PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
21376775-5	2011	However, the S3 peptide interacted only with S4 wild type peptide, but not with S4 mutants, and altered its localization onto the phospholipid membrane with increased resistance against the proteolytic enzyme, proteinase-k, in the presence of the S4 peptide.	Phospholipids	130-142	endogenous retrovirus group K member 7	Homo sapiens	210-220
17393253-0	2007	Heterogeneity of proteinase inhibitors in the water-soluble organic matrix from the oyster nacre.	Water	46-51	endogenous retrovirus group K member 7	Homo sapiens	17-27
17393253-1	2007	We extracted proteinase inhibitors from the nacre of the oyster Pinctada margaritifera with water.	Water	92-97	endogenous retrovirus group K member 7	Homo sapiens	13-23
15607631-6	2005	This activity was completely blocked by 10 mM phenylmethylsulphonyl fluoride (PMSF), a serine proteinase inhibitor, suggesting that this extracellular proteinase belongs to the serine proteinase class.	Phenylmethylsulfonyl Fluoride	46-76	endogenous retrovirus group K member 7	Homo sapiens	94-104
17479173-3	2007	PEG-coupled direct thrombin inhibitors that possess special pharmacokinetic characteristics and that have been designed for long lasting efficacy in extracellular space, control serine proteinase activity in tumour micro environment and therefore they own a high potential anti-tumour efficacy.	Polyethylene Glycols	0-3	endogenous retrovirus group K member 7	Homo sapiens	185-195
15607631-6	2005	This activity was completely blocked by 10 mM phenylmethylsulphonyl fluoride (PMSF), a serine proteinase inhibitor, suggesting that this extracellular proteinase belongs to the serine proteinase class.	Phenylmethylsulfonyl Fluoride	46-76	endogenous retrovirus group K member 7	Homo sapiens	151-161
15607631-6	2005	This activity was completely blocked by 10 mM phenylmethylsulphonyl fluoride (PMSF), a serine proteinase inhibitor, suggesting that this extracellular proteinase belongs to the serine proteinase class.	Phenylmethylsulfonyl Fluoride	46-76	endogenous retrovirus group K member 7	Homo sapiens	151-161
15607631-6	2005	This activity was completely blocked by 10 mM phenylmethylsulphonyl fluoride (PMSF), a serine proteinase inhibitor, suggesting that this extracellular proteinase belongs to the serine proteinase class.	Phenylmethylsulfonyl Fluoride	78-82	endogenous retrovirus group K member 7	Homo sapiens	94-104
15607631-6	2005	This activity was completely blocked by 10 mM phenylmethylsulphonyl fluoride (PMSF), a serine proteinase inhibitor, suggesting that this extracellular proteinase belongs to the serine proteinase class.	Phenylmethylsulfonyl Fluoride	78-82	endogenous retrovirus group K member 7	Homo sapiens	151-161
15607631-6	2005	This activity was completely blocked by 10 mM phenylmethylsulphonyl fluoride (PMSF), a serine proteinase inhibitor, suggesting that this extracellular proteinase belongs to the serine proteinase class.	Phenylmethylsulfonyl Fluoride	78-82	endogenous retrovirus group K member 7	Homo sapiens	151-161
15607631-8	2005	Conversely, a zinc-metalloproteinase inhibitor (1,10-phenanthroline) restrained the proteinase activity released by C. guilliermondii by approximately 50%.	1,10-phenanthroline	48-67	endogenous retrovirus group K member 7	Homo sapiens	26-36
15465346-0	2004	Bicyclic peptidomimetic tetrahydrofuro[3,2-b]pyrrol-3-one and hexahydrofuro[3,2-b]pyridine-3-one based scaffolds: synthesis and cysteinyl proteinase inhibition.	hexahydrofuro[3,2-b]pyridine-3-one	62-96	endogenous retrovirus group K member 7	Homo sapiens	138-148
1491013-1	1992	Skeletal muscle actin was lightly digested by proteinase K, which cleaved the peptide bond between Met-47 and Gly-48, producing a C-terminal 35 kDa fragment.	Methionine	99-102	endogenous retrovirus group K member 7	Homo sapiens	46-56
