D J Hupe
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Explore the profile of D J Hupe including associated specialties, affiliations and a list of published articles.
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21
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222
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Recent Articles
1.
Johnson L, Pavlovsky A, Johnson A, Janowicz J, Man C, Ortwine D, et al.
J Biol Chem
. 2001 Feb;
275(15):11026-33.
PMID: 10753905
The pH dependence of matrix metalloproteinase (MMP) catalysis is described by a broad bell-shaped curve, indicating the involvement of two unspecified ionizable groups in proteolysis. Stromelysin-1 has a third pK(a)...
2.
Zimmerman K, Scholten J, Huang C, Fierke C, Hupe D
Protein Expr Purif
. 1999 Jan;
14(3):395-402.
PMID: 9882574
Farnesyl:protein transferase (FPTase) catalyzes the transfer of a 15-carbon farnesyl isoprenoid group from farnesyl diphosphate to the CaaX cysteine of a variety of cellular proteins. Since FPTase is a large...
3.
Johnson L, Dyer R, Hupe D
Curr Opin Chem Biol
. 1998 Sep;
2(4):466-71.
PMID: 9736919
Matrix metalloproteinases are a family of highly regulated peptidases that are collectively responsible for the degradation of extracellular matrix during tissue remodeling. Dysregulated activity has long been implicated in the...
4.
Scholten J, Zimmerman K, Oxender M, Leonard D, Sebolt-Leopold J, Gowan R, et al.
J Biol Chem
. 1997 Jul;
272(29):18077-81.
PMID: 9218438
Investigation of the comparative activities of various inhibitors of farnesyl:protein transferase (FPTase) has led to the observation that the presence of phosphate or pyrophosphate ions in the assay buffer increases...
5.
Scholten J, Zimmerman K, Oxender M, Sebolt-Leopold J, Gowan R, Leonard D, et al.
Bioorg Med Chem
. 1996 Sep;
4(9):1537-43.
PMID: 8894110
The recent interest in inhibitors of farnesyl:protein transferase (FPTase) has resulted in a better understanding of the enzymology of this protein. Rationally designed inhibitors of prenyl transfer have emerged as...
6.
Tummino P, Prasad J, Ferguson D, Nouhan C, Graham N, Domagala J, et al.
Bioorg Med Chem
. 1996 Sep;
4(9):1401-10.
PMID: 8894098
Several small, achiral nonpeptide inhibitors of HIV-1 protease with low micromolar activity were identified by mass screening of the Parke-Davis compound library. Two of the compounds, structurally similar, were both...
7.
Hayes M, Wrigley S, Chetland I, Reynolds E, Ainsworth A, Renno D, et al.
J Antibiot (Tokyo)
. 1996 Jun;
49(6):505-12.
PMID: 8698631
A series of novel drimane sesquiterpene esters (1-6) was isolated from fermentations of Aspergillus ustus var. pseudodeflectus and their structures elucidated by spectroscopic methods including the HMQC, HMBC and INADEQUATE...
8.
Dhanaraj V, Ye Q, Johnson L, Hupe D, Ortwine D, Dunbar Jr J, et al.
Structure
. 1996 Apr;
4(4):375-86.
PMID: 8740360
Background: Stromelysin belongs to a family of zinc-dependent endopeptidases referred to as matrix metalloproteinases (MMPs, matrixins) because of their capacity for selective degradation of various components of the extracellular matrix....
9.
Dhanaraj V, Ye Q, Johnson L, Hupe D, Ortwine D, Dunbar Jr J, et al.
Drug Des Discov
. 1996 Apr;
13(3-4):3-14.
PMID: 8874040
Structural comparisons of representative members of the zinc metalloproteinase superfamily show that the key secondary structural elements are conserved, in spite of major variations in the sequences including insertions and...
10.
Van Doren S, Kurochkin A, Hu W, Ye Q, Johnson L, Hupe D, et al.
Protein Sci
. 1995 Dec;
4(12):2487-98.
PMID: 8580839
Stromelysin, a representative matrix metalloproteinase and target of drug development efforts, plays a prominent role in the pathological proteolysis associated with arthritis and secondarily in that of cancer metastasis and...