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References from Peptide substrate optimization toward multiplex protease activity profiling under neutral pH conditions using Au microelectrode arrays. Local targets link to admitted publications; unresolved targets remain external evidence.
Site-selective cleavage of peptides and proteins targeting aromatic amino acid residues
10.1039/d4ra08956a · 2025 · External reference
Diagnostic and therapeutic potential of protease inhibition
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Inflammation, extracellular matrix remodeling, and proteostasis in tumor microenvironment
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Extracellular proteolysis in cancer: proteases, substrates, and mechanisms in tumor progression and metastasis
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Cysteine cathepsins: from structure, function and regulation to new frontiers
10.1016/j.bbapap.2011.10.002 · 2012 · External reference
Cysteine cathepsins and their extracellular roles: shaping the microenvironment
10.3390/cells8030264 · 2019 · External reference
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10.3390/ijms21249739 · 2020 · External reference
Insights into the role of matrix metalloproteinases in cancer and its various therapeutic aspects: a review
10.3389/fmolb.2022.896099 · 2022 · External reference
Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response
10.1038/nrc4027 · 2015 · External reference
ADAM proteases in cancer: biological roles, therapeutic challenges, and emerging opportunities
10.3390/cancers17101703 · 2025 · External reference
Novel ELISA for the specific detection of protease NEXIN-1 in human biological samples
10.1002/rth2.12756 · 2022 · External reference
Assay of matrix metalloproteases types 8 and 9 by ELISA in human breast cancer
10.1038/bjc.1995.197 · 1995 · External reference
Peptide probes for proteases - innovations and applications for monitoring proteolytic activity
10.1039/d1cs00798j · 2022 · External reference
Discovery of Leishmania druggable serine proteases by activity-based protein profiling
10.3389/fphar.2022.929493 · 2022 · External reference
Recent advances in activity-based probes (ABPs) and affinity-based probes (A BPs) for profiling of enzymes
10.1039/d1sc01359a · 2021 · External reference
Micro/Nano electrode array sensors: advances in fabrication and emerging applications in bioanalysis
10.3389/fchem.2020.573865 · 2020 · External reference
Trends and recent development of the microelectrode arrays (MEAs)
10.1016/j.bios.2020.112854 · 2021 · External reference
Recent developments in protease activity assays and sensors
10.1039/c6an02647h · 2017 · External reference
Electrochemical biosensors
10.1039/b714449k · 2010 · External reference
Electrochemical protease biosensor based on enhanced AC voltammetry using carbon Nanofiber Nanoelectrode arrays
10.1021/jp312031u · 2013 · External reference
Simultaneous, multiplex quantification of protease activities using a gold microelectrode array
10.1016/j.bios.2020.112330 · 2020 · External reference
Quantitative detection of cathepsin B activity in neutral pH buffers using gold microelectrode arrays: toward direct multiplex analyses of extracellular proteases in human serum
10.1021/acssensors.1c01175 · 2021 · External reference
Mitigating dithiothreitol interference to gold/thiol interface in electrochemical detection of cathepsin B activity toward multiplex protease analysis
2025 · External reference
Rapid and sensitive detection of the activity of ADAM17 using a graphene oxide-based fluorescence sensor
10.1039/c8an02344a · 2019 · External reference
Optimization of fluorescent substrates for ADAM17 and their utility in the detection of diabetes
10.1016/j.ab.2023.115337 · 2023 · External reference
Fluorescent probes towards selective cathepsin B detection and visualization in cancer cells and patient samples
10.1039/c9sc00997c · 2019 · External reference
JG26 attenuates ADAM17 metalloproteinase-mediated ACE2 receptor processing and SARS-CoV-2 infection in vitro
10.1007/s43440-024-00650-0 · 2025 · External reference
Electrochemical proteolytic beacon for detection of matrix metalloproteinase activities
10.1021/ja0626638 · 2006 · External reference
Sensors and regulators of intracellular pH
10.1038/nrm2820 · 2010 · External reference
Glucose dependent insulinotropic polypeptide and dipeptidyl peptidase inhibitors: their roles in management of type 2 diabetes mellitus
10.1016/j.dsx.2016.03.013 · 2016 · External reference
Cathepsin B Dipeptidyl carboxypeptidase and endopeptidase activities demonstrated across a broad pH range
10.1021/acs.biochem.2c00358 · 2022 · External reference
