Voc resolveu este problema? Pois estou na mesma condio. Com o Linker Manager consegui ativar o SAT. Mas quando a aplicao tentar acess-lo - vem a mensagem que o SAT no est ativo. A minha aplicao no usa o ACBr.
Usando o emulador da SEFAZ - tudo correto. A aplicao gerava os arquivos necessrios e os colocava na pasta C:\SAT\COMANDOS. O emulador interpretava os arquivos, criava os arquivos de retorno e os colocava na mesma pasta. A aplicao ficava esperando o retorno, assim que chegava, processava e dava o destino correto aos dados.
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Boa Tarde, por favor algum poderia me socorrer, estou com o mesmo problema da Renata, meu aplicativo envia o comando para o Sat e aparentemente o aplicativo trava, depois de algum tempo ele retorna como esta abaixo:
Bom dia, estou com um problema, como explicado acima, no consigo fazer minha aplicao acessar o LINK SAT da Elgin, j coloquei a Zlib junto com o executavel, nas pastas do Windows, System, System32, tentei fazer um teste com o aplicativo ACBrSatTeste da pasta exemplo e esta acontecendo a mesma mensagem, o aplicativo congela por um tempo e depois retorna conforme postado acima. Realmente j utilizei tudo o que consegui encontrar no forum e nada resolveu. No sei o que pode estar acontecendo. se algum puder me ajudar.
Para Funcionar , use o driver que o windows instala por default, que ja vem assinado, ou vai ter que desabilitar a imposicao de verificacao de assinatura de driver pelo windows..., pois o driver da elgin nao vem assinado....
Depois de muito tempo descobri que quando est com windows 64 tanto no Lazarus quanto no Delphi Seattle quando mandava a venda para o Sat apresentava este erro .Access violation at address 60854438 in module 'DLLSAT.DLL'.
Amigos, estou tento o mesmo problema com o Exemplo da ACBr. Com o emulador da sefaz tudo acontece belezinha, at imprimi. Porem com o SAT da Elgin no vai. Estava funcionando normal. Precisei formatar meu computador. Formatei mais de 2 vezes j. Essa ultima vez deixei apenas o windows 10 32bts, delphi com acbr, fortes e fast report e mais nada.... Instalao mais limpa do que isso impossivel.... O linker Manager comunica normal sem erros !!! Digam as informaes que precisam que eu passo.... Alguem poderia me dar uma dica ?
@Srgio Assuno Usei a dll sim, porm no resolveu tambm. O que resolveu por incrvel que parea foi mesmo colocar a dll zlib.dll na pasta do exemplo do ACBrSAT e funcionou de boa. Essa dll (zlib.dll fica na pasta do linker Manager). Interessante que j tinha feito isso e no tinha funcionado; ms provavelmente fiz algo errado da outra vez que no deu certo. Resumindo.... Formatei meu note novamente (Windows 10 64bits), delphi zerado (Fortes,Fast,ACBr),Linker Manager com a dll que vem com a instalao normal. Agradeo @Srgio Assuno de corao pela ajuda que foi de enorme valia e a todos da comunidade ACBr. Deus queira que essa crise passe pois quero ser um dos que colaboram tambm financeiramente com esse projeto que no pode acabar....
Entao sergio na verdade ele nem citava no viu .... Dava o erro mesmo e ficava naquilo de access violation... Ele registrava no log o access violation mas nao registrava a falta da zlib. Depois que eu coloquei aquela dll que vc me passou de 09.08 se nao me angano que ele mostrou falta da zlib.... Ai eu formatei meu note novamente (Pela quinta vez rsrsrs), Delphi puro com Fortes,Fast e acbr e o detalhe que coloquei a zlib da pasta do linker manager na pasta do executavel do exemplo e eeee... Magicaaaaa rsrs.... Funcionou. Que fique registrado ai para os que tiverem o mesmo problema.... Abraos a todos ...
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The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, including maintenance of nuclear shape and stability, mediation of nuclear mechanoresponses, and nucleo-cytoskeletal coupling. Herein, we investigate how disease-causing mutant lamins alter myonuclear properties in response to mechanical force. This was accomplished via a novel application of a micropipette harpooning assay applied to larval body wall muscles of Drosophila models of lamin-associated muscular dystrophy. The assay enables the measurement of both nuclear deformability and intracellular force transmission between the cytoskeleton and nuclear interior in intact muscle fibers. Our studies revealed that specific mutant lamins increase nuclear deformability while other mutant lamins cause nucleo-cytoskeletal coupling defects, which were associated with loss of microtubular nuclear caging. We found that microtubule caging of the nucleus depended on Msp300, a KASH domain protein that is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Taken together, these findings identified residues in lamins required for connecting the nucleus to the cytoskeleton and suggest that not all muscle disease-causing mutant lamins produce similar defects in subcellular mechanics.
