Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Elizabeth A. Kersteen"'
Publikováno v:
Bioorganic & Medicinal Chemistry. 21:3597-3601
Collagen is the most abundant protein in animals. Its prevalent 4-hydroxyproline residues contribute greatly to its conformational stability. The hydroxyl groups arise from a post-translational modification catalyzed by the non-heme iron-dependent en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52aba70f920db7e09a935713ae476bb9
https://doi.org/10.1016/j.bmc.2013.04.057
https://doi.org/10.1016/j.bmc.2013.04.057
Publikováno v:
Biochemistry. 44:12168-12178
Protein disulfide isomerase (PDI) catalyzes the rearrangement of nonnative disulfide bonds in the endoplasmic reticulum of eukaryotic cells, a process that often limits the rate at which polypeptide chains fold into a native protein conformation. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b227fa1411205f43cc114d93e584e88e
https://doi.org/10.1021/bi0507985
https://doi.org/10.1021/bi0507985
Publikováno v:
Protein Expression and Purification. 38:279-291
Prolyl 4-hydroxylase (P4H) catalyzes the post-translational hydroxylation of proline residues in collagen strands. The enzyme is an alpha2beta2 tetramer in which the alpha subunits contain the catalytic active sites and the beta subunits (protein dis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::041973b4d411b02fe2eb5d79ca184de0
https://doi.org/10.1016/j.pep.2004.09.008
https://doi.org/10.1016/j.pep.2004.09.008
Publikováno v:
Biopolymers. 59:24-28
The collagen triple helix is composed of three polypeptide strands, each with a sequence of repeating (Xaa-Yaa-Gly) triplets. In these triplets, Xaa and Yaa are often tertiary amides: L-proline (Pro) and 4(R)-hydroxy-L-proline (Hyp). To determine the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f14912d7873141596afd2c190c208bed
https://doi.org/10.1002/1097-0282(200107)59:1<24::aid-bip1002>3.0.co
https://doi.org/10.1002/1097-0282(200107)59:1<24::aid-bip1002>3.0.co
Autor:
Paul L. Edmiston, Nichole R. Moore, Charles L. Borders, Elizabeth A. Kersteen, Kristy L. Schavolt
Publikováno v:
Biochimica et biophysica acta. 1546(2)
Sequence homology analysis reveals that arginine-95 is fully conserved in 29 creatine kinases sequenced to date, but fully conserved as a tyrosine residue in 16 arginine kinases. Site-directed mutants of rabbit muscle creatine kinase (rmCK) were prep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62d7ccf0e4476f0cfaaae4455fe5e914
https://pubmed.ncbi.nlm.nih.gov/11295435
https://pubmed.ncbi.nlm.nih.gov/11295435
Publikováno v:
Antioxidants & Redox Signaling; Aug2003, Vol. 5 Issue 4, p413, 12p