about
The crystal structure of Sporosarcina pasteurii urease in a complex with citrate provides new hints for inhibitor designAnalysis of pD-dependent complexation of N-benzyloxycarbonylaminophosphonic acids by alpha-cyclodextrin. Enantiodifferentiation of phosphonic acid pKa values.An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling.Bis(aminomethyl)phosphinic Acid, a Highly Promising Scaffold for the Development of Bacterial Urease Inhibitors.Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.A structural insight into the P1S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases.Urease inhibitors as potential drugs for gastric and urinary tract infections: a patent review.Peptide-based inhibitors of protein-protein interactions.Replacement of Thr32 and Gln34 in the C-terminal neuropeptide Y fragment 25-36 by cis-cyclobutane and cis-cyclopentane β-amino acids shifts selectivity toward the Y(4) receptor.1,2-Benzisoselenazol-3(2H)-one Derivatives As a New Class of Bacterial Urease Inhibitors.Aminophosphinates against Helicobacter pylori ureolysis-Biochemical and whole-cell inhibition characteristics.N-substituted aminomethanephosphonic and aminomethane-P-methylphosphinic acids as inhibitors of ureases.Plant P5C reductase as a new target for aminomethylenebisphosphonates.Potent covalent inhibitors of bacterial urease identified by activity-reactivity profiling.Computer-aided optimization of phosphinic inhibitors of bacterial ureases.Effectiveness and mode of action of phosphonate inhibitors of plant glutamine synthetase.Herbicidal pyridyl derivatives of aminomethylene-bisphosphonic acid inhibit plant glutamine synthetase.Synthesis and evaluation of effective inhibitors of plant δ1-pyrroline-5-carboxylate reductase.Enantiodifferentiation of alpha-hydroxyalkanephosphonic acids in 31P NMR with application of alpha-cyclodextrin as chiral discriminating agent.Design, synthesis, and evaluation of novel organophosphorus inhibitors of bacterial ureases.Tailoring the structure of aminobisphosphonates to target plant P5C reductase.Design, synthesis, and activity of analogues of phosphinothricin as inhibitors of glutamine synthetase.Phosphinothricin analogues as inhibitors of plant glutamine synthetases.Computer-aided analysis of the interactions of glutamine synthetase with its inhibitors.Sequence Engineering to Control the Helix Handedness of Peptide Foldamers.Bioactive Macrocyclic Inhibitors of the PD-1/PD-L1 Immune Checkpoint.Controlling the Helix Handedness of ααβ-Peptide Foldamers through Sequence Shifting.Discovery of new leads against Mycobacterium tuberculosis using scaffold hopping and shape based similarity.Peptides containing β-amino acid patterns: challenges and successes in medicinal chemistry.Novel organophosphorus scaffolds of urease inhibitors obtained by substitution of Morita-Baylis-Hillman adducts with phosphorus nucleophiles.Phytotoxicity of aminobisphosphonates targeting both δ1 -pyrroline-5-carboxylate reductase and glutamine synthetase.Structural exploration of cinnamate-based phosphonic acids as inhibitors of bacterial ureasesUnique α,β- and α,α,β,β-Peptide Foldamers Based on cis-β-Aminocyclopentanecarboxylic AcidBisphosphonic acids and related compounds as inhibitors of nucleotide- and polyphosphate-processing enzymes: A PPK1 and PPK2 case study.Zwitterionic Phosphorylated Quinines as Chiral Solvating