Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Reetta Raag"'
Autor:
Arthur D. Clark, Stephen H. Hughes, Alfredo Jacobo-Molina, Edward Arnold, Chris Tantillo, Premal H. Patel, Raymond G. Nanni, Jianping Ding, Reetta Raag
Publikováno v:
Biochemistry. 34:5351-5363
When the single-stranded RNA genome of HIV-1 is copied into double-stranded DNA, the viral enzyme reverse transcriptase (RT) catalyzes the addition of approximately 20,000 nucleotides; however, the precise mechanism of nucleotide addition is unknown.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08813842c423e66ce5dcbfe364785a4e
https://doi.org/10.1021/bi00016a006
https://doi.org/10.1021/bi00016a006
Autor:
Marc Whitlow, Reetta Raag
Publikováno v:
The FASEB Journal. 9:73-80
Single-chain Fvs (sFvs) are recombinant antibody fragments consisting of only the variable light chain (VL) and variable heavy chain (VH) domains covalently connected to one another by a polypeptide linker. Due to their small size, sFvs have rapid ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c19721df0c77247873b3d0e3fd15301
https://doi.org/10.1096/fasebj.9.1.7821762
https://doi.org/10.1096/fasebj.9.1.7821762
Publikováno v:
Journal of Molecular Biology. 234:897-901
Single chain Fv (sFv) proteins consist of the variable heavy chain (VH) and variable light chain (VL) domains of an antibody, covalently joined by an engineered polypeptide linker. We report the crystallization of single-chain Fv's with specificities
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc69c7c29443f777e2a140322fd8f227
https://doi.org/10.1006/jmbi.1993.1638
https://doi.org/10.1006/jmbi.1993.1638
Autor:
Reetta Raag, Thomas L. Poulos
Publikováno v:
The FASEB Journal. 6:674-679
Several crystal structures of various substrate and inhibited complexes of the camphor monoxygenase, cytochrome P450cam from Pseudomonas putida, are now available. These structures, together with mutagenesis, biochemical, and biophysical studies, hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31bc0ca51146ecfac86814ee18bd4020
https://doi.org/10.1096/fasebj.6.2.1537455
https://doi.org/10.1096/fasebj.6.2.1537455
Autor:
Thomas L. Poulos, Anders L. Svensson, Yoshikatsu Hirai, Yoshihiro Masui, Reetta Raag, B. Veerapandian, Gary L. Gilliland
Publikováno v:
Proteins: Structure, Function, and Genetics. 12:10-23
The molecular structure of interleukin-1 beta, a hormone-like cytokine with roles in several disease processes, has been determined at 2.0 A resolution and refined to a crystallographic R-factor of 0.19. The framework of this molecule consists of 12
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b82476f5f9dd09a76ce0845d828862d
https://doi.org/10.1002/prot.340120103
https://doi.org/10.1002/prot.340120103
Publikováno v:
Biochemistry. 30:11420-11429
The crystal structure of a cytochrome P-450CAM site-directed mutant in which the active site Thr252 has been replaced with an Ala (Thr252Ala) has been refined to an R factor of 0.18 at 2.2 A. According to sequence alignments (Nelson & Strobel, 1989),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76036a5e5cce3397ece1940f5233f9c6
https://doi.org/10.1021/bi00112a008
https://doi.org/10.1021/bi00112a008
Autor:
Kenneth E. Goodwill, Reetta Raag, Raymond C. Stevens, Cara B. Marks, Paul F. Fitzpatrick, Christelle Sabatier
Publikováno v:
Nature structural biology. 4(7)
Tyrosine hydroxylase (TyrOH) catalyzes the conversion of tyrosine to L-DOPA, the rate-limiting step in the biosynthesis of the catecholamines dopamine, adrenaline, and noradrenaline. TyrOH is highly homologous in terms of both protein sequence and ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7726372a2ef9b9db476f3fbcefc16c7d
https://pubmed.ncbi.nlm.nih.gov/9228951
https://pubmed.ncbi.nlm.nih.gov/9228951
The crystal structure of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium has been determined to 2.6 A resolution by usine multiple isomorphous replacement methods and simulated annealing refinement. Of the 343 residues, res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42728e72494ae0d5485ad31e922e71b0
https://europepmc.org/articles/PMC45743/
https://europepmc.org/articles/PMC45743/
Autor:
Thomas L. Poulos, Reetta Raag
Publikováno v:
Biochemistry. 30(10)
X-ray crystal structures have been determined for complexes of cytochrome P-450CAM with the substrates camphane, adamantane, and thiocamphor. Unlike the natural substrate camphor, which hydrogen bonds to Tyr96 and is metabolized to a single product,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::933e346e581f95dd7fa7a1af8d2c446b
https://pubmed.ncbi.nlm.nih.gov/2001355
https://pubmed.ncbi.nlm.nih.gov/2001355
Publikováno v:
Biochemistry. 29(35)
Cytochrome P-450cam reacts with phenyldiazene (PhN = NH), or less efficiently with phenylhydrazine, to give a catalytically inactive complex with an absorption maximum at 474 nm. The prosthetic group extracted anaerobically from the inactivated prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34997fbd1883b7486541f89229a0c70f
https://pubmed.ncbi.nlm.nih.gov/2261467
https://pubmed.ncbi.nlm.nih.gov/2261467