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I don’t know how you configured, but for me VLC has a nice GUI which allows me to add a stream to list.

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Fast RING proteins bind E2 ubiquitin-conjugating enzymes in a RING-dependent manner.
Ubiquitination is a reversible process mediated by the transfer of Ub (ubiquitin) from E2 enzymes to substrate proteins. Besides RING E3 ligases that catalyze the formation of a thioester-linked ubiquitin adduct, RING E2 enzymes also have a mechanism for direct ubiquitin transfer. However, the structural basis for such a mechanism remains unclear, although it was shown in previous studies that a RING E2 enzyme can transfer a Ub moiety to a bound Ub-like domain (UBL) or Sse2 domain of an E3 ligase. Using a photocrosslinking approach, we identified E2-bound regions in RING E2 enzymes. We found that a conserved loop region of the catalytic domain is primarily responsible for the interaction with a Ub-conjugating enzyme, which is in agreement with a RING-dependent ubiquitination. The presence of this conserved loop is a common feature of all RING E2s, although it is missing in the majority of E3-type RING E2s.Trimeric and decameric Cd2+-exchange mediated by a phenolate-based ligand.
A phenolate-based ligand having three CdII tridentate binding sites was designed and synthesized. The solid state structures of two CdII complexes of this ligand have been determined by single crystal X-ray crystallography. The CdII tridentate coordination shows a unique Cd2+-exchange motif involving phenolates and carboxylate oxygens with the inter
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