Agents for NMR SpectroscopyPhosphorylation as a method of tuning the enantiodiscrimination potency of quinine-An NMR studyEnantiodifferentiation of N-benzyloxycarbonylaminophosphonic and phosphinic acids and their esters using cyclodextrins by means of capillary electrophoresisRemarkable potential of the α-aminophosphonate/phosphinate structural motif in medicinal chemistryBisphosphonic acids as effective inhibitors of Mycobacterium tuberculosis glutamine synthetaseToward very potent, non-covalent organophosphonate inhibitors of cathepsin C and related enzymes by 2-amino-1-hydroxy-alkanephosphonates dipeptides
P50
Q27684000-2DA759E1-3199-4789-B0D0-7C190A307CE0Q31120246-7FE86419-D00B-440B-8EF2-BB750F00C541Q34468476-758FF0A1-1352-4EF8-BCFC-F5DCE3B84ECBQ35086742-55D2B439-7B06-47FB-9F3A-3799BDDD2AE1Q35090932-6C6934F8-BB5D-4346-BD5E-98C8DFD88272Q36902177-52FE370A-E5B4-40B7-AA87-95D4F7574D7FQ37860345-D38AFC86-D060-4FD8-82A1-E4E7892E6531Q38695874-2DED9241-DAC2-489E-AB91-95D7C7AE99FAQ39340149-69284427-D69B-4619-ABF9-05D1EF807666Q40576160-861F0422-49B3-47B4-8890-F9153A114F2CQ41327355-F3B93D06-6BFF-43A7-902B-ED3D5A19F707Q42083395-F7172A5B-0769-44C6-826B-4ED344629762Q42619034-37391D42-E4FA-4841-BF54-47EB8E7DB21AQ42802570-59353887-3A5C-4503-A625-90CDC539BB03Q42946894-4430169F-2003-43B8-86DB-FFDDBB602851Q43288247-DCE9EB20-1654-4B80-A825-B33DFA85E75BQ44908917-FBBC1D36-03F3-4119-B3F9-CB32A23F4C93Q46052694-D9D87A19-C526-4A50-8439-8485CD1EA78EQ46078656-BB6BB35B-7693-4838-8855-2E809E35D65FQ46418827-F4ACC821-93E9-4E28-B5BB-50E1E8420016Q46655163-177D2C22-4E82-4EB3-9B62-23F8B4C59A7CQ46725642-53D6B396-A718-4FE2-8C68-BE50F8975713Q46920421-591C6884-D23B-4014-BD08-1FD40D8C555CQ46965815-D10D1383-3BEC-49DD-B27E-D0B83ADBAD4EQ47719434-F052E48E-D433-4F54-80FC-C4B4F7BB27A5Q47842052-8E55A397-34AC-480B-81AA-DF9540AC5428Q48359838-37B26349-231B-44C5-AF60-7E9587BCC52EQ50161318-5BDAD27F-7683-4504-A35D-ABAA43AD4634Q51055342-AC693E2C-80AC-44A4-BEAE-5BA05DB8602FQ53373711-32A49FC0-3810-4EC2-BE96-C2B80C8446C1Q53616276-568D6E9F-67A8-4EAB-827F-15D4D761AEF8Q57298273-0CB8C756-E911-474A-B3BB-E43827F2A0EEQ58214113-AEC4C4A3-77BF-40BE-B46A-766D432D51B0Q59288080-9A3D1746-BDD3-4649-9C9C-2B094F5242D4Q62631557-60AA9D5F-C42B-405B-A2D4-BE64A16CACA5Q62631564-54A6B205-9EEB-4925-85E3-22DF49808E94Q62631600-FD9DFB94-4D9E-4D1A-8BFF-6DD84FA99945Q84585122-548426C0-FE8C-4F8A-95FF-A72A85B7A5DDQ85701656-30784744-1565-46F6-98EB-74902E2889C5Q86860319-BC0B1BCA-9425-49CD-994F-02334DE29104
P50
description
Polish biochemist
@en
Pools onderzoeker
@nl
bithchemiceoir Polannach
@ga
investigador polacu
@ast
polnischer Forscher
@de
polski biochemik
@pl
name
Łukasz Berlicki
@ast
Łukasz Berlicki
@ca
Łukasz Berlicki
@de
Łukasz Berlicki
@en
Łukasz Berlicki
@es
Łukasz Berlicki
@fr
Łukasz Berlicki
@ga
Łukasz Berlicki
@it
Łukasz Berlicki
@nl
Łukasz Berlicki
@pl
type
label
Łukasz Berlicki
@ast
Łukasz Berlicki
@ca
Łukasz Berlicki
@de
Łukasz Berlicki
@en
Łukasz Berlicki
@es
Łukasz Berlicki
@fr
Łukasz Berlicki
@ga
Łukasz Berlicki
@it
Łukasz Berlicki
@nl
Łukasz Berlicki
@pl
altLabel
Lukasz Berlicki
@en
prefLabel
Łukasz Berlicki
@ast
Łukasz Berlicki
@ca
Łukasz Berlicki
@de
Łukasz Berlicki
@en
Łukasz Berlicki
@es
Łukasz Berlicki
@fr
Łukasz Berlicki
@ga
Łukasz Berlicki
@it
Łukasz Berlicki
@nl
Łukasz Berlicki
@pl
P101
P1153
6507332551
P1559
Łukasz Berlicki
@pl
P21
P27
P31
P3124
P3835
lukasz-berlicki
P496
0000-0003-0318-4944