The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues.
about
A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidasesStructure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosisInteractions of the proteins of neuronal ceroid lipofuscinosis: clues to functionLysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis.Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.The intracellular location and function of proteins of neuronal ceroid lipofuscinoses.Histochemical Demonstration of Tripeptidyl Aminopeptidase I.
P2860
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P2860
The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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2001年学术文章
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@zh-hans
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2001年學術文章
@zh-hant
name
The specificity of lysosomal t ...... n on angiotensin-II analogues.
@en
The specificity of lysosomal t ...... n on angiotensin-II analogues.
@nl
type
label
The specificity of lysosomal t ...... n on angiotensin-II analogues.
@en
The specificity of lysosomal t ...... n on angiotensin-II analogues.
@nl
prefLabel
The specificity of lysosomal t ...... n on angiotensin-II analogues.
@en
The specificity of lysosomal t ...... n on angiotensin-II analogues.
@nl
P2860
P1433
P1476
The specificity of lysosomal t ...... n on angiotensin-II analogues.
@en
P2093
Bernardini F
Warburton MJ
P2860
P304
P356
10.1016/S0014-5793(01)02608-4
P407
P577
2001-07-01T00:00:00Z