Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (12215) 12215
Newsletter (3070) 3070
Publication (1378) 1378
Book Chapter (142) 142
Dissertation (99) 99
Book Review (62) 62
Newspaper Article (26) 26
Conference Proceeding (24) 24
Government Document (11) 11
Book / eBook (5) 5
Magazine Article (4) 4
Web Resource (4) 4
Reference (3) 3
Trade Publication Article (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
calpain (10424) 10424
animals (6111) 6111
humans (4108) 4108
calpain - metabolism (3839) 3839
index medicus (3702) 3702
biochemistry & molecular biology (2617) 2617
research (2588) 2588
rats (2314) 2314
apoptosis (2215) 2215
male (2159) 2159
neurosciences (1866) 1866
proteolysis (1824) 1824
mice (1778) 1778
calpain - antagonists & inhibitors (1513) 1513
cell biology (1454) 1454
calcium (1432) 1432
activation (1415) 1415
proteins (1409) 1409
calpain - genetics (1334) 1334
reports (1315) 1315
analysis (1289) 1289
female (1284) 1284
universities and colleges (1174) 1174
calcium - metabolism (1162) 1162
calpastatin (1042) 1042
cells, cultured (989) 989
expression (982) 982
phosphorylation (900) 900
physiological aspects (884) 884
cysteine (836) 836
rats, sprague-dawley (797) 797
amino acid sequence (778) 778
brain (762) 762
molecular sequence data (758) 758
blotting, western (669) 669
article (668) 668
apoptosis - drug effects (658) 658
skeletal-muscle (654) 654
cells (648) 648
mu-calpain (642) 642
oxidative stress (640) 640
time factors (640) 640
neurons (633) 633
cell line (626) 626
signal transduction (623) 623
degradation (619) 619
calpain - physiology (615) 615
cell death (594) 594
biophysics (590) 590
genetic aspects (587) 587
biochemistry (576) 576
cell-death (564) 564
disease models, animal (564) 564
gene expression (558) 558
cysteine proteinase inhibitors - pharmacology (557) 557
cystine (557) 557
cattle (544) 544
cancer (534) 534
enzyme activation (512) 512
pharmacology & pharmacy (511) 511
thiols (510) 510
calcium-binding proteins - metabolism (508) 508
immunohistochemistry (506) 506
ischemia (502) 502
protein (488) 488
protease (477) 477
proteases (474) 474
caspases - metabolism (473) 473
inhibition (473) 473
cell line, tumor (467) 467
caspase (460) 460
cleavage (456) 456
rats, wistar (456) 456
research article (453) 453
mice, inbred c57bl (446) 446
alzheimer's disease (445) 445
calpains (444) 444
physiology (443) 443
adult (440) 440
kinetics (435) 435
food science & technology (429) 429
oncology (422) 422
neurons - metabolism (421) 421
calpain - chemistry (420) 420
molecular weight (420) 420
protein binding (408) 408
mutation (400) 400
electrophoresis, polyacrylamide gel (394) 394
neurology (394) 394
middle aged (392) 392
multidisciplinary sciences (392) 392
medical research (385) 385
dipeptides - pharmacology (381) 381
alzheimers-disease (378) 378
dose-response relationship, drug (371) 371
neurons - drug effects (371) 371
death (368) 368
in-vitro (368) 368
mitochondria (366) 366
muscle, skeletal - metabolism (365) 365
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (15136) 15136
Japanese (122) 122
Chinese (108) 108
Russian (50) 50
Spanish (31) 31
French (28) 28
Korean (12) 12
Polish (10) 10
Portuguese (5) 5
Ukrainian (4) 4
German (3) 3
Catalan (2) 2
Hungarian (2) 2
Czech (1) 1
Italian (1) 1
Persian (1) 1
Serbian (1) 1
Swedish (1) 1
Turkish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Phosphorylation inhibits the activity of [mu]-calpain at different incubation temperatures and Ca.sup.2+ concentrations in vitro
by Du, Manting and Li, Xin and Li, Zheng and Li, Meng and Gao, Lingling and Zhang, Dequan
Food Chemistry, ISSN 0308-8146, 08/2017, Volume 228, p. 649
* The effect of phosphorylation on the activity of [mu]-calpain was detected in vitro. * Incubation at 25[degrees]C could diminish the influence of... 
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Calpain Inhibitors: Promising Agents in Respiratory Medicine
by Alshami, Abbas and Varon, Daryelle S and Varon, Joseph
Current Respiratory Medicine Reviews, ISSN 1573-398X, 12/2018, Volume 14, Issue 4, p. 187
Calpain
Journal Article
Details down arrow
3. Full Text Cardiac injury: Role of mitochondrial calpain 1 activation
by Thompson, Jeremy and Hu, Ying and Lesnefsky, Edward J and Chen, Qun
Mitochondrion, ISSN 1567-7249, 09/2015, Volume 24, pp. S29 - S29
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Secalonic acid D reduced the percentage of side populations by down-regulating the expression of ABCG2
by Hu, Ya-peng and Tao, Li-yang and Wang, Fang and Zhang, Jian-ye and Liang, Yong-ju and Fu, Li-wu
Biochemical Pharmacology, ISSN 0006-2952, 06/2013, Volume 85, Issue 11, pp. 1619 - 1625
The side population cells characterized by the ability to transport Hoechst 33342 out of cells have been identified as cancer stem-like cells. ABCG2 is found... 
Calpain
Journal Article
Details down arrow
5. Full Text [beta]-Hydroxy-[beta]-methylbutyrate prevents sepsis-induced diaphragm dysfunction in mice
by Supinski, Gerald S and Callahan, Leigh A
Respiratory Physiology & Neurobiology, ISSN 1569-9048, 06/2014, Volume 196, p. 63
acents [beta]-Hydroxy-[beta]-methylbutyrate (HMB) prevents sepsis-induced diaphragm weakness. acents HMB blocks sepsis-induced diaphragm caspase 3 and 20S... 
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text The Ca.sup.2+-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel
FEBS Letters, ISSN 0014-5793, 03/2014, Volume 588, Issue 5, p. 665
acents Ca.sup.2+-dependence of calpastatin domain L (CS.sub.L) binding with Cav1.2 was studied. acents Besides binding with the IQ motif, CS.sub.L was also... 
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text The effect of temperature on the activity of [mu]- and m-calpain and calpastatin during post-mortem storage of porcine longissimus muscle
by Pomponio, Luigi and Ertbjerg, Per
Meat Science, ISSN 0309-1740, 05/2012, Volume 91, Issue 1, p. 50
The experiment was conducted to determine the effect of temperature during post-mortem muscle storage on the activity of the calpain system, the myofibril... 
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Erratum: Ancestral founder mutations in calpain‐3 in the Indian Agarwal community: Historical, clinical, and molecular perspective
Muscle & Nerve, ISSN 0148-639X, 12/2013, Volume 48, Issue 6, pp. 999 - 999
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text Development of amperometric immunoassays for calpastatin and [mu]-calpain with possible applications in the biomedical field
by Zor, Kinga and Zabara, Alexandru and Gorton, Lo and Nistor, Mihaela
Sensors & Actuators: B. Chemical, ISSN 0925-4005, 03/2011, Volume 152, Issue 2, p. 248
Due to the involvement of calpains and calpastatin in the pathology of several diseases, it is important to create an analytical tool for their accurate and... 
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text The blockade of dihydropyridine channels prevents an increase in [micro]-calpain level under m. soleus unloading
by Belova, S. P and Lomonosova, