-
1
-
-
0029615496
-
How MHC class II molecules acquire peptide cargo: Biosynthesis and trafficking through the endocytic pathway
-
Wolf P.R., Ploegh H.L. How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. Annu Rev Cell Biol. 11:1995;267-306.
-
(1995)
Annu Rev Cell Biol
, vol.11
, pp. 267-306
-
-
Wolf, P.R.1
Ploegh, H.L.2
-
2
-
-
0030937833
-
Capture and processing of exogenous antigens for presentation on MHC molecules
-
Watts C. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu Rev Immunol. 15:1997;821-850.
-
(1997)
Annu Rev Immunol
, vol.15
, pp. 821-850
-
-
Watts, C.1
-
3
-
-
0031012835
-
Role of the occluding loop in cathepsin B activity
-
Illy C., Quraishi O., Wang J., Purisima E., Vernet T., Mort J.S. Role of the occluding loop in cathepsin B activity. J Biol Chem. 272:1997;1197-1202.
-
(1997)
J Biol Chem
, vol.272
, pp. 1197-1202
-
-
Illy, C.1
Quraishi, O.2
Wang, J.3
Purisima, E.4
Vernet, T.5
Mort, J.S.6
-
4
-
-
0032518496
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Crystal structure of porcine cathepsin H determined at 2.1 A resolution: Location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
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This report describes the crystal structure of cathepsin H, which has an octapeptide 'minichain' derived from its propiece that partially obscures the active site and influences enzyme activity
-
Guncar G., Podobnik M., Pungercar J., Strukelj B., Turk V., Turk D. Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure. 6:1998;51-61. This report describes the crystal structure of cathepsin H, which has an octapeptide 'minichain' derived from its propiece that partially obscures the active site and influences enzyme activity.
-
(1998)
Structure
, vol.6
, pp. 51-61
-
-
Guncar, G.1
Podobnik, M.2
Pungercar, J.3
Strukelj, B.4
Turk, V.5
Turk, D.6
-
5
-
-
0033610817
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Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization
-
Wang B., Shi G.P., Yao P.M., Li Z., Chapman H.A., Bromme D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J Biol Chem. 273:1998;32000-32008.
-
(1998)
J Biol Chem
, vol.273
, pp. 32000-32008
-
-
Wang, B.1
Shi, G.P.2
Yao, P.M.3
Li, Z.4
Chapman, H.A.5
Bromme, D.6
-
6
-
-
0033553419
-
Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
-
Santamaria I., Velasco G., Pendas A.M., Az A., Lopez-Otin C. Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J Biol Chem. 274:1999;13800-13809.
-
(1999)
J Biol Chem
, vol.274
, pp. 13800-13809
-
-
Santamaria, I.1
Velasco, G.2
Pendas, A.M.3
Az, A.4
Lopez-Otin, C.5
-
7
-
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0033109243
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Expression of cathepsin K in lung epithelial cells
-
Buhling F., Gerber A., Hackel C., Kruger S., Kohnlein T., Bromme D., Reinhold D., Ansorge S., Welte T. Expression of cathepsin K in lung epithelial cells. Am J Respir Cell Mol Biol. 20:1999;612-619.
-
(1999)
Am J Respir Cell Mol Biol
, vol.20
, pp. 612-619
-
-
Buhling, F.1
Gerber, A.2
Hackel, C.3
Kruger, S.4
Kohnlein, T.5
Bromme, D.6
Reinhold, D.7
Ansorge, S.8
Welte, T.9
-
8
-
-
0038687865
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Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
-
Bromme D., Li Z., Barnes M., Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry. 38:1999;2377-2383.
