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Mine3leo

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1
Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
1
Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
1
Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
1
The mouse tiling array (2006-07-17MM8 tiling_set38), which covers the second half of the X chromosome (ChrX:93,883,966- 165,556,020, UCSC mouse genome Feb 2006 assembly) and the complete Y chromosome, was used in this study to closely compare the H4K16 acetylation pattern between Jarid1c and Jarid1d present on the same array. Analysis was done using the manufacturer software.Supporting Information
1
The mouse tiling array (2006-07-17MM8 tiling_set38), which covers the second half of the X chromosome (ChrX:93,883,966- 165,556,020, UCSC mouse genome Feb 2006 assembly) and the complete Y chromosome, was used in this study to closely compare the H4K16 acetylation pattern between Jarid1c and Jarid1d present on the same array. Analysis was done using the manufacturer software.Supporting Information
1
Tion via a thiolester linkage to an internal cysteine in E1, which then transfers the ubiquitin to a cysteine residue of an E2 protein. The E2 interacts with an E3 to mediate covalent attachment of ubiquitin onto substrate proteins. Repeated rounds of E2/E3mediated ubiquitin transfer result in polyubiquitylation, allowing substrate proteins to be recognized and destroyed by the proteasome. Vertebr
1
Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
1
Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure