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    PMEL premelanosome protein [ Homo sapiens (human) ]

    Gene ID: 6490, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    GP100 expression is variable in intensity in melanoma.

    GP100 expression is variable in intensity in melanoma.
    Mann JE, Hasson N, Su DG, Adeniran AJ, Smalley KSM, Djureinovic D, Jilaveanu LB, Schoenfeld DA, Kluger HM., Free PMC Article

    08/19/2024
    Biogenesis of fibrils requires C-mannosylation of PMEL.

    Biogenesis of fibrils requires C-mannosylation of PMEL.
    Kawahara R, Usami T, Arakawa S, Kamo H, Suzuki T, Komatsu R, Hara H, Niwa Y, Shimizu E, Dohmae N, Shimizu S, Simizu S.

    11/16/2023
    PMEL as a Prognostic Biomarker and Negatively Associated With Immune Infiltration in Skin Cutaneous Melanoma (SKCM).

    PMEL as a Prognostic Biomarker and Negatively Associated With Immune Infiltration in Skin Cutaneous Melanoma (SKCM).
    Zhang S, Chen K, Liu H, Jing C, Zhang X, Qu C, Yu S., Free PMC Article

    01/22/2022
    Identification of critical amino acid residues in the regulatory N-terminal domain of PMEL.

    Identification of critical amino acid residues in the regulatory N-terminal domain of PMEL.
    Mitchell SM, Graham M, Liu X, Leonhardt RM., Free PMC Article

    11/13/2021
    Functional Domains and Evolutionary History of the PMEL and GPNMB Family Proteins.

    Functional Domains and Evolutionary History of the PMEL and GPNMB Family Proteins.
    Chrystal PW, Footz T, Hodges ED, Jensen JA, Walter MA, Allison WT., Free PMC Article

    07/31/2021
    Hofmeister Ions Modulate the Autocatalytic Amyloidogenesis of an Intrinsically Disordered Functional Amyloid Domain via Unusual Biphasic Kinetics.

    Hofmeister Ions Modulate the Autocatalytic Amyloidogenesis of an Intrinsically Disordered Functional Amyloid Domain via Unusual Biphasic Kinetics.
    Dogra P, Roy SS, Joshi A, Mukhopadhyay S.

    03/6/2021
    Modulating functional amyloid formation via alternative splicing of the premelanosomal protein PMEL17.

    Modulating functional amyloid formation via alternative splicing of the premelanosomal protein PMEL17.
    Dean DN, Lee JC., Free PMC Article

    12/26/2020
    Defining an amyloid link Between Parkinson's disease and melanoma.

    Defining an amyloid link Between Parkinson's disease and melanoma.
    Dean DN, Lee JC., Free PMC Article

    10/31/2020
    pH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence.

    pH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence.
    Dean DN, Lee JC., Free PMC Article

    01/18/2020
    These results can give insight into how lysophospholipids might influence repeat domain of Pmel17 aggregation and can give some understanding of general protein-lipid interactions of amyloidogenic proteins.

    Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures.
    Pedersen JN, Jiang Z, Christiansen G, Lee JC, Pedersen JS, Otzen DE., Free PMC Article

    09/7/2019
    This report establishes variation in PMEL as a cause of pigment dispersion syndrom/Pigmentary glaucoma based on several mutually supporting lines of evidence. First, WES of two families affected by PDS/PG and having pedigrees consistent with dominant modes of inheritance led to identification of heterozygous non-synonymous variants in PMEL. We identified seven associated non-synonymous variants.

    Non-Synonymous variants in premelanosome protein (PMEL) cause ocular pigment dispersion and pigmentary glaucoma.
    Lahola-Chomiak AA, Footz T, Nguyen-Phuoc K, Neil GJ, Fan B, Allen KF, Greenfield DS, Parrish RK, Linkroum K, Pasquale LR, Leonhardt RM, Ritch R, Javadiyan S, Craig JE, Allison WT, Lehmann OJ, Walter MA, Wiggs JL., Free PMC Article

    07/6/2019
    silencing of PMEL suppressed melanization through activating lysosomes and degradation of tyrosinase by lysosomes.

    Silencing of PMEL attenuates melanization via activating lysosomes and degradation of tyrosinase by lysosomes.
    Sun L, Hu L, Zhang P, Li H, Sun J, Wang H, Xie X, Hu J.

