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1 milar treatment did not affect processing of procathepsin L.
2 gnals (Asn-X-Ser/Thr) into the cDNA of human procathepsin L, a lysosomal acid protease.
3 tion of a C-terminal epitope tag sequence to procathepsin L also induced misfolding of the proenzyme,
4 at several locations on the surface of mouse procathepsin L and modeling oligosaccharide conformation
5                            Whereas wild-type procathepsin L and mutants bearing carbohydrate at Asn-1
6  models, we have compared the itineraries of procathepsins L and B, two closely related members of th
7 amino acids Tyr-Asn allowed secretion of the procathepsin L, but the replacement of these two amino a
8 biting sequence near the N terminus of mouse procathepsin L can result in glycosylation of a normally
9  and transport kinetics of recombinant human procathepsin L containing one, two, or three glycosylati
10 refore conclude that the carboxy terminus of procathepsin L contains a sequence essential for its sec
11 gged protein did not compete with endogenous procathepsin L for targeting to lysosomes.
12     High-level transient expression of human procathepsin L in mouse NIH 3T3 cells results in the sec
13       At the same time, the endogenous mouse procathepsin L in these nontransformed cells is found in
14 uration was not associated with mutations in procathepsin L mRNA, was not complemented by procathepsi
15                                      But the procathepsin L mutant having phenylalanine in place of T
16 procathepsin L mRNA, was not complemented by procathepsin L overexpression, and did not affect the ma
17                    After several hours, much procathepsin L remains as precursor in a compartment tha
18  may have identified a recognition domain in procathepsin L that is important for its interactions wi
19                       Misfolded mutant mouse procathepsin L was not efficiently targeted to lysosomes
20              Similarly, epitope-tagged mouse procathepsin L was not targeted to lysosomes in homologo
21 dent lysine-based phosphorylation signals on procathepsin L, which account for the low level of phosp
22                             Mutants of human procathepsin L with carboxy-terminus deletions involving

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