نتائج البحث

1

Discovery of potent BET bromodomain 1 stereoselective inhibitors using DNA-encoded chemical library selections

المصدر: Proceedings of the National Academy of Sciences of the United States of America. 119(22)

مصطلحات موضوعية: Male, Small Molecule Libraries, Structure-Activity Relationship, Multidisciplinary, Protein Domains, Anti-Inflammatory Agents, Non-Steroidal, Drug Discovery, Contraceptive Agents, Male, Humans, Nuclear Proteins, Antineoplastic Agents, DNA

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79a851d4e692ff7c8340bbbd30abba30Test
https://pubmed.ncbi.nlm.nih.gov/35622893Test

2

Discovery and characterization of bromodomain 2-specific inhibitors of BRDT

المؤلفون: Justin L. Anglin, Kevin Riehle, John C. Faver, Marta Storl-Desmond, Rajesh Sharma, Damian W. Young, Melek N. Ucisik, Gundeep Kaur, Feng Li, Choel Kim, Kiran L. Sharma, Nicholas Simmons, Zhifeng Yu, Sureshbabu Nagarajan, Martin M. Matzuk, Pranavanand Nyshadham, Stephen Palmer, Banumathi Sankaran, Angela F. Ku

المصدر: Proceedings of the National Academy of Sciences of the United States of America, vol 118, iss 9
Proceedings of the National Academy of Sciences of the United States of America

مصطلحات موضوعية: Protein Conformation, alpha-Helical, Male, Subfamily, Protein Conformation, Gene Expression, Quantitative Structure-Activity Relationship, Cell Cycle Proteins, Crystallography, X-Ray, Ligands, 01 natural sciences, Biochemistry, Mice, Testis, Drug Discovery, Cloning, Molecular, Cancer, 0303 health sciences, Multidisciplinary, Crystallography, Chemistry, Nuclear Proteins, Azepines, Biological Sciences, Small molecule, Recombinant Proteins, Molecular Docking Simulation, small-molecule inhibitors, Knockout mouse, Protein Binding, BRD4, Genetic Vectors, 03 medical and health sciences, DNA-encoded chemistry, Contraceptive Agents, In vivo, Escherichia coli, Genetics, Potency, Animals, Humans, Protein Interaction Domains and Motifs, 030304 developmental biology, BET bromodomains, Binding Sites, 010405 organic chemistry, Contraception/Reproduction, alpha-Helical, Contraceptive Agents, Male, Molecular, Triazoles, In vitro, 0104 chemical sciences, Bromodomain, High-Throughput Screening Assays, male contraceptive, X-Ray, Protein Conformation, beta-Strand, beta-Strand, Transcription Factors, Cloning

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a47b29b36c4d8ecbdaff9fff6156c7cTest
https://escholarship.org/uc/item/9t49g9frTest

3

Liquid condensation of reprogramming factor KLF4 with DNA provides a mechanism for chromatin organization

المؤلفون: Choel Kim, Banumathi Sankaran, Jean J Kim, Kyoung-Jae Choi, Rajesh Sharma, Kevin R. MacKenzie, Sonum Sharma, Josephine C. Ferreon, Allan Chris M. Ferreon, My Diem Quan, Hyekyung Park, Anel LaGrone

المصدر: Nature Communications
Nature communications, vol 12, iss 1
Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021)

مصطلحات موضوعية: Models, Molecular, General Physics and Astronomy, Transcription (biology), Models, Promoter Regions, Genetic, Multidisciplinary, Chemistry, Zinc Fingers, Nanog Homeobox Protein, Cellular Reprogramming, Chromatin, Cell biology, embryonic structures, DNA methylation, biological phenomena, cell phenomena, and immunity, Reprogramming, Transcription, Science, Kruppel-Like Transcription Factors, General Biochemistry, Genetics and Molecular Biology, Article, Cell Line, Promoter Regions, Kruppel-Like Factor 4, stomatognathic system, Genetic, Genetics, Transcription factors, Humans, Protein Interaction Domains and Motifs, Epigenetics, Enhancer, Transcription factor, Cell Nucleus, Base Sequence, SOXB1 Transcription Factors, fungi, Human Genome, Molecular, General Chemistry, DNA-binding domain, DNA, DNA Methylation, Stem Cell Research, Mutation, sense organs, Generic health relevance, Octamer Transcription Factor-3

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::453c720582ced092e0600872a1a48214Test
https://pubmed.ncbi.nlm.nih.gov/34552088Test

4

A substitution in cGMP-dependent protein kinase 1 associated with aortic disease induces an active conformation in the absence of cGMP

المؤلفون: Darren E. Casteel, Choel Kim, Renate B. Pilz, Amatya Taran, Sheng Li, Sahar Aminzai, Tingfei Hu, Matthew Chan

