Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases
about
Protein adaptations in archaeal extremophiles.The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-rollSome like it cold: understanding the survival strategies of psychrophilesOptimization to low temperature activity in psychrophilic enzymesProbing the Role of Divalent Metal Ions in a Bacterial Psychrophilic Metalloprotease: Binding Studies of an Enzyme in the Crystalline State by X-Ray CrystallographyStructure Analysis of a New Psychrophilic Marine ProteaseStructure of a complete four-domain chitinase from Moritella marina, a marine psychrophilic bacteriumDiscovery, Molecular Mechanisms, and Industrial Applications of Cold-Active EnzymesA novel ∼34-kDa α-amylase from psychrotroph Exiguobacterium sp. SH3: production, purification, and characterization.Thermal adaptation of α-amylases: a review.Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibilityFunction and biotechnology of extremophilic enzymes in low water activity.Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome.Some like it cold: biocatalysis at low temperatures.Crystallization and preliminary X-ray crystallographic studies of a psychrophilic subtilisin-like protease Apa1 from Antarctic Pseudoalteromonas sp. strain AS-11Homology modeling and molecular dynamics simulation studies of a marine alkaline proteaseExtracellular overproduction and preliminary crystallographic analysis of a family I.3 lipase.Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: new insights into relationship between conformational flexibility anPsychrophilic enzymes: from folding to function and biotechnology.Psychrophily and catalysis.Proteases from psychrotrophs: an overview.Recent developments in production and biotechnological applications of cold-active microbial proteases.Features of pseudomonads growing at low temperatures: another facet of their versatility.Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants.Cold-adapted proteases as an emerging class of therapeutics.Molecular dynamics of the salt dependence of a cold-adapted enzyme: endonuclease I.Potential use of Atlantic cod trypsin in biomedicine.The role of Ca²⁺ in the activity of Mycobacterium tuberculosis DNA gyrase.Cloning, expression, and characterization of a recombinant esterase from cold-adapted Pseudomonas mandelii.Importance of a repetitive nine-residue sequence motif for intracellular stability and functional structure of a family I.3 lipase.NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase.Insight into the cold adaptation and hemicellulose utilization of Cladosporium neopsychrotolerans from genome analysis and biochemical characterization.
P2860
Q21285082-606E3875-136C-4656-9083-FFA7E4D017DDQ24605244-5818FC7A-7C60-4B30-B660-601B7EB00F70Q27021642-2E8BA1DA-2554-4FD5-8132-EE0AB30DC973Q27027749-1696FC36-4C63-4770-AEEE-98A328B60FA9Q27641595-ACF50661-656A-4B13-A0EE-3143D8948AB1Q27675902-F0A9869F-0B4A-4F6D-8237-D53FAEF2F970Q27684527-7C0ADA36-432C-4C69-B2B9-5551BAA62F5CQ28077585-0CAA5F8C-2F4A-4329-BFA5-D2C1D6220653Q30009878-27A14462-7B21-4A7F-900C-9A7E35F26DC5Q30365616-FB946AC6-D4BA-4B39-B73C-89DCF327B6DDQ34052344-7CBBCC82-9A79-45B0-9402-568198D0A5B9Q34266261-D12E7985-99CA-4285-9AC6-170E250FCE3AQ35169545-9B2B6DA8-FB38-4332-9E9D-176D1FCCCBEBQ35671851-18A93C2F-ADE6-40F4-A54A-B5A3FF4F9266Q35950539-3A7C2952-B635-4F67-A82E-D03603FD3EE4Q36436668-C7E90481-01F6-409B-B67A-4066A7209B24Q36580557-531B65AE-7450-4C9E-92C1-13C4F788E59DQ37152850-040BA06C-E752-4B46-BF9C-759B1C4D38F3Q37287783-D079BCA2-0A59-4F90-862F-078894AC294DQ37651499-EE13F4DA-50F5-48F0-8B16-E6B51D53D7DDQ37667053-C5D8D58C-7A80-4596-9CC5-0E05584CE004Q38030992-E659CD43-3335-4617-960A-4B48BC221415Q38342251-99CA916A-0028-4E16-9FAE-21E7F90E3D08Q39195492-92E1F55C-5FD9-4132-A9F0-C1887DBE62A0Q39410680-5609DB78-555C-4D7E-97CC-D548BF6CA01FQ41482021-2E993581-BED2-4407-ACA9-43792642E29FQ42055253-D80422D4-381A-423C-891F-9D10E2E65A49Q42408670-E6E36C0F-1D89-4D7C-920D-005D72317877Q42674996-5B2E4DD5-5EF2-4285-8D65-175424B34319Q46649185-DE934559-10C9-453B-B297-EE0573AC9EC3Q46890318-158D9E13-35FC-4BC3-A87C-3ACA6C08B387Q55177185-A52206C1-2C67-4F85-AF14-9C9050DE8BEB
P2860
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@ast
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@en
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@nl
type
label
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@ast
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@en
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@nl
prefLabel
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@ast
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@en
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@nl
P2093
P2860
P50
P3181
P356
P1433
P1476
Crystal structures of a psychr ...... ysis by cold-adapted proteases
@en
P2093
Charles Gerday
Jean-Pierre Chessa
Jozef Van Beeumen
Richard Haser
P2860
P304
P3181
P356
10.1002/PROT.10264
P407
P577
2003-03-01T00:00:00Z