Evidence of MTCBP-1 interaction with the cytoplasmic domain of MT1-MMP: Implications in the autophagy cell index of high-grade glioblastoma.

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Diagnostic and clinical relevance of the autophago-lysosomal network in human gliomas The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.

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P2860

Evidence of MTCBP-1 interaction with the cytoplasmic domain of MT1-MMP: Implications in the autophagy cell index of high-grade glioblastoma.

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Evidence of MTCBP-1 interactio ...... ex of high-grade glioblastoma.

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Evidence of MTCBP-1 interactio ...... ex of high-grade glioblastoma.

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Evidence of MTCBP-1 interactio ...... ex of high-grade glioblastoma.

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Evidence of MTCBP-1 interactio ...... ex of high-grade glioblastoma.

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Borhane Annabi

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Jonathan Pratt

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Mustapha Iddir

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Steve Bourgault

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P2860

Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors

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The 2007 WHO classification of tumours of the central nervous system

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A concerted HIF-1α/MT1-MMP signalling axis regulates the expression of the 3BP2 adaptor protein in hypoxic mesenchymal stromal cells

Gliomas induce and exploit microglial MT1-MMP expression for tumor expansion

The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein.

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10.1002/MC.22264

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autophagy

Evidence of MTCBP-1 interaction with the cytoplasmic domain of MT1-MMP: Implications in the autophagy cell index of high-grade glioblastoma.

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P2860

P2860

Evidence of MTCBP-1 interaction with the cytoplasmic domain of MT1-MMP: Implications in the autophagy cell index of high-grade glioblastoma.

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