-
(1999)
Biochemistry
, vol.38
, pp. 2377-2383
-
-
Bromme, D.1
Li, Z.2
Barnes, M.3
Mehler, E.4
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9
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0032522413
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Cathepsin L2, a novel human cysteine protease produced by breast and colorectal carcinomas
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One of two reports (with [8]) describing a new cysteine protease that is highly homologous to cathepsin L and exhibits restricted tissue expression to thymus, testis and tumor cell lines. This cathepsin has no mouse homologue. It may play a similar role in Ii processing within human cortical thymus as does mouse cathepsin L. This protease has also been referred to as cathepsins V and U
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Santamaria I., Velasco G., Cazoria M., Fueyo A., Campo E., Lopez-Otin C. Cathepsin L2, a novel human cysteine protease produced by breast and colorectal carcinomas. Cancer Res. 58:1998;1624-1630. One of two reports (with [8]) describing a new cysteine protease that is highly homologous to cathepsin L and exhibits restricted tissue expression to thymus, testis and tumor cell lines. This cathepsin has no mouse homologue. It may play a similar role in Ii processing within human cortical thymus as does mouse cathepsin L. This protease has also been referred to as cathepsins V and U.
-
(1998)
Cancer Res
, vol.58
, pp. 1624-1630
-
-
Santamaria, I.1
Velasco, G.2
Cazoria, M.3
Fueyo, A.4
Campo, E.5
Lopez-Otin, C.6
-
10
-
-
0032479144
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Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location
-
Santamaria I., Velasco G., Pendas A.M., Fueyo A., Lopez-Otin C. Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location. J Biol Chem. 273:1998;16816-16823.
-
(1998)
J Biol Chem
, vol.273
, pp. 16816-16823
-
-
Santamaria, I.1
Velasco, G.2
Pendas, A.M.3
Fueyo, A.4
Lopez-Otin, C.5
-
11
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0040234054
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Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions
-
One of two articles (with [10]) describing the discovery of a new cysteine protease with a very short propiece and a 15 amino acid insertion analogous to the 'occluding loop' region of cathepsin B. This protease has also been called cathepsins Z and P
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Nagler D.K., Menard R. Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions. FEBS Lett. 434:1998;135-139. One of two articles (with [10]) describing the discovery of a new cysteine protease with a very short propiece and a 15 amino acid insertion analogous to the 'occluding loop' region of cathepsin B. This protease has also been called cathepsins Z and P.
-
(1998)
FEBS Lett
, vol.434
, pp. 135-139
-
-
Nagler, D.K.1
Menard, R.2
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12
-
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0032551750
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Genomic structure, chromosomal localization, and expression of human cathepsin W
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Wex T., Levy B., Smeekens S.P., Ansorge S., Desnick R.J., Bromme D. Genomic structure, chromosomal localization, and expression of human cathepsin W. Biochem Biophys Res Comm. 248:1998;255-261.
-
(1998)
Biochem Biophys Res Comm
, vol.248
, pp. 255-261
-
-
Wex, T.1
Levy, B.2
Smeekens, S.P.3
Ansorge, S.4
Desnick, R.J.5
Bromme, D.6
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13
-
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0031785963
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Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase
-
Brown J., Matutes E., Singleton A., Price C., Molgaard H., Buttle D., Enver T. Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase. Leukemia. 12:1998;1771-1781.
-
(1998)
Leukemia
, vol.12
, pp. 1771-1781
-
-
Brown, J.1
Matutes, E.2
Singleton, A.3
Price, C.4
Molgaard, H.5
Buttle, D.6
Enver, T.7
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14
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0033587689
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Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
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This article shows that dipeptidyl peptidase I (cathepsin C) is required for activation of granzymes A and B; the authors analyzed cytotoxic lymphocytes from cathepsin-C-null mice
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Pham C.T.N., Ley T.J. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc Natl Acad Sci USA. 96:1999;8627-8632. This article shows that dipeptidyl peptidase I (cathepsin C) is required for activation of granzymes A and B; the authors analyzed cytotoxic lymphocytes from cathepsin-C-null mice.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 8627-8632
-
-
Pham, C.T.N.1
Ley, T.J.2
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15
-
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0032516003
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Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
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Deussing J., Roth W., Saftig P., Peters C., Ploegh H.L., Villadangos J.A. Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc Natl Acad Sci USA. 95:1998;4516-4521.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 4516-4521
-
-
Deussing, J.1
Roth, W.2
Saftig, P.3
Peters, C.4
Ploegh, H.L.5
Villadangos, J.A.6
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16
-
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0032542285
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An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation
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A newly discovered cysteine protease mediates the initial cleavages of tetanus toxin processing. This enzyme has a predilection for nonglycosylated asparagine moieties that may select for processing of bacterial proteins
-
Manoury B., Hewitt E.W., Morrice N., Dando P.M., Barrett A.J., Watt C. An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. Nature. 396:1998;695-699. A newly discovered cysteine protease mediates the initial cleavages of tetanus toxin processing. This enzyme has a predilection for nonglycosylated asparagine moieties that may select for processing of bacterial proteins.
