User:Hsavino2016/SWI/SNF

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The human analogs of SWI/SNF are BAF (SWI/SNF-A) and PBAF (SWI/SNF-B). BAF in turn stands for "BRG1- or BRM-associated factors", and PBAF is for "polybromo-associated BAF".

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The human analogs of SWI/SNF are BAF (SWI/SNF-A) and PBAF (SWI/SNF-B). BAF stands for "BRG1- or BRM-associated factors", while PBAF stands for "Polybromo-associated BAF". There are also Drosophila analogs of SWI/SNF, known as BAP and PBAP. BAP stands for "Brahma Associated Protein" and PBAP stands for "Polybromo-associated BAP"

Combine the sentences and shorten them up; rearrange the order (write the words first, them the abbreviation) same thing for

Drosophila needs italicized

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Below is a list of yeast SWI/SNF family members and human orthologs: Revised:

Below is a list of yeast SWI/SNF family members with human and Drosophila orthologs

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The mammalian SWI/SNF (mSWI/SNF) complex functions as a tumor suppressor in many human malignancies. Early studies identified that SWI/SNF subunits were frequently absent in cancer cell lines. It was first identified in 1998 as a tumor suppressor in rhabdoid tumors, a rare pediatric malignancy. As DNA sequencing costs diminished, many tumors were sequenced for the first time around 2010. Several of these studies revealed SWI/SNF to be a tumor suppressor in a number of diverse malignancies. Several studies revealed that subunits of the mammalian complex, including ARID1A, PBRM1, SMARCB1,SMARCA4, and ARID2, are frequently mutated in human cancers. A meta-analysis of many sequencing studies demonstrated SWI/SNF to be mutated in approximately 20% of human malignancies.

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Change the heading to something like "SWI/SNF acts as a tumor supressor"

The mammalian SWI/SNF (mSWI/SNF) complex functions as a tumor suppressor in many human malignant cancers. Early studies identified that SWI/SNF subunits were frequently absent in cancer cell lines. SWI/SNF was first identified in 1998 as a tumor suppressor in rhabdoid tumors, a rare pediatric malignant cancer. Other instances of SWI/SNF acting as a tumor suppressor comes from the heterozygous deletion of BAF47 or alteration of BAF47. These cases result in cases of chronic and acute CML and in rarer cases, Hodgkin's lymphoma, respectively. To prove that BAF47, also known as SMARCB1, acts a tumor suppressor, experiments resulting in the formation of rhabdoid tumors in mice were conducted via total knockout of BAF47 (dont use primary research for the wiki; keep it vague i guess?). As DNA sequencing costs diminished, many tumors were sequenced for the first time around 2010(probably dont need this sentence). Several of these studies revealed SWI/SNF to be a tumor suppressor in a number of diverse malignancies. Several studies revealed that subunits of the mammalian complex, including ARID1A, PBRM1, SMARCB1,SMARCA4, and ARID2, are frequently mutated in human cancers. It has been noted that total loss of BAF47 is extremely rare and instead, most cases of tumors that resulted from SWI/SNF subunits come from BRG1 deletion, BRM deletion, or total loss of both subunits. Further analysis concluded that total loss of both sub-units was present in about 10% of tumor cell lines after 100 cell lines were looked at. A meta-analysis of many sequencing studies demonstrated SWI/SNF to be mutated in approximately 20% of human malignancies. Too much fluff? Revised from article:

In molecular biology, SWI/SNF (SWItch/Sucrose Non-Fermentable), is a subfamiliy of ATP-Dependent chromatin remodeling complexes, which is found in eukaryotes. In other words, it is a group of proteins that associate to remodel the way DNA is packaged. This complex is composed of several proteins, products of the SWI and SNF genes, (, /,, , ) and other polypeptides. It possesses a DNA-stimulated ATPase activity that can destabilize histone-DNA interactions in reconstituted nucleosomes in an ATP-dependent manner, though the exact nature of this structural change is unknown. The SWI/SNF subfamily provides crucial nucleosome rearrangement, which is seen as ejection and/or sliding. The movement of nucleosomes provides easier access to the chromatin, allowing genes to be activated or repressed.

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Electron microscopy studies of SWI/SNF and RSC (SWI/SNF-B) reveal large, lobed 1.1-1.3 MDa structures. No atomic-resolution structures of the entire SWI/SNF complex have been obtained to date, due to the protein complex being highly dynamic and composed of many subunits. However, domains and several individual subunits from yeast and mammals have been described. In particular, the cryo-EM structure of the ATPase Snf2 in complex with a nucleosome shows that nucleosomal DNA is locally deformed at the site of binding. A model of the mammalian ATPase SMARCA4 shows similar features, based on the high degree of sequence homology with yeast Snf2. The interface between two subunits, BAF155 (SMARCC1) and BAF47 (SMARCB1) was also resolved, providing important insights into the mechanisms of the SWI/SNF complex assembly pathway.

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Electron microscopy studies of SWI/SNF and RSC (SWI/SNF-B) reveal large, lobed 1.1-1.3 MDa structures. These structures resemble RecA and cover both sides of a conserved section of the ATPase domain. The domain also contains a separate domain, HSA, that is capable of binding actin, and resides on the N-terminus. No atomic-resolution structures of the entire SWI/SNF complex have been obtained to date, due to the protein complex being highly dynamic and composed of many subunits. However, domains and several individual subunits from yeast and mammals have been described. In particular, the cryo-EM structure of the ATPase Snf2 in complex with a nucleosome shows that nucleosomal DNA is locally deformed at the site of binding. A model of the mammalian ATPase SMARCA4 shows similar features, based on the high degree of sequence homology with yeast Snf2. The interface between two subunits, BAF155 (SMARCC1) and BAF47 (SMARCB1) was also resolved, providing important insights into the mechanisms of the SWI/SNF complex assembly pathway.