows are generated by cross-linked networks of actin filaments and myosin motors, in which active stress produced by motor activity is opposed by passive resistance to network deformation. Continuous flow requires local remodeling through crosslink unbinding and and/or filament disassembly. But how local remodeling tunes stress production and dissipation, and how this in turn shapes long range flow, remains poorly understood. Here, we study a computational model for a cross-linked network with active motors based on minimal requirements for production and dissipation of contractile stress: Asymmetric filament compliance, spatial heterogeneity of motor activity, reversible cross-links and filament turnover. We characterize how the production and dissipation of network stress depend, individually, on cross-link dynamics and filament turnover, and how these dependencies combine to determine overall rates of cortical flow. Our analysis predicts that filament turnover is required to maintain active stress against external resistance and steady state flow in response to external stress. Steady state stress increases with filament lifetime up to a characteristic time τm, then decreases with lifetime above τm. Effective viscosity increases with filament lifetime up to a characteristic time τc, and then becomes independent of filament lifetime and sharply dependent on crosslink dynamics. These individual dependencies of active stress and effective viscosity define multiple regimes of steady state flow. In particular our model predicts that when filament lifetimes are shorter than both τc and τm, the dependencies of effective viscosity and steady state stress on filament turnover cancel one another, such that flow speed is insensitive to filament turnover, and shows a simple dependence on motor activity and crosslink dynamics. These results provide a framework for understanding how animal cells tune cortical flow through local control of network remodeling.
[Mh] Termos MeSH primário: Actomiosina/fisiologia
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/química
Citoesqueleto de Actina/fisiologia
Actomiosina/química
Animais
Fenômenos Biomecânicos
Biologia Computacional
Simulação por Computador
Citoesqueleto/fisiologia
Modelos Biológicos
Proteínas Motores Moleculares/química
Proteínas Motores Moleculares/fisiologia
Morfogênese
Reologia
Estresse Fisiológico
Viscosidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Molecular Motor Proteins); 9013-26-7 (Actomyosin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005811


  7 / 3870 MEDLINE  
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[PMID]:28460181
[Au] Autor:Jung GS; Buehler MJ
[Ad] Endereço:Laboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139; email: mbuehler@MIT.edu.
[Ti] Título:Multiscale Modeling of Muscular-Skeletal Systems.
[So] Source:Annu Rev Biomed Eng;19:435-457, 2017 Jun 21.
[Is] ISSN:1545-4274
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Multiscale modeling of muscular-skeletal systems-the materials and structures that help organisms support themselves and move-is a rapidly growing field of study that has contributed key elements to the understanding of these systems, especially from a multiscale perspective. The systems, including materials such as bone and muscle, have hierarchical structures ranging from the nano- to the macroscale, and it is difficult to understand their macroscopic behaviors, both physiological and pathological, without knowledge of their hierarchical structures and properties. In this review, we discuss the methods of multiscale modeling. Through a series of case studies about key materials in muscular-skeletal systems, we describe how different methods can bridge the gap between hierarchical structures and their roles in the systems' mechanical properties. In particular, we emphasize the importance of the quality of minerals in bone. Finally, we discuss biomimetic material designs facilitated by additive manufacturing technology.
[Mh] Termos MeSH primário: Osso e Ossos/fisiologia
Articulações/fisiologia
Modelos Biológicos
Proteínas Motores Moleculares/fisiologia
Contração Muscular/fisiologia
Músculo Esquelético/fisiologia
[Mh] Termos MeSH secundário: Animais
Simulação por Computador
Seres Humanos
Estresse Mecânico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Molecular Motor Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-bioeng-071516-044555