-
(1998)
Nature
, vol.396
, pp. 695-699
-
-
Manoury, B.1
Hewitt, E.W.2
Morrice, N.3
Dando, P.M.4
Barrett, A.J.5
Watt, C.6
-
17
-
-
0031468018
-
Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
-
Cygler M., Mort J.S. Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity. Biochimie. 79:1997;645-652.
-
(1997)
Biochimie
, vol.79
, pp. 645-652
-
-
Cygler, M.1
Mort, J.S.2
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18
-
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0028309017
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The proregion of cathepsin L is required for proper folding, stability, and ER exit
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Tao K., Stearns N.A., Dong J., Wu Q.L., Sahagian G.G. The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch Biochem Biophys. 311:1994;19-27.
-
(1994)
Arch Biochem Biophys
, vol.311
, pp. 19-27
-
-
Tao, K.1
Stearns, N.A.2
Dong, J.3
Wu, Q.L.4
Sahagian, G.G.5
-
19
-
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0028905069
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Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing
-
Vernet T., Berti P.J., de Montigny C., Musil R., Tessier D.C., Menard R., Magny M.C., Storer A.C., Thomas D.Y. Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing. J Biol Chem. 270:1995;10838-10846.
-
(1995)
J Biol Chem
, vol.270
, pp. 10838-10846
-
-
Vernet, T.1
Berti, P.J.2
De Montigny, C.3
Musil, R.4
Tessier, D.C.5
Menard, R.6
Magny, M.C.7
Storer, A.C.8
Thomas, D.Y.9
-
20
-
-
0029976244
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Crystal structures of human cathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide
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Turk D., Podobnik M., Kuhelj R., Dolinar M., Turk V. Crystal structures of human cathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. 384:1996;211-214.
-
(1996)
FEBS Lett
, vol.384
, pp. 211-214
-
-
Turk, D.1
Podobnik, M.2
Kuhelj, R.3
Dolinar, M.4
Turk, V.5
-
21
-
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0029902382
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Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
-
Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., Cygler M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15:1996;5492-5503.
-
(1996)
EMBO J
, vol.15
, pp. 5492-5503
-
-
Coulombe, R.1
Grochulski, P.2
Sivaraman, J.3
Menard, R.4
Mort, J.S.5
Cygler, M.6
-
22
-
-
0033579959
-
The crystal structure of human procathepsin K
-
LaLonde J.M., Zhao B., Janson C.A., D'Alessio K.J., McQueney M.S., Orsini M.J., Debouck C.M., Smith W.W. The crystal structure of human procathepsin K. Biochemistry. 38:1999;802-809.
-
(1999)
Biochemistry
, vol.38
, pp. 802-809
-
-
Lalonde, J.M.1
Zhao, B.2
Janson, C.A.3
D'Alessio, K.J.4
McQueney, M.S.5
Orsini, M.J.6
Debouck, C.M.7
Smith, W.W.8
-
23
-
-
0031013054
-
Friends and relatives of the cystatin superfamily - new members and their evolution
-
Brown W.M., Dziegielewska K.M. Friends and relatives of the cystatin superfamily - new members and their evolution. Protein Sci. 6:1997;5-12.
-
(1997)
Protein Sci
, vol.6
, pp. 5-12
-
-
Brown, W.M.1
Dziegielewska, K.M.2
-
24
-
-
0030918546
-
Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
-
Turk B., Turk V., Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol Chem. 378:1997;141-150.