11438752-3	2001	A serine proteinase, proteinase K, was subjected to three-phase partitioning (TPP).	tpp	78-81	endogenous retrovirus group K member 7	Homo sapiens	9-19
11438752-3	2001	A serine proteinase, proteinase K, was subjected to three-phase partitioning (TPP).	tpp	78-81	endogenous retrovirus group K member 7	Homo sapiens	21-31
11438752-4	2001	A 3 ml volume of proteinase K solution (3 mg/ml in 0.05 M acetate buffer, pH 6.0) was brought to 30% (w/v) ammonium sulphate saturation by addition of saturated ammonium sulphate.	Ammonium Sulfate	107-124	endogenous retrovirus group K member 7	Homo sapiens	17-27
15623031-0	2004	[Inactivation of T4 phage in water environment using proteinase].	Water	29-34	endogenous retrovirus group K member 7	Homo sapiens	53-64
15623031-3	2004	In the optimum conditions and 67.5 u/mL concentration, the inactivation rate of proteinase K to T4 phage in sterilized water and in sewage achieved 99.4% and 49.4% respectively in an hour, and achieved >99.9% and 81.1% in three hours.	Water	119-124	endogenous retrovirus group K member 7	Homo sapiens	80-90
15623031-4	2004	The inactivation rate of the industrial proteinase 1398 to T4 phage in sterilized water achieved 74.4% in an hour.	Water	82-87	endogenous retrovirus group K member 7	Homo sapiens	40-50
12556442-1	2003	The dissociation equilibrium constant for heparin binding to antithrombin III (ATIII) is a measure of the cofactor"s binding to and activation of the proteinase inhibitor, and its salt dependence indicates that ionic and non-ionic interactions contribute approximately 40 and approximately 60% of the binding free energy, respectively.	Heparin	42-49	endogenous retrovirus group K member 7	Homo sapiens	150-160
7527012-4	1994	Thus, we examined in this study the inhibitory effect and therapeutic efficacy of newly produced recombinant human Kunitz-type proteinase inhibitor (R-020), which coded the second domain of human urinary trypsin inhibitor.	r-020	149-154	endogenous retrovirus group K member 7	Homo sapiens	127-137
8137934-5	1994	The active serine residue of proteinase K in this complex possesses a somewhat different configuration to that found in its native structure and hence renders the enzyme inactive.	Serine	11-17	endogenous retrovirus group K member 7	Homo sapiens	29-39
1491013-1	1992	Skeletal muscle actin was lightly digested by proteinase K, which cleaved the peptide bond between Met-47 and Gly-48, producing a C-terminal 35 kDa fragment.	Glycine	110-113	endogenous retrovirus group K member 7	Homo sapiens	46-56
3203685-3	1988	Besides this Cys72, proteinase K has two disulfide bonds, Cys34--Cys123 and Cys178--Cys249, which contribute to the stability of the tertiary structure consisting of an extended central parallel beta-sheet decorated by six alpha-helices, three short antiparallel beta-sheets, 18 beta-turns and involving several internal, structurally important water molecules.	Disulfides	41-50	endogenous retrovirus group K member 7	Homo sapiens	20-30
2794914-1	1989	Using Proteinase K with sodium dodecyl sulphate, it is possible to digest all the cellular material apart from the spermatozoa, resulting in a quick and effective method of their isolation.	Sodium Dodecyl Sulfate	24-47	endogenous retrovirus group K member 7	Homo sapiens	6-16
2915693-0	1989	Long-range structural changes in proteinase K triggered by calcium ion removal.	Calcium	59-66	endogenous retrovirus group K member 7	Homo sapiens	33-43
2915693-3	1989	Although Ca2+ is not directly involved in the catalytic mechanism and is 16.6 A away from the alpha-carbon atoms of the catalytic triad Asp 39-His 69-Ser 224, the activity of proteinase K towards the synthetic substrate succinyl-Ala-Ala-Ala-p-nitroanilide drops slowly to approximately 20% of its original value when it is depleted of Ca2+.	Carbon	100-106	endogenous retrovirus group K member 7	Homo sapiens	175-185
