Zobrazeno 1 - 10
of 35
pro vyhledávání: '"J A, Hartsuck"'
Publikováno v:
Journal of Biological Chemistry. 267:18413-18418
The pH dependence of the kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants has been determined. These data have permitted the calculation of two active-site ionization constants in the free enzymes (pKe1 and pK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::adf066d508d14a532ced687fa8197f4f
https://doi.org/10.1016/s0021-9258(19)36978-9
https://doi.org/10.1016/s0021-9258(19)36978-9
Publikováno v:
Journal of Biological Chemistry. 266:23365-23372
Lysosomal enzymes contain a common protein determinant that is recognized by UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, the initial enzyme in the biosynthesis of mannose-6-P residues. Previously, we generated a lysosomal en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6cb0ff5347747438a42b4cd18907a140
https://doi.org/10.1016/s0021-9258(18)54505-1
https://doi.org/10.1016/s0021-9258(18)54505-1
Publikováno v:
Journal of Biological Chemistry. 266:11718-11725
A cDNA clone, which contained the complete rhizopuspepsin structure and the putative proregion, was placed in three different Escherichia coli expression vectors for the synthesis of rhizopuspepsinogen (Rpg). Recombinant Rpgs which were expressed in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d665a8c3d46d8edfe6aa1feca144a659
https://doi.org/10.1016/s0021-9258(18)99016-2
https://doi.org/10.1016/s0021-9258(18)99016-2
Publikováno v:
Advances in experimental medicine and biology. 436
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::310c3b0075b912753e03f82f42674a91
https://pubmed.ncbi.nlm.nih.gov/9561200
https://pubmed.ncbi.nlm.nih.gov/9561200
Publikováno v:
Protein science : a publication of the Protein Society. 7(2)
The mutation Ala28 to serine in human immunodeficiency virus, type 1, (HIV-1) protease introduces putative hydrogen bonds to each active-site carboxyl group. These hydrogen bonds are ubiquitous in pepsin-like eukaryotic aspartic proteases. In order t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::82126da51b59ddbc70798ebe8af13c85
https://pubmed.ncbi.nlm.nih.gov/9521105
https://pubmed.ncbi.nlm.nih.gov/9521105
Publikováno v:
FEBS letters. 420(1)
The crystal structure of human immunodeficiency virus type 1 (HIV-1) protease mutant G48H with peptidic inhibitor U-89360E is described. Comparison with wild-type protease-inhibitor complex shows that mutation of flap residue 48 to histidine allows s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6571ca2ea50c995686fa5423ed1dafd8
https://pubmed.ncbi.nlm.nih.gov/9450540
https://pubmed.ncbi.nlm.nih.gov/9450540
Publikováno v:
Advances in experimental medicine and biology. 362
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6b76ce5103705cdbbf78c5e9ec38132f
https://pubmed.ncbi.nlm.nih.gov/8540347
https://pubmed.ncbi.nlm.nih.gov/8540347
Publikováno v:
The Journal of biological chemistry. 267(26)
The pH dependence of the kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants has been determined. These data have permitted the calculation of two active-site ionization constants in the free enzymes (pKe1 and pK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::608562804479e3234d5cc4993bf1efc8
https://pubmed.ncbi.nlm.nih.gov/1526982
https://pubmed.ncbi.nlm.nih.gov/1526982
Publikováno v:
Scandinavian journal of clinical and laboratory investigation. Supplementum. 210
The protease of human immunodeficiency virus (HIV) has been extensively studied. The structure and function relationships of this protease and its role in HIV life cycle is well known. We have use recombinant HIV protease and mutagenesis technology t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ed8d45e6b6998a0e490adb3547501779
https://pubmed.ncbi.nlm.nih.gov/1455175
https://pubmed.ncbi.nlm.nih.gov/1455175
Publikováno v:
The Journal of biological chemistry. 266(34)
Lysosomal enzymes contain a common protein determinant that is recognized by UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, the initial enzyme in the biosynthesis of mannose-6-P residues. Previously, we generated a lysosomal en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2085a579997d4232d2badf18f643c4d8
https://pubmed.ncbi.nlm.nih.gov/1660471
https://pubmed.ncbi.nlm.nih.gov/1660471