| Year |
Citation |
Score |
| 2024 |
Karalia S, Meena VK, Kumar V. Deciphering structural variation upon biotinylation of biotin carboxyl carrier protein domain in Streptococcus pneumoniae. International Journal of Biological Macromolecules. 133580. PMID 38960227 DOI: 10.1016/j.ijbiomac.2024.133580 |
0.339 |
|
| 2023 |
Mack AR, Kumar V, Taracila MA, Mojica MF, O'Shea M, Schinabeck W, Silver G, Hujer AM, Papp-Wallace KM, Chen S, Haider S, Caselli E, Prati F, van den Akker F, Bonomo RA. Natural protein engineering in the Ω-loop: the role of Y221 in ceftazidime and ceftolozane resistance in -derived cephalosporinase. Antimicrobial Agents and Chemotherapy. e0079123. PMID 37850746 DOI: 10.1128/aac.00791-23 |
0.651 |
|
| 2023 |
Kumar V, Boorman J, Greenlee WJ, Zeng X, Lin J, van den Akker F. Exploring the inhibition of the soluble lytic transglycosylase Cj0843c of Campylobacter jejuni via targeting different sites with different scaffolds. Protein Science : a Publication of the Protein Society. e4683. PMID 37209283 DOI: 10.1002/pro.4683 |
0.655 |
|
| 2021 |
Kumar V, Viviani SL, Ismail J, Agarwal S, Bonomo RA, van den Akker F. Structural analysis of the boronic acid β-lactamase inhibitor vaborbactam binding to Pseudomonas aeruginosa penicillin-binding protein 3. Plos One. 16: e0258359. PMID 34653211 DOI: 10.1371/journal.pone.0258359 |
0.679 |
|
| 2021 |
Goldberg JA, Kumar V, Spencer EJ, Hoyer D, Marshall SH, Hujer AM, Hujer KM, Bethel CR, Papp-Wallace KM, Perez F, Jacobs MR, van Duin D, Kreiswirth BN, van den Akker F, Plummer MS, et al. A γ-lactam siderophore antibiotic effective against multidrug-resistant Pseudomonas aeruginosa, Klebsiella pneumoniae, and Acinetobacter spp. European Journal of Medicinal Chemistry. 220: 113436. PMID 33933754 DOI: 10.1016/j.ejmech.2021.113436 |
0.635 |
|
| 2021 |
Hahn MG, Lampe T, El Sheikh S, Griebenow N, Woltering E, Schlemmer KH, Dietz L, Gerisch M, Wunder F, Becker-Pelster EM, Mondritzki T, Tinel H, Knorr A, Kern A, Lang D, ... ... Kumar V, et al. Discovery of the Soluble Guanylate Cyclase Activator Runcaciguat (BAY 1101042). Journal of Medicinal Chemistry. PMID 33872507 DOI: 10.1021/acs.jmedchem.0c02154 |
0.603 |
|
| 2021 |
Kumar V, Mathure SA, Lee M, Boorman J, Zeng X, Lin J, Hesek D, Lastochkin E, Mobashery S, van den Akker F. Turnover Chemistry and Structural Characterization of the Cj0843c Lytic Transglycosylase of . Biochemistry. PMID 33749238 DOI: 10.1021/acs.biochem.1c00027 |
0.635 |
|
| 2021 |
Rajavel M, Kumar V, Nguyen H, Wyatt J, Marshall SH, Papp-Wallace KM, Deshpande P, Bhavsar S, Yeole R, Bhagwat S, Patel M, Bonomo RA, van den Akker F. Structural Characterization of Diazabicyclooctane β-Lactam "Enhancers" in Complex with Penicillin-Binding Proteins PBP2 and PBP3 of Pseudomonas aeruginosa. Mbio. 12. PMID 33593978 DOI: 10.1128/mBio.03058-20 |
0.731 |
|
| 2020 |
