Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion.

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P1476

Distinct Epitopes on CD13 Mediate Opposite Consequences for Cell Adhesion

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P2093

Claudia A Garay-Canales

http://www.w3.org/2001/XMLSchema#string

Ileana Licona-Limón

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P2860

Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N

The X-ray Crystal Structure of Human Aminopeptidase N Reveals a Novel Dimer and the Basis for Peptide Processing

Structural basis for multifunctional roles of mammalian aminopeptidase N

CD13 is a novel mediator of monocytic/endothelial cell adhesion.

The Rational Design of Therapeutic Peptides for Aminopeptidase N using a Substrate-Based Approach.

Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis

Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects.

CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated.

Aminopeptidase N (CD13) as a target for cancer chemotherapy.

The significance of aminopeptidases and haematopoietic cell differentiation.

P304

4093435

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P31

scholarly article

P356

10.1155/2018/4093435

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P407

English

P478

2018

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P50

Enrique Ortega

P577

2018-03-29T00:00:00Z

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P698

29789790

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P932

5896358

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