Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells. - Wikidata - wikimedia - TriplyDB

Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells.

Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells.

http://www.wikidata.org/entity/Q36988317

about

Macrophage derived cystatin B/cathepsin B in HIV replication and neuropathogenesis Expression of metabolic, tissue remodeling, oxidative stress, and inflammatory pathways in mammary tissue during involution in lactating dairy cows Predictions versus high-throughput experiments in T-cell epitope discovery: competition or synergy?Cathepsin B controls the persistence of memory CD8+ T lymphocytes.Cathepsin B inhibition limits bone metastasis in breast cancer.Anaplasma phagocytophilum increases cathepsin L activity, thereby globally influencing neutrophil function.Cathepsins and their endogenous inhibitors cystatins: expression and modulation in multiple sclerosis Cathepsin L in metastatic bone disease: therapeutic implications.Integrated computational prediction and experimental validation identifies promiscuous T cell epitopes in the proteome of Mycobacterium bovis.Multiple interleukin-1beta-converting enzymes contribute to inflammatory arthritis.Impaired turnover of autophagolysosomes in cathepsin L deficiency.A novel cysteine cathepsin inhibitor yields macrophage cell death and mammary tumor regression.

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P2860

Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells.

http://www.wikidata.org/entity/Q36988317

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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name

Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells.

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Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells.

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Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells.

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Biological Chemistry

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Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells

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Tina Zavasnik-Bergant

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P2860

Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase

Lysosomal cysteine proteases: facts and opportunities.

Collagen degradation in the abdominal aneurysm: a conspiracy of matrix metalloproteinase and cysteine collagenases

Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages

Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L

Osteoclasts: what do they do and how do they do it?

MEROPS: the peptidase database

IrAE – An asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S.

Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases

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1141-1149

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10.1515/BC.2007.144

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11

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388

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17976006

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