-
(1997)
Biol Chem
, vol.378
, pp. 141-150
-
-
Turk, B.1
Turk, V.2
Turk, D.3
-
25
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0040909177
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The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide
-
The ability of the cathepsin B propiece, and potentially that of cystatin C, to inhibit cathepsin B is dependent on the flexibility of the cathepsin B occluding loop. At neutral pH, the occluding loop exhibits enhanced flexibility - permitting displacement and facilitating inhibition by its propiece. However at acidic pH the occluding loop assumes a 'closed' and more rigid position, which effectively blocks entry of its propiece into the active site cleft. This variability of the occluding loop flexibility may alter the proteolytic potential of cathepsin B within endosomes of differing pH
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Quraishi O., Nagler D.K., Fox T., Sivaraman J., Cygler M., Mort J.S., Storer A. The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide. Biochemistry. 38:1999;3017-3023. The ability of the cathepsin B propiece, and potentially that of cystatin C, to inhibit cathepsin B is dependent on the flexibility of the cathepsin B occluding loop. At neutral pH, the occluding loop exhibits enhanced flexibility - permitting displacement and facilitating inhibition by its propiece. However at acidic pH the occluding loop assumes a 'closed' and more rigid position, which effectively blocks entry of its propiece into the active site cleft. This variability of the occluding loop flexibility may alter the proteolytic potential of cathepsin B within endosomes of differing pH.
-
(1999)
Biochemistry
, vol.38
, pp. 3017-3023
-
-
Quraishi, O.1
Nagler, D.K.2
Fox, T.3
Sivaraman, J.4
Cygler, M.5
Mort, J.S.6
Storer, A.7
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26
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0032568806
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Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
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This study reveals that degradation of Ii is required for maturation and cell surface expression of class II molecules in DCs. Inhibition of Ii degradation in immature DCs occurs by increased expression of cystatin C, resulting in accumulation of class-II-Lip10 complexes within lysosomal structures. As DCs mature, the intralysosomal level of cystatin C decreases - allowing complete Ii degradation and efflux of class II molecules to the cell surface. Thus, DCs may utilize regulation of Ii processing as a physiologic mechanism for controlling cell surface class II expression
-
Pierre P., Mellman I. Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell. 93:1998;1135-1145. This study reveals that degradation of Ii is required for maturation and cell surface expression of class II molecules in DCs. Inhibition of Ii degradation in immature DCs occurs by increased expression of cystatin C, resulting in accumulation of class-II-Lip10 complexes within lysosomal structures. As DCs mature, the intralysosomal level of cystatin C decreases - allowing complete Ii degradation and efflux of class II molecules to the cell surface. Thus, DCs may utilize regulation of Ii processing as a physiologic mechanism for controlling cell surface class II expression.
-
(1998)
Cell
, vol.93
, pp. 1135-1145
-
-
Pierre, P.1
Mellman, I.2
-
27
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0031030180
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Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer
-
Sotiropoulou G., Anisowicz A., Sager R. Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J Biol Chem. 272:1997;903-910.
-
(1997)
J Biol Chem
, vol.272
, pp. 903-910
-
-
Sotiropoulou, G.1
Anisowicz, A.2
Sager, R.3
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28
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0032544743
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Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor
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Ni J., Fernandez M.A., Danielsson L., Chillakuru R.A., Zhang J., Grubb A., Su J., Gentz R., Abrahamson M. Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor. J Biol Chem. 273:1998;24797-24804.
-
(1998)
J Biol Chem
, vol.273
, pp. 24797-24804
-
-
Ni, J.1
Fernandez, M.A.2
Danielsson, L.3
Chillakuru, R.A.4
Zhang, J.5
Grubb, A.6
Su, J.7
Gentz, R.8
Abrahamson, M.9
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29
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0032569023
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Leukocystatin, a new class II cystatin expressed selectively by hematopoietic cells
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Halfon S., Ford J., Foster J., Dowling L., Lucian L., Sterling M., Zu Y., Weiss M., Ikeda M., Liggett D.et al. Leukocystatin, a new class II cystatin expressed selectively by hematopoietic cells. J Biol Chem. 273:1998;16400-16408.