Goldberg J, Nguyen H, Kumar V, Spencer E, Hoyer D, Marshall E, Cmolik A, O'Shea M, Marshall S, Hujer A, Hujer K, Rudin SD, Domitrovic TN, Bethel C, Papp-Wallace KM, et al. A γ-Lactam Siderophore Antibiotic Effective Against Multidrug-Resistant Gram-Negative Bacilli. Journal of Medicinal Chemistry. PMID 32420736 DOI: 10.1021/acs.jmedchem.0c00255 |
0.641 |
|
| 2020 |
Kumar V, Tang C, Bethel CR, Papp-Wallace KM, Wyatt J, Desarbre E, Bonomo RA, van den Akker F. Structural insights into ceftobiprole inhibition of penicillin-binding protein 3. Antimicrobial Agents and Chemotherapy. PMID 32152075 DOI: 10.1128/AAC.00106-20 |
0.699 |
|
| 2019 |
Papp-Wallace KM, Kumar V, Zeiser ET, Becka SA, van den Akker F. Structural Analysis of The OXA-48 Carbapenemase Bound to A "Poor" Carbapenem Substrate, Doripenem. Antibiotics (Basel, Switzerland). 8. PMID 31514291 DOI: 10.3390/antibiotics8030145 |
0.664 |
|
| 2019 |
Barnes MD, Kumar V, Bethel CR, Moussa SH, O'Donnell J, Rutter JD, Good CE, Hujer KM, Hujer AM, Marshall SH, Kreiswirth BN, Richter SS, Rather PN, Jacobs MR, Papp-Wallace KM, et al. Targeting Multidrug-Resistant spp.: Sulbactam and the Diazabicyclooctenone β-Lactamase Inhibitor ETX2514 as a Novel Therapeutic Agent. Mbio. 10. PMID 30862744 DOI: 10.1128/Mbio.00159-19 |
0.634 |
|
| 2018 |
Vijayaraghavan J, Kumar V, Krishnan NP, Kaufhold RT, Zeng X, Lin J, van den Akker F. Structural studies and molecular dynamics simulations suggest a processive mechanism of exolytic lytic transglycosylase from Campylobacter jejuni. Plos One. 13: e0197136. PMID 29758058 DOI: 10.1371/journal.pone.0197136 |
0.699 |
|
| 2018 |
Papp-Wallace KM, Nguyen NQ, Jacobs MR, Bethel CR, Barnes MD, Kumar V, Bajaksouzian S, Rudin SD, Rather PN, Bhavsar S, Ravikumar T, Deshpande PK, Patil V, Yeole R, Bhagwat SS, et al. Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234. Journal of Medicinal Chemistry. PMID 29627985 DOI: 10.1021/Acs.Jmedchem.8B00091 |
0.641 |
|
| 2017 |
Pratap S, Dev A, Kumar V, Yadav R, Narwal M, Tomar S, Kumar P. Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals Conformational Plasticity of Active Site. Scientific Reports. 7: 6364. PMID 28743924 DOI: 10.1038/s41598-017-06578-1 |
0.363 |
|
| 2013 |
von Wantoch Rekowski M, Kumar V, Zhou Z, Moschner J, Marazioti A, Bantzi M, Spyroulias GA, van den Akker F, Giannis A, Papapetropoulos A. Insights into soluble guanylyl cyclase activation derived from improved heme-mimetics. Journal of Medicinal Chemistry. 56: 8948-52. PMID 24090476 DOI: 10.1021/jm400539d |
0.659 |
|
| 2013 |
Kumar V, Martin F, Hahn MG, Schaefer M, Stamler JS, Stasch JP, van den Akker F. Insights into BAY 60-2770 activation and S-nitrosylation-dependent desensitization of soluble guanylyl cyclase via crystal structures of homologous nostoc H-NOX domain complexes. Biochemistry. 52: 3601-8. PMID 23614626 DOI: 10.1021/Bi301657W |
0.711 |
|
| 2011 |
van den Akker F, Martin F, Kumar V, Ma X, Stasch J, Schaefer M, Baskaran P, Beuve A, van Dunten PW. Structural insights into sGC activation by different activators Bmc Pharmacology. 11. DOI: 10.1186/1471-2210-11-S1-O11 |
0.691 |
|
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