2915693-3	1989	Although Ca2+ is not directly involved in the catalytic mechanism and is 16.6 A away from the alpha-carbon atoms of the catalytic triad Asp 39-His 69-Ser 224, the activity of proteinase K towards the synthetic substrate succinyl-Ala-Ala-Ala-p-nitroanilide drops slowly to approximately 20% of its original value when it is depleted of Ca2+.	Aspartic Acid	136-139	endogenous retrovirus group K member 7	Homo sapiens	175-185
2915693-3	1989	Although Ca2+ is not directly involved in the catalytic mechanism and is 16.6 A away from the alpha-carbon atoms of the catalytic triad Asp 39-His 69-Ser 224, the activity of proteinase K towards the synthetic substrate succinyl-Ala-Ala-Ala-p-nitroanilide drops slowly to approximately 20% of its original value when it is depleted of Ca2+.	SUC-ALA-ALA-ALA-PNA	220-255	endogenous retrovirus group K member 7	Homo sapiens	175-185
1316092-4	1992	Proteinase inhibitors (E64, Stefin A or leupeptin) revealed a slightly negative influence.	E 64	23-26	endogenous retrovirus group K member 7	Homo sapiens	0-10
1316092-4	1992	Proteinase inhibitors (E64, Stefin A or leupeptin) revealed a slightly negative influence.	leupeptin	40-49	endogenous retrovirus group K member 7	Homo sapiens	0-10
2714465-6	1989	Digestive enzymes: alpha-amylase and proteinase are resistant to the action of mineral water and its components.	Mineral Waters	79-92	endogenous retrovirus group K member 7	Homo sapiens	37-47
3203685-3	1988	Besides this Cys72, proteinase K has two disulfide bonds, Cys34--Cys123 and Cys178--Cys249, which contribute to the stability of the tertiary structure consisting of an extended central parallel beta-sheet decorated by six alpha-helices, three short antiparallel beta-sheets, 18 beta-turns and involving several internal, structurally important water molecules.	Water	345-350	endogenous retrovirus group K member 7	Homo sapiens	20-30
3203685-4	1988	Proteinase K exhibits two Ca2+-binding sites, one very strong and the other weak, which were the sites of the heavy atoms (Pb2+, Sm3+) used to solve the crystal structure.	Lead	123-127	endogenous retrovirus group K member 7	Homo sapiens	0-10
3203685-4	1988	Proteinase K exhibits two Ca2+-binding sites, one very strong and the other weak, which were the sites of the heavy atoms (Pb2+, Sm3+) used to solve the crystal structure.	sm3+	129-133	endogenous retrovirus group K member 7	Homo sapiens	0-10
3203685-10	1988	Based on these experiments, a reaction mechanism is proposed where the peptide substrate forms a three-stranded antiparallel pleated sheet with the recognition site of proteinase K consisting of Ser132--Leu133--Gly134 on one side and Gly100--Ser101 on the other, followed by expulsion of the oxyanion hole water W335 and hydrolytic cleavage by the Asp39--His69--Serr224 triad.	Water	306-311	endogenous retrovirus group K member 7	Homo sapiens	168-178
3203685-10	1988	Based on these experiments, a reaction mechanism is proposed where the peptide substrate forms a three-stranded antiparallel pleated sheet with the recognition site of proteinase K consisting of Ser132--Leu133--Gly134 on one side and Gly100--Ser101 on the other, followed by expulsion of the oxyanion hole water W335 and hydrolytic cleavage by the Asp39--His69--Serr224 triad.	serr224	362-369	endogenous retrovirus group K member 7	Homo sapiens	168-178
3271105-6	1988	Four corrections to the amino acid sequence were made, which were confirmed later by sequence analysis of the proteinase K gene: a deletion of one glycine in position 80; a change of sequence in position 207-208 and insertions of the dipeptide 210-211 and of residue 270.	Glycine	147-154	endogenous retrovirus group K member 7	Homo sapiens	110-120
3271105-6	1988	Four corrections to the amino acid sequence were made, which were confirmed later by sequence analysis of the proteinase K gene: a deletion of one glycine in position 80; a change of sequence in position 207-208 and insertions of the dipeptide 210-211 and of residue 270.	Dipeptides	234-243	endogenous retrovirus group K member 7	Homo sapiens	110-120