-
(1998)
J Biol Chem
, vol.273
, pp. 16400-16408
-
-
Halfon, S.1
Ford, J.2
Foster, J.3
Dowling, L.4
Lucian, L.5
Sterling, M.6
Zu, Y.7
Weiss, M.8
Ikeda, M.9
Liggett, D.10
-
30
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0039642231
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Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen
-
This report describes the full length sequence of cathepsin F, showing an unusually long propiece. Interestingly, this propiece contains a cystatin-like domain at the amino-terminus as well as the expected cathepsin-L-like propiece domain. Thus, cathepsin F has two regions within its propiece which could potentially inhibit the mature enzyme. This is unique among the papain-like cysteine proteases
-
Nagler D.K., Sulea T., Menard R. Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. Biochem Biophys Res Commun. 257:1999;313-318. This report describes the full length sequence of cathepsin F, showing an unusually long propiece. Interestingly, this propiece contains a cystatin-like domain at the amino-terminus as well as the expected cathepsin-L-like propiece domain. Thus, cathepsin F has two regions within its propiece which could potentially inhibit the mature enzyme. This is unique among the papain-like cysteine proteases.
-
(1999)
Biochem Biophys Res Commun
, vol.257
, pp. 313-318
-
-
Nagler, D.K.1
Sulea, T.2
Menard, R.3
-
31
-
-
0029924123
-
Major histocompatibility complex class-II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L.
-
Bevec T., Stoka V., Pungercic G., Dolenc I., Turk V. Major histocompatibility complex class-II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L. J Exp Med. 183:1996;1331-1338.
-
(1996)
J Exp Med
, vol.183
, pp. 1331-1338
-
-
Bevec, T.1
Stoka, V.2
Pungercic, G.3
Dolenc, I.4
Turk, V.5
-
32
-
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0039547996
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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
-
The crystal structure of the p41 Ii exon bound to cathepsin L reveals a similar 'wedge-shaped' binding motif to that observed with cystatin B bound to papain. However the p41 Ii exon exhibits a unique fold that accounts for its high degree of specificity for inhibition of cathepsin L
-
Guncar G., Pungercic G., Klemencic I., Turk V., Turk D. 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. EMBO J. 18:1999;793-808. The crystal structure of the p41 Ii exon bound to cathepsin L reveals a similar 'wedge-shaped' binding motif to that observed with cystatin B bound to papain. However the p41 Ii exon exhibits a unique fold that accounts for its high degree of specificity for inhibition of cathepsin L.
-
(1999)
EMBO J
, vol.18
, pp. 793-808
-
-
Guncar, G.1
Pungercic, G.2
Klemencic, I.3
Turk, V.4
Turk, D.5
-
33
-
-
0031965961
-
Intracellular transport of molecules engaged in the presentation of exogenous antigens
-
Nordeng T.W., Gorvel J.P., Bakke O. Intracellular transport of molecules engaged in the presentation of exogenous antigens. Curr Top Microbiol Immunol. 232:1998;179-215.
-
(1998)
Curr Top Microbiol Immunol
, vol.232
, pp. 179-215
-
-
Nordeng, T.W.1
Gorvel, J.P.2
Bakke, O.3
-
34
-
-
0029931108
-
Essential role for cathepsin S in MHC class-II-associated invariant chain processing and peptide loading
-
Riese R.J., Wolf P.R., Bromme D., Natkin L.R., Villadangos J.A., Ploegh H.L., Chapman H.A. Essential role for cathepsin S in MHC class-II-associated invariant chain processing and peptide loading. Immunity. 4:1996;357-366.
-
(1996)
Immunity
, vol.4
, pp. 357-366
-
-
Riese, R.J.1
Wolf, P.R.2
Bromme, D.3
Natkin, L.R.4
Villadangos, J.A.5
Ploegh, H.L.6
Chapman, H.A.7
-
35
-
-
0030790341
-
Degradation of mouse invariant chain: Roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism
-
Villadangos J.A., Riese R.J., Peters C., Chapman H.A., Ploegh H.L. Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism. J Exp Med. 186:1997;549-560.