  8 / 3870 MEDLINE  
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[PMID]:29240771
[Au] Autor:Wang X; Carlsson AE
[Ad] Endereço:Department of Bioinformatics, UT Southwestern Medical Center, Dallas, Texas, United States of America.
[Ti] Título:A master equation approach to actin polymerization applied to endocytosis in yeast.
[So] Source:PLoS Comput Biol;13(12):e1005901, 2017 12.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We present a Master Equation approach to calculating polymerization dynamics and force generation by branched actin networks at membranes. The method treats the time evolution of the F-actin distribution in three dimensions, with branching included as a directional spreading term. It is validated by comparison with stochastic simulations of force generation by actin polymerization at obstacles coated with actin "nucleation promoting factors" (NPFs). The method is then used to treat the dynamics of actin polymerization and force generation during endocytosis in yeast, using a model in which NPFs form a ring around the endocytic site, centered by a spot of molecules attaching the actin network strongly to the membrane. We find that a spontaneous actin filament nucleation mechanism is required for adequate forces to drive the process, that partial inhibition of branching and polymerization lead to different characteristic responses, and that a limited range of polymerization-rate values provide effective invagination and obtain correct predictions for the effects of mutations in the active regions of the NPFs.
[Mh] Termos MeSH primário: Actinas/metabolismo
Endocitose/fisiologia
Modelos Biológicos
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Actinas/química
Fenômenos Biomecânicos
Membrana Celular/metabolismo
Biologia Computacional
Simulação por Computador
Proteínas Motores Moleculares/química
Proteínas Motores Moleculares/metabolismo
Mutação
Polimerização
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Molecular Motor Proteins); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180123
[Lr] Data última revisão:
180123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005901


  9 / 3870 MEDLINE  
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[PMID]:29200148
[Au] Autor:Aoki T; Kunishima S; Yamashita Y; Minamitani K; Ota S
[Ad] Endereço:Department of Pediatrics, Teikyo University Chiba Medical Center, Chiba.
[Ti] Título:Macrothrombocytopenia With Congenital Bilateral Cataracts: A Phenotype of MYH9 Disorder With Exon 24 Indel Mutations.
[So] Source:J Pediatr Hematol Oncol;40(1):76-78, 2018 Jan.
[Is] ISSN:1536-3678
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:MYH9 disorder is characterized by large platelets and granulocyte inclusion bodies, and can be complicated with young-adult onsets of nephropathy, sensorineural hearing loss, and cataracts. Congenital cataracts in patients with MYH9 disorder is rare, and their etiology has not been elucidated. We report a 3-year-old patient with MYH9 disorder who had a p.E1066_A1072del mutation and developed cataracts congenitally. A review of the literature reveals that patients with an MYH9 exon 24 indel mutation, including p.E1066_A1072del, are susceptible to developing congenital cataracts and should be followed closely for other nonhematological complications.
[Mh] Termos MeSH primário: Catarata/congênito
Granulócitos/ultraestrutura
Mutação INDEL
Proteínas Motores Moleculares/genética
Cadeias Pesadas de Miosina/genética
Trombocitopenia/complicações
[Mh] Termos MeSH secundário: Plaquetas/patologia
Catarata/genética
Pré-Escolar
Éxons
Granulócitos/patologia
Perda Auditiva Neurossensorial
Seres Humanos
Corpos de Inclusão/patologia
Fenótipo
Trombocitopenia/congênito
Trombocitopenia/etiologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MYH9 protein, human); 0 (Molecular Motor Proteins); EC 3.6.4.1 (Myosin Heavy Chains)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1097/MPH.0000000000000998


  10 / 3870 MEDLINE  
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[PMID]:29183938
[Au] Autor:Heer NC; Martin AC
[Ad] Endereço:Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
[Ti] Título:Tension, contraction and tissue morphogenesis.
[So] Source:Development;144(23):4249-4260, 2017 Dec 01.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:D'Arcy Thompson was a proponent of applying mathematical and physical principles to biological systems, an approach that is becoming increasingly common in developmental biology. Indeed, the recent integration of quantitative experimental data, force measurements and mathematical modeling has changed our understanding of morphogenesis - the shaping of an organism during development. Emerging evidence suggests that the subcellular organization of contractile cytoskeletal networks plays a key role in force generation, while on the tissue level the spatial organization of forces determines the morphogenetic output. Inspired by D'Arcy Thompson's , we review our current understanding of how biological forms are created and maintained by the generation and organization of contractile forces at the cell and tissue levels. We focus on recent advances in our understanding of how cells actively sculpt tissues and how forces are involved in specific morphogenetic processes.
[Mh] Termos MeSH primário: Morfogênese/fisiologia
[Mh] Termos MeSH secundário: Actinas/fisiologia
Animais
Fenômenos Biomecânicos
Movimento Celular/fisiologia
Células Epiteliais/fisiologia
Seres Humanos
Junções Intercelulares/fisiologia
Modelos Biológicos
Proteínas Motores Moleculares/fisiologia
Contração Muscular/fisiologia
Miosinas/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Actins); 0 (Molecular Motor Proteins); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1242/dev.151282



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