CW operation of GaInAsP buried ridge structure laser at 1.5 μm grown by LP-MOCVD

1984 ◽  
Vol 20 (21) ◽  
pp. 850 ◽  
Author(s):  
R. Blondeau ◽  
M. Razeghi ◽  
M. Krakowski ◽  
G. Vilain ◽  
B. de Cremoux ◽  
...  
1989 ◽  
Vol 25 (21) ◽  
pp. 1433 ◽  
Author(s):  
C. Kazmierski ◽  
B. Theys ◽  
B. Rose ◽  
A. Mircea ◽  
A. Jalil ◽  
...  

1996 ◽  
Vol 449 ◽  
Author(s):  
Shuji Nakamura

ABSTRACTThe continuous-wave (CW) operation of InGaN multi-quantum-well-structure laser diodes (LDs) was demonstrated at room temperature (RT) with a lifetime of 35 hours. The threshold current and the voltage of the LDs were 80 mA and 5.5 V, respectively. The threshold current density was 3.6 kA/cm2. Longitudinal modes with a mode separation of 0.042 nm were observed under CW operation at RT. When the temperature of the LDs was varied, large mode hopping of the emission wavelength was observed. The carrier lifetime and the threshold carrier density were estimated to be 10 ns and 2 × 1020/cm3, respectively. The beam full width at half-power values for the parallel and the perpendicular near-field patterns were 1.6 µm and 0.8 µm, respectively. Those of the far-field patterns were 6.8° and 33.6°, respectively.


1988 ◽  
Vol 24 (10) ◽  
pp. 609-611 ◽  
Author(s):  
A. Talneau ◽  
D. Rondi ◽  
M. Krakowski ◽  
R. Blondeau

1989 ◽  
Vol 25 (6) ◽  
pp. 1346-1352 ◽  
Author(s):  
M. Krakowski ◽  
D. Rondi ◽  
A. Talneau ◽  
Y. Combemale ◽  
G. Chevalier ◽  
...  

2003 ◽  
Vol 70 ◽  
pp. 201-212 ◽  
Author(s):  
Hideaki Nagase ◽  
Keith Brew

The tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors of the matrix metalloproteinases (MMPs), enzymes that play central roles in the degradation of extracellular matrix components. The balance between MMPs and TIMPs is important in the maintenance of tissues, and its disruption affects tissue homoeostasis. Four related TIMPs (TIMP-1 to TIMP-4) can each form a complex with MMPs in a 1:1 stoichiometry with high affinity, but their inhibitory activities towards different MMPs are not particularly selective. The three-dimensional structures of TIMP-MMP complexes reveal that TIMPs have an extended ridge structure that slots into the active site of MMPs. Mutation of three separate residues in the ridge, at positions 2, 4 and 68 in the amino acid sequence of the N-terminal inhibitory domain of TIMP-1 (N-TIMP-1), separately and in combination has produced N-TIMP-1 variants with higher binding affinity and specificity for individual MMPs. TIMP-3 is unique in that it inhibits not only MMPs, but also several ADAM (a disintegrin and metalloproteinase) and ADAMTS (ADAM with thrombospondin motifs) metalloproteinases. Inhibition of the latter groups of metalloproteinases, as exemplified with ADAMTS-4 (aggrecanase 1), requires additional structural elements in TIMP-3 that have not yet been identified. Knowledge of the structural basis of the inhibitory action of TIMPs will facilitate the design of selective TIMP variants for investigating the biological roles of specific MMPs and for developing therapeutic interventions for MMP-associated diseases.


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