-
(1997)
J Exp Med
, vol.186
, pp. 549-560
-
-
Villadangos, J.A.1
Riese, R.J.2
Peters, C.3
Chapman, H.A.4
Ploegh, H.L.5
-
36
-
-
0033083688
-
Cathepsin S required for normal MHC class II peptide loading and germinal center formation
-
3 antibody responses. Interestingly, IgE responses are normal
-
3 antibody responses. Interestingly, IgE responses are normal.
-
(1999)
Immunity
, vol.10
, pp. 197-206
-
-
Shi, G.P.1
Villadangos, J.A.2
Dranoff, G.3
Small, C.4
Gu, L.J.5
Haley, K.J.6
Riese, R.7
Ploegh, H.L.8
Chapman, H.A.9
-
37
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-
2442549710
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Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice
-
q mice do demonstrate diminished collagen-induced arthritis. Thus cathepsin S may be required for processing of an immunodominant antigen mediating collagen-induced arthritis in this mouse model, or the absence of cathepsin S may result in a more subtle kinetic alteration in Ii processing and class-II-peptide loading without affecting bulk biochemistry
-
q mice do demonstrate diminished collagen-induced arthritis. Thus cathepsin S may be required for processing of an immunodominant antigen mediating collagen-induced arthritis in this mouse model, or the absence of cathepsin S may result in a more subtle kinetic alteration in Ii processing and class-II-peptide loading without affecting bulk biochemistry.
-
(1999)
Immunity
, vol.10
, pp. 207-217
-
-
Nakagawa, T.Y.1
Brissette, W.H.2
Lira, P.D.3
Griffiths, R.J.4
Petrushova, N.5
Stock, J.6
McNeish, J.D.7
Eastman, S.E.8
Howard, E.D.9
Clarke, S.R.M.10
Rosloniec, E.F.11
Elliott, E.A.12
Rudensky, A.Y.13
-
38
-
-
0032540474
-
Cathepsin L: Critical role in Ii degradation and CD4 T cell selection in the thymus
-
+ T cell positive selection
-
+ T cell positive selection.
-
(1998)
Science
, vol.280
, pp. 450-453
-
-
Nakagawa, T.1
Roth, W.2
Wong, P.3
Nelson, A.4
Farr, A.5
Deussing, J.6
Villadangos, J.A.7
Ploegh, H.L.8
Peters, C.9
Rudensky, A.Y.10
-
39
-
-
0030985764
-
Ii chain controls the transport of major histocompatibility complex class II molecules to and from lysosomes
-
Brachet V., Raposo G., Amigorena S., Mellman I. Ii chain controls the transport of major histocompatibility complex class II molecules to and from lysosomes. J Cell Biol. 137:1997;51-65.
-
(1997)
J Cell Biol
, vol.137
, pp. 51-65
-
-
Brachet, V.1
Raposo, G.2
Amigorena, S.3
Mellman, I.4
-
40
-
-
0033571691
-
Cathepsin S controls the trafficking and maturation of MHC class II molecules in dendritic cells
-
This study reveals that cathepsin S activity is required for normal MHC class II trafficking within DCs. Cathepsin S activity is found throughout the endocytic pathway. In DCs from mice genetically deficient in cathepsin S, class-II-Lip10 complexes accumulate within the lysosomes and efflux of class II molecules to the cell surface is severely reduced
-
Driessen C., Bryant R.A.R., Lennon-Dumenil A-M., Villadangos J.A., Bryant P.W., Shi G-P., Chapman H.A., Ploegh H.L. Cathepsin S controls the trafficking and maturation of MHC class II molecules in dendritic cells. J Cell Biol. 147:1999;775-790. This study reveals that cathepsin S activity is required for normal MHC class II trafficking within DCs. Cathepsin S activity is found throughout the endocytic pathway. In DCs from mice genetically deficient in cathepsin S, class-II-Lip10 complexes accumulate within the lysosomes and efflux of class II molecules to the cell surface is severely reduced.