The goal of this study was to determine the effects of specific mutant lamins on the nuclear shape and nucleo-cytoskeletal coupling in muscle. To achieve this goal, we generated Drosophila models of LMNA muscular dystrophy possessing either wild-type or mutant Lamin C (LamC) transgenes. The LamC transgenic lines have similar genetic backgrounds, with the exception of the site of insertion of the P-element. LamC is an orthologue of human LMNA and the only A-type lamin encoded by the Drosophila genome. The Drosophila LamC protein shares a domain structure that includes 35% amino acid identity and 54% similarity with human lamin A/C. Like human LMNA, the expression of endogenous LamC is initiated upon cellular differentiation (Riemer et al., 1995). The transcriptional regulators that drive muscle cell differentiation are similar between Drosophila and humans (Tapscott et al., 1988; Maire et al., 2020). In both species, differentiated myoblasts fuse to form multinucleated muscle fibers that attach to tendon cells (Ovalle, 1987; Krimm et al., 2002; Schulman et al., 2015; Lemke & Schnorrer, 2018; Richier et al., 2018; Balakrishnan et al., 2021). Thus, much of muscle development and physiology is shared between the two species. Herein, we use the Drosophila larval body wall muscles as a proxy for human skeletal muscles. Larval body wall muscles are represented by over 300 individual muscle fibers that can easily be prepared as a muscle fillet (Ramachandran & Budnik, 2010). The use of larval body wall muscles allows for whole organism muscle function assays, cytological analyses, and fillets for in situ microharpooning assays to measure nuclear-cytoskeletal coupling and nuclear deformability.
Muscle-specific expression of mutant lamins in an otherwise wild-type Drosophila background caused dominant effects on muscle physiology and/or function. These Drosophila models of lamin-associated muscle disease revealed vast differences among the mutant lamins tested. Specific mutant lamins altered nuclear shape and succumbed to nuclear envelope deformation under force application. By contrast, other mutant lamins partially uncoupled the nucleus from the cytoskeleton. Interestingly, the domain of lamin affected did not correlate with the loss of a particular nuclear defect, suggesting a complex structure/function relationship, potentially involving additional binding partners. Muscles expressing mutant lamins that caused uncoupling of the nucleus from the cytoskeleton showed a lack of microtubule nuclear caging. A lack of microtubule caging was also observed upon RNAi knockdown of Msp300, a Drosophila KASH domain protein. Taken together, these data suggest that specific residues within lamin alter nucleo-cytoskeletal coupling that is supported by Msp300. Furthermore, mutation-specific cellular defects suggest that different pathological mechanisms might lead to the common muscle atrophy associated with LMNA skeletal muscle disease.
Drosophila stocks were cultured in cornmeal/sucrose media at 25C (Shaffer et al., 1994). To generate the Lamin C (LamC) transgenic lines, full length LamC (Gold Clone, accession number AY095046, Berkeley Drosophila Genome Project, available from the Drosophila Genomics Resource Center, Bloomington, IN) was cloned into the pUAST P-element transformation vector (Brand & Perrimon, 1993). This vector contains a minimal promoter downstream of five upstream activating sequences (UAS) that bind the yeast Gal4 transcriptional activator. Standard embryo injection procedures were used to generate the transgenic stocks in which the P-element was relatively randomly inserted within the genome (BestGene, Chino Hills). Eight to ten independent transgenic lines were established for each LamC construct. The site of insertion was mapped to a specific chromosome, and the transgenes were made homozygous. Insertions that were not homozygous viable were discarded. Western analysis was performed, and transgenes that expressed levels of LamC relative to that of the endogenous LamC gene were used for analysis. Muscle-specific expression was achieved by crossing the transgenic lines to the C57 Gal4 driver stock that expresses the yeast Gal4 specifically in larval body wall muscles (Brand and Perrimon, 1993; Gorczyca et al., 2007). The resulting progeny express either wild-type or mutant LamC in their larval body wall muscles. 152ee80cbc
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