PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3318115-2	1987	Recently the factors, contributing to dipeptidyl carboxypeptidase properties of brain cathepsin B, were identified: I. occupation of the enzyme S3 subsite, 2. free C-terminal group of the substrate, 3. specific interaction between the split off dipeptide and the enzyme active site.	Dipeptides	245-254	cathepsin B	Homo sapiens	86-97	
3318115-6	1987	Cathepsin B split off the C-terminal dipeptide in synthetic substrates Leu-Trp-Met-Arg-Phe-Ala and Trp-Met-Arg-Phe-Ala but not in Met-Arg-Phe-Ala.	Dipeptides	37-46	cathepsin B	Homo sapiens	0-11	
23712251-5	2013	These dipeptide mimetics appear also to be potent inhibitors of other cysteine proteases such as papain, cathepsin B and cathepsin K, thus providing new leading structures for these medicinally important enzymes.	Dipeptides	6-15	cathepsin B	Homo sapiens	105-116	
31184188-2	2019	The new probe consists of (1) octreotide as a synthetic ligand of somatostatin receptors, (2) a H2O2-responsive phenylboronic acid, (3) a dipeptide substrate for cathepsin B, and (4) a NIR fluorophore.	Dipeptides	138-147	cathepsin B	Homo sapiens	162-173	
31156276-0	2018	Improved Methodology for the Synthesis of a Cathepsin B Cleavable Dipeptide Linker, Widely Used in Antibody-Drug Conjugate Research.	Dipeptides	66-75	cathepsin B	Homo sapiens	44-55	
666735-5	1978	Measurement of the rate of formation of the products showed that cathepsin B degraded glucagon by a sequential cleavage of dipeptides from the C-terminal end of the molecule.	Dipeptides	123-133	cathepsin B	Homo sapiens	65-76	
32798638-2	2020	Here, model drug monomethyl auristatin E (MMAE) was conjugated ex vivo to Cys34 of albumin via a cathepsin B-sensitive dipeptide linker to ensure that all drug would be bound specifically to albumin.	Dipeptides	119-128	cathepsin B	Homo sapiens	97-108	
29473076-2	2018	These linkers vary by both cleavable trigger motif and hydrophilicity, containing one of two cathepsin B sensitive dipeptides (Val-Cit and Val-Ala), and engendered with either hydrophilic or hydrophobic character via application of a PEG12 spacer.	Dipeptides	115-125	cathepsin B	Homo sapiens	93-104	
29123088-4	2017	By connecting a tumor-targeting nucleolin aptamer (NucA) to the active hydroxyl group at 2" position of PTX via a cathepsin B sensitive dipeptide bond, NucA-PTX remains stable and inactive in the circulation.	Dipeptides	136-145	cathepsin B	Homo sapiens	114-125	
29123088-6	2017	Once inside cells, the dipeptide bond linker of NucA-PTX is cleaved by cathepsin B and then the conjugated PTX is released for action.	Dipeptides	23-32	cathepsin B	Homo sapiens	71-82	
23903896-3	2014	In order to further enhance the anticancer effect of OFA, anti-CD20 OFA has been conjugated with highly cytotoxic monomethyl auristatin E (MMAE) through a cathepsin-B-cleavable valine-citrulline (vc) dipeptide linkage to form OFA-vcMMAE and the anti-tumor activity of OFA-vcMMAE against CD20-positive B lymphoma cells are then evaluated in vitro and in vivo.	Dipeptides	200-209	cathepsin B	Homo sapiens	155-166	
24900316-3	2011	Further, utilizing the 4-substituted colchicines, we prepared pro-drugs having a dipeptide side chain and demonstrated that these pro-drugs were activated by cathepsin B, an enzyme overexpressed in tumor cells, and exhibited selective toxicity to the tumor cells.	Dipeptides	81-90	cathepsin B	Homo sapiens	158-169	
19199576-2	2009	The linker consists of a carboxyl group in one arm and an activated 1,6-self-immolative para-aminobenzyloxycarbonyl spacer together with a cathepsin B cleavable dipeptide Phe-Lys in the other.	Dipeptides	161-170	cathepsin B	Homo sapiens	139-150	
