Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Leonardus M. I. Koharudin"'
Autor:
Kumaran Baskaran, Colin W. Wilburn, Jonathan R. Wedell, Leonardus M. I. Koharudin, Eldon L. Ulrich, Adam D. Schuyler, Hamid R. Eghbalnia, Angela M. Gronenborn, Jeffrey C. Hoch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::119180019cfcac20b951ecdbcc63dc79
https://doi.org/10.5194/mr-2021-53-supplement
https://doi.org/10.5194/mr-2021-53-supplement
Autor:
Leonardus M. I. Koharudin, Caitlin M. Quinn, Mingzhang Wang, Angela M. Gronenborn, Jochem Struppe, Xingyu Lu, Guangjin Hou, David A. Case, Matthew Fritz, Tatyana Polenova
Publikováno v:
Physical Chemistry Chemical Physics. 20:9543-9553
Chemical shifts are highly sensitive probes of local conformation and overall structure. Both isotropic shifts and chemical shift tensors are readily accessible from NMR experiments but their quantum mechanical calculations remain challenging. In thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::237f26da85045e1adedefdd412ebe610
https://doi.org/10.1039/c8cp00647d
https://doi.org/10.1039/c8cp00647d
Publikováno v:
Chemical Communications. 52:1737-1740
Biochemical characterization of aromatic prenyltransferase AmbP1 and its close homologs WelP1/FidP1 in hapalindole-type alkaloid biosynthetic pathways is reported. These enzymes mediate the magnesium-dependent selective formation of 3-geranyl 3-isocy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23489b679bac76efdcf679b9f82387f0
https://doi.org/10.1039/c5cc10060g
https://doi.org/10.1039/c5cc10060g
Autor:
Karl T. Debiec, Lillian T. Chong, Angela M. Gronenborn, Matthew J. Whitley, Leonardus M. I. Koharudin
Publikováno v:
Biophysical journal. 114(4)
Multidomain proteins with two or more independently folded functional domains are prevalent in nature. Whereas most multidomain proteins are linked linearly in sequence, roughly one-tenth possess domain insertions where a guest domain is implanted in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff3481317aaf3f978e3d149a904e64d6
https://pubmed.ncbi.nlm.nih.gov/29490245
https://pubmed.ncbi.nlm.nih.gov/29490245
Autor:
Angela M. Gronenborn, Leonardus M. I. Koharudin, Ying Wu, Maria DeLucia, Jinwoo Ahn, Jennifer Mehrens
Publikováno v:
Journal of Biological Chemistry. 289:32617-32627
Sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) plays a critical role in inhibiting HIV infection, curtailing the pool of dNTPs available for reverse transcription of the viral genome. Recent structural data suggested a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c19c4bebaf0a03c9084702d6f8a7b224
https://doi.org/10.1074/jbc.m114.591958
https://doi.org/10.1074/jbc.m114.591958
Publikováno v:
Current Opinion in Virology. 7:95-100
A growing class of potential antivirals encompasses carbohydrate-binding proteins, such as antibodies and lectins. They block virus entry into host target cells and halt virus transmission from virus-infected cells to non-infected cells, thereby prev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17a4a50b743ebcbd946e6f37e0e9704a
https://doi.org/10.1016/j.coviro.2014.05.006
https://doi.org/10.1016/j.coviro.2014.05.006
Autor:
Sam Noppen, Dominique Schols, Leonardus M. I. Koharudin, Geoffrey Férir, Dana Huskens, Angela M. Gronenborn
Publikováno v:
Journal of Antimicrobial Chemotherapy. 69:2746-2758
OBJECTIVES Oscillatoria agardhii agglutinin homologue (OAAH) proteins belong to a recently discovered lectin family. The founding member OAA and a designed hybrid OAAH (OPA) recognize similar but unique carbohydrate structures of Man-9, compared with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf98f4fc4fb9f269298334194ee470f7
https://doi.org/10.1093/jac/dku220
https://doi.org/10.1093/jac/dku220
Autor:
Mingzhang Wang, Matthew Fritz, Tatyana Polenova, Guangjin Hou, Caitlin M. Quinn, Leonardus M. I. Koharudin, Angela M. Gronenborn, Xingyu Lu
Publikováno v:
The journal of physical chemistry. B. 121(15)
NMR chemical shifts are exquisitely sensitive probes for conformation and dynamics in molecules and supramolecular assemblies. Although isotropic chemical shifts are easily measured with high accuracy and precision in conventional NMR experiments, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a82ebd442ce7621034dc34d1acb8342
https://pubmed.ncbi.nlm.nih.gov/28001418
https://pubmed.ncbi.nlm.nih.gov/28001418
Autor:
Yiqi Qian, Shan Luan, Laura L. Thomas, Panayiotis V. Benos, Laurel Thomas, Gary Thomas, Angela M. Gronenborn, You-Jin Choi, Daniel L. Marks, Sylvain Auclair, Leonardus M. I. Koharudin, Stephanie M. Krasnow, Troy C. Krzysiak
Publikováno v:
Molecular Cell. 72:985-998.e7
Current models of SIRT1 enzymatic regulation primarily consider the effects of fluctuating levels of its co-substrate NAD+, which binds to the stably folded catalytic domain. By contrast, the roles of the sizeable disordered N- and C-terminal regions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49d64cf2e856ab27bf74bd5f46569c8b
https://doi.org/10.1016/j.molcel.2018.10.007
https://doi.org/10.1016/j.molcel.2018.10.007
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:1493-1498
Up to now, efforts to crystallize the cataract-associated P23T mutant of human γD-crystallin have not been successful. Therefore, insights into the light scattering mechanism of this mutant have been exclusively obtained from solution work. Here we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab55c0f724b4f990fddcf04f39352a95
https://doi.org/10.1002/prot.24321
https://doi.org/10.1002/prot.24321