Distinct cleavage properties of cathepsin B compared to cysteine cathepsins enable the design and validation of a specific substrate for cathepsin B over a broad pH range
10.1021/acs.biochem.3c00139 · 2023 · External reference
Multiplex substrate profiling by mass spectrometry for proteases
10.1016/bs.mie.2022.09.009 · 2023 · External reference
Unresolved reference
2009 · External reference
Harnessing protein sensing ability of electrochemical biosensors via a controlled peptide receptor-electrode interface
10.1186/s12951-023-01843-0 · 2023 · External reference
Towards rational computational peptide design
10.3389/fbinf.2022.1046493 · 2022 · External reference
Leveraging machine learning models for peptide-protein interaction prediction
10.1039/d3cb00208j · 2024 · External reference
Cathepsin B
10.1016/s1357-2725(96)00152-5 · 1997 · External reference
Role of the occluding loop in cathepsin B activity
10.1074/jbc.272.2.1197 · 1997 · External reference
Lysosomal cysteine proteases: facts and opportunities
10.1093/emboj/20.17.4629 · 2001 · External reference
Cysteine cathepsins: multifunctional enzymes in cancer
10.1038/nrc1949 · 2006 · External reference
Cathepsin B: multiple roles in cancer
10.1002/prca.201300105 · 2014 · External reference
IL-4 induces cathepsin protease activity in tumor-associated macrophages to promote cancer growth and invasion
10.1101/gad.1874010 · 2010 · External reference
Selective neutral pH inhibitor of cathepsin B designed based on cleavage preferences at cytosolic and lysosomal pH conditions
10.1021/acschembio.1c00138 · 2021 · External reference
Fluorescent peptomer substrates for differential degradation by metalloproteases
10.1021/acs.biomac.2c01077 · 2022 · External reference
Clinical significance of serum cathepsin B and cystatin C levels and their ratio in the prognosis of patients with esophageal cancer
10.2147/ott.s123042 · 2017 · External reference
Cathepsin B, cathepsin H, cathepsin X and cystatin C in sera of patients with early-stage and inflammatory breast cancer
10.1177/172460080802300305 · 2008 · External reference
Cathepsin B: plasma expression and concentration in non-hodgkin lymphoma patients
10.3390/hemato6020013 · 2025 · External reference
Prognostic values of cathepsin B and carcinoembryonic antigen in sera of patients with colorectal cancer
1998 · External reference
Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library
10.1074/jbc.m004538200 · 2000 · External reference
Using peptide libraries to identify optimal cleavage motifs for proteolytic enzymes
10.1016/j.ymeth.2003.10.003 · 2004 · External reference
Characterization of the peptide substrate specificities of interstitial collagenase and 92-Kda gelatinase - implications for substrate optimization
10.1016/s0021-9258(20)30064-8 · 1994 · External reference
Fluorescence-quenched solid phase combinatorial libraries in the characterization of cysteine protease substrate specificity
10.1021/cc990031u · 1999 · External reference
Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides to define substrate specificity of carboxydipeptidases: assays with human cathepsin B
10.1016/j.ab.2004.09.012 · 2004 · External reference
Cathepsin B: active site mapping with peptidic substrates and inhibitors
10.1016/j.bmc.2018.10.017 · 2019 · External reference
A summary of the measured pK values of the ionizable groups in folded proteins
10.1002/pro.19 · 2009 · External reference
S2' substrate specificity and the role of His110 and His111 in the exopeptidase activity of human cathepsin B
10.1042/bj3610613 · 2002 · External reference
Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts
10.1021/bi971264+ · 1997 · External reference
Cathepsin B carboxydipeptidase specificity analysis using internally quenched fluorescent peptides
10.1042/bj20020840 · 2002 · External reference
Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: a basis for the design of specific epoxysuccinyl inhibitors
10.1021/bi00014a037 · 1995 · External reference
ColabFold: making protein folding accessible to all
10.1038/s41592-022-01488-1 · 2022 · External reference
CB-Dock2: improved protein-ligand blind docking by integrating cavity detection, docking and homologous template fitting
10.1093/nar/gkac394 · 2022 · External reference
AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
10.1002/jcc.21334 · 2010 · External reference
Inhibition of endogenous dentin matrix metalloproteinases by ethylenediaminetetraacetic acid
10.1016/j.joen.2011.09.005 · 2012 · External reference
Specificity determinants of human cathepsin s revealed by crystal structures of complexes
10.1021/bi027308i · 2003 · External reference
Substrate specificity of cysteine proteases beyond the S(2) pocket: mutagenesis and molecular dynamics investigation of Fasciola hepatica cathepsins L
10.3389/fmolb.2018.00040 · 2018 · External reference