19131246-2	2009	Additionally, the prodrug contains a 1,6-self-immolative spacer coupled to the dipeptide Phe-Lys that acts as a substrate for cathepsin B.	Dipeptides	79-88	cathepsin B	Homo sapiens	126-137	
9873731-0	1998	Cathepsin B-sensitive dipeptide prodrugs.	Dipeptides	22-31	cathepsin B	Homo sapiens	0-11	
12121142-0	2002	Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer activity.	Dipeptides	19-28	cathepsin B	Homo sapiens	0-11	
11802791-1	2002	The ability of the lysosomal cysteine protease cathepsin B to function as a peptidyldipeptidase (removing C-terminal dipeptides) has been attributed to the presence of two histidine residues (His(110) and His(111)) present in the occluding loop, an extra peptide segment located in the primed side of the active-site cleft.	Dipeptides	117-127	cathepsin B	Homo sapiens	47-58	
11802791-6	2002	These studies showed that cathepsin B is optimized to act as an exopeptidase, cleaving dipeptides from protein substrates in a successive manner, because of its relaxed specificity in P2" and its other subsites.	Dipeptides	87-97	cathepsin B	Homo sapiens	26-37	
10841792-3	2000	Stabilization of lead compounds against cathepsin B cleavage by N-methylation of noncritical backbone NH groups or by dipeptide mimetic substitutions has generated analogues that compete effectively against protein antigens in cellular assays, resulting in inhibition of T-cell proliferation.	Dipeptides	118-127	cathepsin B	Homo sapiens	40-51	
9873732-0	1998	Cathepsin B-sensitive dipeptide prodrugs.	Dipeptides	22-31	cathepsin B	Homo sapiens	0-11	
9873732-3	1998	Substrates containing doxorubicin (DOX), paclitaxel (taxol), and mitomycin C (MMC) attached to the cathepsin B-sensitive dipeptide Phe-Lys via a self-immolative spacer were prepared as model compounds for internalizing anticancer immunoconjugates.	Dipeptides	121-130	cathepsin B	Homo sapiens	99-110	
8230139-4	1993	Extending the dipeptide alpha-keto ester to a tripeptide alpha-keto ester yielded significant enhancement in the inhibitory potency toward cathepsin B, but smaller changes toward the calpains.	Dipeptides	14-23	cathepsin B	Homo sapiens	139-150	
8754751-7	1996	Lysosomal dipeptidase I alone had no effect on 20 kDa but acted in combination with cathepsin B to release T4 from the T4-Gln dipeptide.	Dipeptides	126-135	cathepsin B	Homo sapiens	84-95	
8754751-10	1996	We conclude that the N-terminus of Tg, which contains its major hormonogenic site, is particularly susceptible to hydrolysis by the endopeptidase cathepsin B and that cathepsin B additionally has an important exopeptidase action that allows it to release a T4 dipeptide that is then further degraded by LDPI to release free T4.	Dipeptides	260-269	cathepsin B	Homo sapiens	167-178	
1797709-6	1991	The Z-Ala-His products showed enhanced selectivity for inactivation of cathepsin B over L when compared to analogous dipeptide inhibitors.	Dipeptides	117-126	cathepsin B	Homo sapiens	71-82	
34953094-0	2022	Engineering Enzyme-Cleavable Oligonucleotides by Automated Solid-Phase Incorporation of Cathepsin B Sensitive Dipeptide Linkers.	Dipeptides	110-119	cathepsin B	Homo sapiens	88-99	
34953094-3	2022	Inspired by the cathepsin B-sensitive dipeptide linkers in antibody-drug conjugates (ADCs) such as Adcetris, we have developed Val-Ala-02 and Val-Ala-Chalcone phosphoramidites for the automated synthesis of enzyme-cleavable oligonucleotides.	Dipeptides	38-47	cathepsin B	Homo sapiens	16-27