University of Maryland Baltiore

Frederick, MD, United States

University of Maryland Baltiore

Frederick, MD, United States
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Dang Y.-H.,Health Science University | Liu Z.-W.,Shanxi Provincial Peoples Hospital | Chen F.,Nanjing Medical University | Guo K.,Xi'an Jiaotong University | Wang J.-B.,University of Maryland Baltiore
Acta Academiae Medicinae Sinicae | Year: 2014

Histidine triad nucleotide-binding protein 1 (HINTI) is a member of a superfamily of histidine triad proteins named by the conserved nueleotide-binding motif histidine-x-histidine-x-histidine-xx, in which x represents hydrophobic amino acid. HINT1 is implicated in pathological progress of many human diseases including cancer and schizophrenia; however, little is known about the essential role and pathological consequences of HINT1 in cellular physiology and diseases. Therefore, we summarize the structure, distribution, and physio logical function of HINT1 in cells and tissues as well as the correlation between HINTI and human diseases.


PubMed | Shanxi Provincial Peoples Hospital, Nanjing Medical University, Xi'an Jiaotong University and University of Maryland Baltiore
Type: Journal Article | Journal: Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae | Year: 2014

Histidine triad nucleotide-binding protein 1 (HINT1) is a member of a superfamily of histidine triad proteins named by the conserved nucleotide-binding motif histidine-x-histidine-x-histidine-xx, in which x represents hydrophobic amino acid. HINT1 is implicated in pathological progress of many human diseases including cancer and schizophrenia; however, little is known about the essential role and pathological consequences of HINT1 in cellular physiology and diseases. Therefore, we summarize the structure, distribution, and physiological function of HINT1 in cells and tissues as well as the correlation between HINT1 and human diseases.

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