3019385-0	1986	Iron-containing metallocenes as active site directed inhibitors of the proteinase that cleaves the NH2-terminal propeptides from type I procollagen.	Iron	0-4	endogenous retrovirus group K member 7	Homo sapiens	71-81
3019385-0	1986	Iron-containing metallocenes as active site directed inhibitors of the proteinase that cleaves the NH2-terminal propeptides from type I procollagen.	Metallocenes	16-28	endogenous retrovirus group K member 7	Homo sapiens	71-81
3019385-0	1986	Iron-containing metallocenes as active site directed inhibitors of the proteinase that cleaves the NH2-terminal propeptides from type I procollagen.	propeptides	112-123	endogenous retrovirus group K member 7	Homo sapiens	71-81
3019385-1	1986	Derivatives of ferrocene (dicyclopentadienyliron) (Fc) were examined as active site directed inhibitors of type I procollagen N-proteinase, the enzyme that cleaves the NH2-terminal propeptides from type I procollagen.	ferrocene	15-24	endogenous retrovirus group K member 7	Homo sapiens	128-138
3019385-1	1986	Derivatives of ferrocene (dicyclopentadienyliron) (Fc) were examined as active site directed inhibitors of type I procollagen N-proteinase, the enzyme that cleaves the NH2-terminal propeptides from type I procollagen.	ferrocene	26-48	endogenous retrovirus group K member 7	Homo sapiens	128-138
3019385-1	1986	Derivatives of ferrocene (dicyclopentadienyliron) (Fc) were examined as active site directed inhibitors of type I procollagen N-proteinase, the enzyme that cleaves the NH2-terminal propeptides from type I procollagen.	Fc(alpha) receptor	51-53	endogenous retrovirus group K member 7	Homo sapiens	128-138
32683266-4	2020	Enzymatic treatment by Flavourzyme and bromelain significantly elevated the levels of ketones and odors, whereas excessive proteolysis by papain and proteinase K largely reduced the levels of esters and aldehydes.	Esters	192-198	endogenous retrovirus group K member 7	Homo sapiens	149-159
300629-8	1977	This heptadecapeptide which contains all of the amino acid residues of BPTI taking part in the interaction of the proteinase inhibitor with trypsin binds 3 X 10(7) time more weakly to the enzyme than native BPTI does.	gastrin 17	5-21	endogenous retrovirus group K member 7	Homo sapiens	114-124
32683266-4	2020	Enzymatic treatment by Flavourzyme and bromelain significantly elevated the levels of ketones and odors, whereas excessive proteolysis by papain and proteinase K largely reduced the levels of esters and aldehydes.	Aldehydes	203-212	endogenous retrovirus group K member 7	Homo sapiens	149-159
29782985-8	2018	On the extracellular environment, ethanol-mediated silk spheres exhibited higher resistance against enzymatic degradation of proteinase K when compared with pristine spheres.	Ethanol	34-41	endogenous retrovirus group K member 7	Homo sapiens	125-135
26760982-12	2015	Here, it is proposed that a decreased DHEA/cortisol ratio may favor the accumulation of foamy macrophages reflecting the cortisol induction of HERV-K102 particle production concomitant with the blocked release of particles by secreted AFP.	Dehydroepiandrosterone	38-42	endogenous retrovirus group K member 7	Homo sapiens	143-152
26760982-12	2015	Here, it is proposed that a decreased DHEA/cortisol ratio may favor the accumulation of foamy macrophages reflecting the cortisol induction of HERV-K102 particle production concomitant with the blocked release of particles by secreted AFP.	Hydrocortisone	43-51	endogenous retrovirus group K member 7	Homo sapiens	143-152
26760982-12	2015	Here, it is proposed that a decreased DHEA/cortisol ratio may favor the accumulation of foamy macrophages reflecting the cortisol induction of HERV-K102 particle production concomitant with the blocked release of particles by secreted AFP.	Hydrocortisone	121-129	endogenous retrovirus group K member 7	Homo sapiens	143-152