Dipeptidyl peptidase 4
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Dipeptidyl peptidase 4
Summary
Dipeptidyl peptidase 4 is a protein[1]. It has Wikipedia articles in 10 language editions, a strong signal of global cultural recognition.[2]
Key Facts
- Dipeptidyl peptidase 4's instance of is recorded as protein[3].
- Dipeptidyl peptidase 4's physically interacts with is recorded as alogliptin[4].
- Dipeptidyl peptidase 4's physically interacts with is recorded as linagliptin[5].
- Dipeptidyl peptidase 4's physically interacts with is recorded as omarigliptin[6].
- Dipeptidyl peptidase 4's physically interacts with is recorded as saxagliptin[7].
- Dipeptidyl peptidase 4's physically interacts with is recorded as sitagliptin[8].
- Dipeptidyl peptidase 4's physically interacts with is recorded as vildagliptin[9].
- Dipeptidyl peptidase 4's physically interacts with is recorded as teneligliptin[10].
- Dipeptidyl peptidase 4's physically interacts with is recorded as anagliptin[11].
- Dipeptidyl peptidase 4's physically interacts with is recorded as Trelagliptin[12].
- Dipeptidyl peptidase 4's physically interacts with is recorded as omarigliptin[13].
- Dipeptidyl peptidase 4's physically interacts with is recorded as Evogliptin[14].
- Dipeptidyl peptidase 4's physically interacts with is recorded as gosogliptin[15].
- Dipeptidyl peptidase 4 is part of Alpha/Beta hydrolase fold[16].
- Dipeptidyl peptidase 4 is part of dipeptidyl-peptidase IV family[17].
- Dipeptidyl peptidase 4 is part of Peptidase S9, prolyl oligopeptidase, catalytic domain, protein family[18].
- Dipeptidyl peptidase 4 is part of Peptidase S9, serine active site, protein family[19].
- Dipeptidyl peptidase 4 comprises Dipeptidylpeptidase IV, N-terminal domain[20].
- Dipeptidyl peptidase 4 comprises Peptidase S9, serine active site[21].
- Dipeptidyl peptidase 4 comprises Peptidase S9, prolyl oligopeptidase, catalytic domain[22].
Why It Matters
Dipeptidyl peptidase 4 has Wikipedia articles in 10 language editions, a strong signal of global cultural recognition.[2] It is known by 25 alternative names across languages and contexts.[23]