    01/19/2019
    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

    Dual-specific Chimeric Antigen Receptor T Cells and an Indirect Vaccine Eradicate a Variety of Large Solid Tumors in an Immunocompetent, Self-antigen Setting.
    Slaney CY, von Scheidt B, Davenport AJ, Beavis PA, Westwood JA, Mardiana S, Tscharke DC, Ellis S, Prince HM, Trapani JA, Johnstone RW, Smyth MJ, Teng MW, Ali A, Yu Z, Rosenberg SA, Restifo NP, Neeson P, Darcy PK, Kershaw MH., Free PMC Article

    02/24/2018
    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.

    Polyfunctional response by ImmTAC (IMCgp100) redirected CD8(+) and CD4(+) T cells.
    Boudousquie C, Bossi G, Hurst JM, Rygiel KA, Jakobsen BK, Hassan NJ., Free PMC Article

    10/21/2017
    our work attempts to provide structural insights into the RPT domain structure and to elucidate its contribution to Pmel17 amyloid fibril formation.

    A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.
    Louros NN, Baltoumas FA, Hamodrakas SJ, Iconomidou VA.

    12/17/2016
    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.

    A Molecular Switch Abrogates Glycoprotein 100 (gp100) T-cell Receptor (TCR) Targeting of a Human Melanoma Antigen.
    Bianchi V, Bulek A, Fuller A, Lloyd A, Attaf M, Rizkallah PJ, Dolton G, Sewell AK, Cole DK., Free PMC Article

    11/5/2016
    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.

    The Kringle-like Domain Facilitates Post-endoplasmic Reticulum Changes to Premelanosome Protein (PMEL) Oligomerization and Disulfide Bond Configuration and Promotes Amyloid Formation.
    Ho T, Watt B, Spruce LA, Seeholzer SH, Marks MS., Free PMC Article

    07/16/2016
    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.

    The T210M Substitution in the HLA-a*02:01 gp100 Epitope Strongly Affects Overall Proteasomal Cleavage Site Usage and Antigen Processing.
    Textoris-Taube K, Keller C, Liepe J, Henklein P, Sidney J, Sette A, Kloetzel PM, Mishto M., Free PMC Article

    04/23/2016
    Data indicate that repeat domain (RPT) derived from Pmel17 aggregation kinetics were influenced only by lysolipid-containing phospholipid vesicles.

    Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.
    Jiang Z, Lee JC., Free PMC Article

    04/25/2015
    Melanosome-autonomous regulation of size and number: the OA1 receptor sustains PMEL expression.

    Melanosome-autonomous regulation of size and number: the OA1 receptor sustains PMEL expression.
    Falletta P, Bagnato P, Bono M, Monticone M, Schiaffino MV, Bennett DC, Goding CR, Tacchetti C, Valetti C.

    02/14/2015
    SIL-TAL1 rearrangement identifies a distinct subtype with inferior outcome which could allow for individual therapeutic stratification for T-ALL patients.

    SIL-TAL1 rearrangement is related with poor outcome: a study from a Chinese institution.
    Wang D, Zhu G, Wang N, Zhou X, Yang Y, Zhou S, Xiong J, He J, Jiang L, Li C, Xu D, Huang L, Zhou J., Free PMC Article

    06/21/2014
    the molecular basis for the distinct trafficking and morphogenetic properties of PMEL and GPNMB is the PKD domain

    The PKD domain distinguishes the trafficking and amyloidogenic properties of the pigment cell protein PMEL and its homologue GPNMB.
    Theos AC, Watt B, Harper DC, Janczura KJ, Theos SC, Herman KE, Marks MS., Free PMC Article

    02/8/2014
    Data indicat that the N-terminal region of PMEL/Pmel17 is essential for the formation of melanosomal fibrils.

    Critical residues in the PMEL/Pmel17 N-terminus direct the hierarchical assembly of melanosomal fibrils.
    Leonhardt RM, Vigneron N, Hee JS, Graham M, Cresswell P., Free PMC Article

    09/21/2013
    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.

    BACE2 processes PMEL to form the melanosome amyloid matrix in pigment cells.
    Rochin L, Hurbain I, Serneels L, Fort C, Watt B, Leblanc P, Marks MS, De Strooper B, Raposo G, van Niel G., Free PMC Article

    09/7/2013
    The recombinant Pmel 17 plasmids were right as we expected by DNA sequencing

    [Detection of serum autoantibodies against premelanosome protein 17 increases in the vitiligo patients].
    Hu L, Sun L, Li Y, Li H, Liang D, Sun J, Wang X, Hu J, Xie X.

    08/3/2013
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