Page last updated: 2024-08-17

histidine and Carcinoma, Lewis Lung

histidine has been researched along with Carcinoma, Lewis Lung in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Fink, A; Makovitzki, A; Shai, Y	1
Birsner, AE; Folkman, J; Javaherian, K; Ramanujam, VM; Satchi-Fainaro, R; Tjin Tham Sjin, RM	1

Other Studies

2 other study(ies) available for histidine and Carcinoma, Lewis Lung

Article	Year
Suppression of human solid tumor growth in mice by intratumor and systemic inoculation of histidine-rich and pH-dependent host defense-like lytic peptides. Cancer research, 2009, Apr-15, Volume: 69, Issue:8 Topics: Adenocarcinoma; Animals; Carcinoma, Lewis Lung; Cell Growth Processes; Cell Line, Tumor; Histidine; Humans; Hydrogen-Ion Concentration; Lysine; Male; Mice; Mice, Nude; NIH 3T3 Cells; Oligopeptides; Prostatic Neoplasms; Structure-Activity Relationship; Xenograft Model Antitumor Assays	2009
A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity. Cancer research, 2005, May-01, Volume: 65, Issue:9 Topics: Adenocarcinoma; Amino Acid Sequence; Animals; Carcinoma, Lewis Lung; Cell Movement; Endostatins; Endothelial Cells; Histidine; Humans; Mice; Mice, Inbred C57BL; Mice, SCID; Molecular Sequence Data; Pancreatic Neoplasms; Peptide Fragments; Protein Conformation; Protein Structure, Tertiary; Structure-Activity Relationship; Xenograft Model Antitumor Assays; Zinc	2005

Article

Year

Suppression of human solid tumor growth in mice by intratumor and systemic inoculation of histidine-rich and pH-dependent host defense-like lytic peptides.

Cancer research, 2009, Apr-15, Volume: 69, Issue:8

Topics: Adenocarcinoma; Animals; Carcinoma, Lewis Lung; Cell Growth Processes; Cell Line, Tumor; Histidine; Humans; Hydrogen-Ion Concentration; Lysine; Male; Mice; Mice, Nude; NIH 3T3 Cells; Oligopeptides; Prostatic Neoplasms; Structure-Activity Relationship; Xenograft Model Antitumor Assays

2009

A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity.

Cancer research, 2005, May-01, Volume: 65, Issue:9

Topics: Adenocarcinoma; Amino Acid Sequence; Animals; Carcinoma, Lewis Lung; Cell Movement; Endostatins; Endothelial Cells; Histidine; Humans; Mice; Mice, Inbred C57BL; Mice, SCID; Molecular Sequence Data; Pancreatic Neoplasms; Peptide Fragments; Protein Conformation; Protein Structure, Tertiary; Structure-Activity Relationship; Xenograft Model Antitumor Assays; Zinc

2005