| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-95 |
Sentence |
denotes |
Dolichol phosphate mannose synthase: a Glycosyltransferase with Unity in molecular diversities. |
| T1 |
0-95 |
Sentence |
denotes |
Dolichol phosphate mannose synthase: a Glycosyltransferase with Unity in molecular diversities. |
| TextSentencer_T2 |
96-217 |
Sentence |
denotes |
N-glycans provide structural and functional stability to asparagine-linked (N-linked) glycoproteins, and add flexibility. |
| T2 |
96-217 |
Sentence |
denotes |
N-glycans provide structural and functional stability to asparagine-linked (N-linked) glycoproteins, and add flexibility. |
| TextSentencer_T3 |
218-313 |
Sentence |
denotes |
Glycan biosynthesis is elaborative, multi-compartmental and involves many glycosyltransferases. |
| T3 |
218-313 |
Sentence |
denotes |
Glycan biosynthesis is elaborative, multi-compartmental and involves many glycosyltransferases. |
| TextSentencer_T4 |
314-460 |
Sentence |
denotes |
Failure to assemble N-glycans leads to phenotypic changes developing infection, cancer, congenital disorders of glycosylation (CDGs) among others. |
| T4 |
314-460 |
Sentence |
denotes |
Failure to assemble N-glycans leads to phenotypic changes developing infection, cancer, congenital disorders of glycosylation (CDGs) among others. |
| TextSentencer_T5 |
461-681 |
Sentence |
denotes |
Biosynthesis of N-glycans begins at the endoplasmic reticulum (ER) with the assembly of dolichol-linked tetra-decasaccharide (Glc3Man9GlcNAc2-PP-Dol) where dolichol phosphate mannose synthase (DPMS) plays a central role. |
| T5 |
461-681 |
Sentence |
denotes |
Biosynthesis of N-glycans begins at the endoplasmic reticulum (ER) with the assembly of dolichol-linked tetra-decasaccharide (Glc3Man9GlcNAc2-PP-Dol) where dolichol phosphate mannose synthase (DPMS) plays a central role. |
| TextSentencer_T6 |
682-815 |
Sentence |
denotes |
DPMS is also essential for GPI anchor biosynthesis as well as for O- and C-mannosylation of proteins in yeast and in mammalian cells. |
| T6 |
682-815 |
Sentence |
denotes |
DPMS is also essential for GPI anchor biosynthesis as well as for O- and C-mannosylation of proteins in yeast and in mammalian cells. |
| TextSentencer_T7 |
816-946 |
Sentence |
denotes |
DPMS has been purified from several sources and its gene has been cloned from 39 species (e.g., from protozoan parasite to human). |
| T7 |
816-946 |
Sentence |
denotes |
DPMS has been purified from several sources and its gene has been cloned from 39 species (e.g., from protozoan parasite to human). |
| TextSentencer_T8 |
947-1066 |
Sentence |
denotes |
It is an inverting GT-A folded enzyme and classified as GT2 by CAZy (carbohydrate active enZyme; http://www.cazy.org ). |
| T8 |
947-1066 |
Sentence |
denotes |
It is an inverting GT-A folded enzyme and classified as GT2 by CAZy (carbohydrate active enZyme; http://www.cazy.org ). |
| TextSentencer_T9 |
1067-1258 |
Sentence |
denotes |
The sequence alignment detects the presence of a metal binding DAD signature in DPMS from all 39 species but finds cAMP-dependent protein phosphorylation motif (PKA motif) in only 38 species. |
| T9 |
1067-1258 |
Sentence |
denotes |
The sequence alignment detects the presence of a metal binding DAD signature in DPMS from all 39 species but finds cAMP-dependent protein phosphorylation motif (PKA motif) in only 38 species. |
| TextSentencer_T10 |
1259-1295 |
Sentence |
denotes |
DPMS also has hydrophobic region(s). |
| T10 |
1259-1295 |
Sentence |
denotes |
DPMS also has hydrophobic region(s). |
| TextSentencer_T11 |
1296-1452 |
Sentence |
denotes |
Hydropathy analysis of amino acid sequences from bovine, human, S. crevisiae and A. thaliana DPMS show PKA motif is present between the hydrophobic domains. |
| T11 |
1296-1452 |
Sentence |
denotes |
Hydropathy analysis of amino acid sequences from bovine, human, S. crevisiae and A. thaliana DPMS show PKA motif is present between the hydrophobic domains. |
| TextSentencer_T12 |
1453-1566 |
Sentence |
denotes |
The location of PKA motif as well as the hydrophobic domain(s) in the DPMS sequence vary from species to species. |
| T12 |
1453-1566 |
Sentence |
denotes |
The location of PKA motif as well as the hydrophobic domain(s) in the DPMS sequence vary from species to species. |
| TextSentencer_T13 |
1567-1656 |
Sentence |
denotes |
For example, the domain(s) could be located at the center or more towards the C-terminus. |
| T13 |
1567-1656 |
Sentence |
denotes |
For example, the domain(s) could be located at the center or more towards the C-terminus. |
| TextSentencer_T14 |
1657-1878 |
Sentence |
denotes |
Irrespective of their catalytic similarity, the DNA sequence, the amino acid identity, and the lack of a stretch of hydrophobic amino acid residues at the C-terminus, DPMS is still classified as Type I and Type II enzyme. |
| T14 |
1657-1878 |
Sentence |
denotes |
Irrespective of their catalytic similarity, the DNA sequence, the amino acid identity, and the lack of a stretch of hydrophobic amino acid residues at the C-terminus, DPMS is still classified as Type I and Type II enzyme. |
| TextSentencer_T15 |
1879-2001 |
Sentence |
denotes |
Because of an apparent bio-sensing ability, extracellular signaling and microenvironment regulate DPMS catalytic activity. |
| T15 |
1879-2001 |
Sentence |
denotes |
Because of an apparent bio-sensing ability, extracellular signaling and microenvironment regulate DPMS catalytic activity. |
| TextSentencer_T16 |
2002-2093 |
Sentence |
denotes |
In this review, we highlight some important features and the molecular diversities of DPMS. |
| T16 |
2002-2093 |
Sentence |
denotes |
In this review, we highlight some important features and the molecular diversities of DPMS. |