المصدر: J Biol Chem
The Journal of biological chemistry, vol 295, iss 30

مصطلحات موضوعية: 0301 basic medicine, CGMP-Dependent Protein Kinase 1, Thoracic, Cardiovascular, Biochemistry, Medical and Health Sciences, 2.1 Biological and endogenous factors, Aetiology, Phosphorylation, Cyclic GMP-Dependent Protein Kinase Type I, thoracic aortic aneurysm and dissection, CGMP binding, Kinase, Chemistry, Autophosphorylation, kinase signaling, Biological Sciences, Enzyme structure, Aortic Aneurysm, enzyme structure, hydrogen exchange mass spectrometry, Protein Structure and Folding, autophosphorylation, mutagenesis, Leucine zipper, Protein Structure, Biochemistry & Molecular Biology, deuterium exchange, hydrogen/deuterium exchange, Mutation, Missense, Cell Line, Quaternary, 03 medical and health sciences, cyclic GMP, Genetics, Humans, mutant, Kinase activity, Protein kinase A, Protein Structure, Quaternary, Molecular Biology, 030102 biochemistry & molecular biology, protein kinase G, Aortic Aneurysm, Thoracic, Cell Biology, Molecular biology, Aneurysm, Aortic Dissection, 030104 developmental biology, Amino Acid Substitution, hydrogen, Mutation, Chemical Sciences, cardiovascular system, Missense, Protein Multimerization, Dissecting

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::191849eab750aff14c357b96d0115868Test
https://pubmed.ncbi.nlm.nih.gov/32506052Test

5

Neutron Crystallography Detects Differences in Protein Dynamics: Structure of the PKG II Cyclic Nucleotide Binding Domain in Complex with an Activator

المؤلفون: James C. Campbell, Matthew P. Blakeley, Andrey Kovalevsky, Oksana Gerlits, Choel Kim

المصدر: Biochemistry. 57:1833-1837

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::665b0512550bf25b17b94236306854d1Test
https://doi.org/10.1021/acs.biochem.8b00010Test

6

Structural Basis of Analog Specificity in PKG I and II

المؤلفون: James C. Campbell, Eugen Franz, Choel Kim, Friedrich W. Herberg, Philipp Henning, Banumathi Sankaran

المصدر: ACS Chemical Biology. 12:2388-2398

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d397dcbc40ba4b8f6def9384f7975348Test
https://doi.org/10.1021/acschembio.7b00369Test

7

AMPK and Endothelial Nitric Oxide Synthase Signaling Regulates K-Ras Plasma Membrane Interactions via Cyclic GMP-Dependent Protein Kinase 2

المؤلفون: Darren E. Casteel, Priyanka Prakash, Alemayehu A. Gorfe, Choel Kim, Robert J. Capon, Ernest Lacey, Angela A. Salim, Dharini van der Hoeven, Shane R. Cunha, Kwang Jin Cho, John F. Hancock, Lingxiao Tan

المصدر: Molecular and Cellular Biology. 36:3086-3099

مصطلحات موضوعية: 0301 basic medicine, Lung Neoplasms, Nitric Oxide Synthase Type III, Endocytic recycling, Cyclic GMP-Dependent Protein Kinase Type II, AMP-Activated Protein Kinases, Biology, Nitric Oxide, Sildenafil Citrate, Cell Line, Madin Darby Canine Kidney Cells, Nitric oxide, 03 medical and health sciences, chemistry.chemical_compound, Dogs, 0302 clinical medicine, Carcinoma, Non-Small-Cell Lung, Cell Line, Tumor, Serine, Animals, Humans, Phosphorylation, Protein kinase A, Molecular Biology, Cell Proliferation, Kinase, Cell Membrane, AMPK, Articles, Cell Biology, Endocytosis, Cell biology, Gene Expression Regulation, Neoplastic, 030104 developmental biology, chemistry, 030220 oncology & carcinogenesis, ras Proteins, Signal transduction, Soluble guanylyl cyclase, Signal Transduction

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::859d3f8fc2c223d949127e0e56ba12d8Test
https://doi.org/10.1128/mcb.00365-16Test

8

FRET-based cyclic GMP biosensors measure low cGMP concentrations in cardiomyocytes and neurons

المؤلفون: Lise Román Moltzau, Andrea Hembre Ulsund, Jeong Joo Kim, Marianne Bjørnerem, Finn Olav Levy, Oliver C. Neely, Dan Li, Kjetil Wessel Andressen, Gaia Calamera, Choel Kim, David J. Paterson

المصدر: Communications Biology
Communications Biology, Vol 2, Iss 1, Pp 1-12 (2019)

