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silencing of PMEL suppressed melanization through activating lysosomes and degradation of tyrosinase by lysosomes.
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To provide a source of dual-specific T cells for ACT, we generated a transgenic mouse strain expressing a CAR specific for Her2 in leukocytes under the control of the vav promoter .This CAR mouse strain was bred onto the pMEL transgenic mouse strain, expressing a TCR specific for the premelanosome protein, gp100
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IMCgp100 (ImmTAC recognizing a peptide derived from the melanoma-specific protein, gp100, presented by HLA-A*0201) efficiently redirects and activates effector and memory cells from both CD8(+) and CD4(+) repertoires to kill melanoma cells.
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our work attempts to provide structural insights into the RPT domain structure and to elucidate its contribution to Pmel17 amyloid fibril formation.
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These findings help to clarify the mechanism of T-cell recognition of gp100 during melanoma responses and could direct the development of altered peptides for vaccination.
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Data suggest that the Kringle-like domain of PMEL facilitates post-endoplasmic reticulum processing of disulfide-bonded PMEL dimers and promotes formation of PMEL functional amyloid fibrillar structures within multivesicular endosomes.
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mutant N-terminally extended peptides exhibited significantly increased HLA-A*02:01 binding affinity and elicited CD8(+) T cell stimulation in vitro similar to the wtgp100209-217 epitope.
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Data indicate that repeat domain (RPT) derived from Pmel17 aggregation kinetics were influenced only by lysolipid-containing phospholipid vesicles.
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Melanosome-autonomous regulation of size and number: the OA1 receptor sustains PMEL expression.
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SIL-TAL1 rearrangement identifies a distinct subtype with inferior outcome which could allow for individual therapeutic stratification for T-ALL patients.
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the molecular basis for the distinct trafficking and morphogenetic properties of PMEL and GPNMB is the PKD domain
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Data indicat that the N-terminal region of PMEL/Pmel17 is essential for the formation of melanosomal fibrils.
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BACE2 cleaves the integral membrane form of PMEL within the juxtamembrane domain, releasing the PMEL luminal domain into endosomal precursors for the formation of amyloid fibrils and downstream melanosome morphogenesis.
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The recombinant Pmel 17 plasmids were right as we expected by DNA sequencing
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The most significant single-nucleotide polymorphism in the 12q13.2 locus is located immediately upstream of the promoter region of PMEL for vitiligo in Han Chinese.
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An antibody drug conjugate reactive with PMEL17 exhibits target-dependent tumor cell killing in vitro and in vivo.
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This is a review on two human amyloidogenic polypeptides, one associated with Parkinson's disease, alpha-synuclein (alpha-syn), and the other important for melanin synthesis, the repeat domain (RPT) from Pmel17.[Review]
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MART-1- and gp100-expressing and -non-expressing melanoma cells are equally proliferative in tumors and clonogenic in vitro.
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Pmel17 repeat domain fibril dissolution is pH dependent
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the DW and HoSi mutations alter PMEL TMD oligomerization and/or association with membranes, with consequent formation of aberrantly packed fibrils. PMEL mutations can model the conversion between physiological and pathological amyloid