-
(1999)
J Cell Biol
, vol.147
, pp. 775-790
-
-
Driessen, C.1
Bryant, R.A.R.2
Lennon-Dumenil, A.-M.3
Villadangos, J.A.4
Bryant, P.W.5
Shi, G.-P.6
Chapman, H.A.7
Ploegh, H.L.8
-
41
-
-
0030869567
-
Developmental regulation of MHC class II transport in mouse dendritic cells
-
Pierre P., Turley S.J., Gatti E., Hull M., Meltzer J., Mirza A., Inaba K., Steinman R.M., Mellman I. Developmental regulation of MHC class II transport in mouse dendritic cells. Nature. 388:1997;787-791.
-
(1997)
Nature
, vol.388
, pp. 787-791
-
-
Pierre, P.1
Turley, S.J.2
Gatti, E.3
Hull, M.4
Meltzer, J.5
Mirza, A.6
Inaba, K.7
Steinman, R.M.8
Mellman, I.9
-
42
-
-
0030858138
-
Inflammatory stimuli induce accumulation of MHC class II complexes on dendritic cells
-
Cella M., Engering A., Pinet V., Pieters J., Lanzavecchia A. Inflammatory stimuli induce accumulation of MHC class II complexes on dendritic cells. Nature. 388:1997;782-786.
-
(1997)
Nature
, vol.388
, pp. 782-786
-
-
Cella, M.1
Engering, A.2
Pinet, V.3
Pieters, J.4
Lanzavecchia, A.5
-
43
-
-
0032540248
-
Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages
-
These authors utilize percoll-gradient centrifugation to separate intracellular compartments into phagosomes, early endosomes, late endosomes and lysosomes. The investigators find that cathepsin H is localized to the early endosomal compartments, and cathepsins B and L to the lysosomes
-
Claus V., Jahraus A., Tjelle T., Berg T., Kirschke H., Faulstich H., Griffiths G. Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. J Biol Chem. 273:1998;9842-9851. These authors utilize percoll-gradient centrifugation to separate intracellular compartments into phagosomes, early endosomes, late endosomes and lysosomes. The investigators find that cathepsin H is localized to the early endosomal compartments, and cathepsins B and L to the lysosomes.
-
(1998)
J Biol Chem
, vol.273
, pp. 9842-9851
-
-
Claus, V.1
Jahraus, A.2
Tjelle, T.3
Berg, T.4
Kirschke, H.5
Faulstich, H.6
Griffiths, G.7
-
44
-
-
0033083868
-
Acidic pH as a physiological regulator of human cathepsin L activity
-
Turk B., Dolenc I., Lenarcic B., Krizaj I., Turk V., Bieth J.G., Bjork I. Acidic pH as a physiological regulator of human cathepsin L activity. Eur J Biochem. 259:1999;926-932.
-
(1999)
Eur J Biochem
, vol.259
, pp. 926-932
-
-
Turk, B.1
Dolenc, I.2
Lenarcic, B.3
Krizaj, I.4
Turk, V.5
Bieth, J.G.6
Bjork, I.7
-
45
-
-
0029284365
-
Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins
-
Turk B., Bieth J.G., Bjork I., Dolenc I., Turk D., Cimerman N., Kos J., Colic A., Stoka V., Turk V. Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins. Biol Chem Hoppe Seyler. 376:1995;225-230.
-
(1995)
Biol Chem Hoppe Seyler
, vol.376
, pp. 225-230
-
-
Turk, B.1
Bieth, J.G.2
Bjork, I.3
Dolenc, I.4
Turk, D.5
Cimerman, N.6
Kos, J.7
Colic, A.8
Stoka, V.9
Turk, V.10
-
46
-
-
0032477737
-
Dendritic cell maturation and antigen presentation in the absence of invariant chain
-
k class II molecules are less reliant on Ii for proper function, implying that disruption of Ii processing by inhibition of cysteine proteases would also be less affected
-
k class II molecules are less reliant on Ii for proper function, implying that disruption of Ii processing by inhibition of cysteine proteases would also be less affected.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 1067-1072
-
-
Rovere, P.1
Zimmerman, V.S.2
Forquet, F.3
Demandolx, D.4
Trucy, J.5
Ricciardi-Castagnoli, P.6
Davoust, J.7
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