مصطلحات موضوعية: 0301 basic medicine, Male, Models, Molecular, Cell signaling, Recombinant Fusion Proteins, Plasmodium falciparum, Protozoan Proteins, Medicine (miscellaneous), Biosensing Techniques, macromolecular substances, Cellular imaging, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, 0302 clinical medicine, Soluble Guanylyl Cyclase, Computer Systems, Membrane proteins, Cyclic GMP-Dependent Protein Kinases, Fluorescence Resonance Energy Transfer, Animals, Humans, Nucleotide, Myocytes, Cardiac, Rats, Wistar, Protein kinase A, lcsh:QH301-705.5, Cyclic GMP, chemistry.chemical_classification, Neurons, Chemistry, technology, industry, and agriculture, Fluorescent proteins, 3. Good health, 030104 developmental biology, Förster resonance energy transfer, HEK293 Cells, lcsh:Biology (General), Cyclic nucleotide-binding domain, Guanylate Cyclase, Biophysics, Single-Cell Analysis, General Agricultural and Biological Sciences, Soluble guanylyl cyclase, Biosensor, 030217 neurology & neurosurgery, Intracellular, Cell signalling

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f359e72d39705af2d461a133223e554Test
http://hdl.handle.net/10852/75288Test

9

Crystal Structure of PKG I:cGMP Complex Reveals a cGMP-Mediated Dimeric Interface that Facilitates cGMP-Induced Activation

المؤلفون: Robin Lorenz, Albert S. Reger, Jeong Joo Kim, Darren E. Casteel, Stefan T. Arold, Banumathi Sankaran, Choel Kim, Friedrich W. Herberg

المصدر: Structure (London, England : 1993), vol 24, iss 5
Kim, JJ; Lorenz, R; Arold, ST; Reger, AS; Sankaran, B; Casteel, DE; et al.(2016). Crystal Structure of PKG I:cGMP Complex Reveals a cGMP-Mediated Dimeric Interface that Facilitates cGMP-Induced Activation. Structure, 24(5), 710-720. doi: 10.1016/j.str.2016.03.009. Lawrence Berkeley National Laboratory: Lawrence Berkeley National Laboratory. Retrieved from: http://www.escholarship.org/uc/item/8q56g7g4Test

مصطلحات موضوعية: 0301 basic medicine, crystal structure, second messengers, 1.1 Normal biological development and functioning, allosteric activation, Allosteric regulation, Biophysics, Plasma protein binding, Molecular Dynamics Simulation, Crystallography, X-Ray, Article, 03 medical and health sciences, chemistry.chemical_compound, NO-cGMP signaling, Underpinning research, Structural Biology, Information and Computing Sciences, cyclic nucleotide-binding domain, Humans, 2.1 Biological and endogenous factors, Aetiology, Binding site, Protein kinase A, Cyclic GMP, Molecular Biology, Cyclic guanosine monophosphate, Cyclic GMP-Dependent Protein Kinase Type I, Crystallography, Binding Sites, 030102 biochemistry & molecular biology, Chemistry, Biological Sciences, Cell biology, Molecular Docking Simulation, 030104 developmental biology, Cyclic nucleotide-binding domain, cGMP-dependent protein kinase, small-angle X-ray scattering, Chemical Sciences, Second messenger system, cardiovascular system, X-Ray, Protein Multimerization, Protein Binding

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2fb2e3ab12b4c73bc1c9f951f34d814Test
https://doi.org/10.1016/j.str.2016.03.009Test

10

Structural basis for selective inhibition of human PKG Iα by the balanol-like compound N46

المؤلفون: Choel Kim, Darren E. Casteel, Sahar Aminzai, Liying Qin, Banumathi Sankaran

المصدر: Qin, L; Sankaran, B; Aminzai, S; Casteel, DE; & Kim, C. (2018). Structural basis for selective inhibition of human PKG Iα by the balanol-like compound N46. Journal of Biological Chemistry, 293(28), 10985-10992. doi: 10.1074/jbc.RA118.002427. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/3096c18dTest
The Journal of biological chemistry, vol 293, iss 28

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, protein–ligand complex, Protein Conformation, Crystallography, X-Ray, Biochemistry, Medical and Health Sciences, nonopioid analgesics, chemistry.chemical_compound, 0302 clinical medicine, Models, Catalytic Domain, Hydroxybenzoates, 2.1 Biological and endogenous factors, Phosphorylation, Cyclic GMP-Dependent Protein Kinase Type I, Crystallography, biology, Pain Research, Azepines, Biological Sciences, inhibitor, cardiovascular system, Chronic Pain, Signal Transduction, Steric effects, crystal structure, Biochemistry & Molecular Biology, Stereochemistry, drug design, Balanol, Hydrophobic effect, 03 medical and health sciences, cyclic GMP, Humans, Protein kinase A, Molecular Biology, IC50, ATP competitive inhibitor, inhibitor specificity, protein kinase G, protein-ligand complex, Active site, Molecular, Cell Biology, 030104 developmental biology, chemistry, Helix, Chemical Sciences, biology.protein, X-Ray, cGMP-dependent protein kinase, 030217 neurology & neurosurgery

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b24fa8960a4c930e6c18404a6592d8e5Test
http://www.escholarship.org/uc/item/3096c18dTest

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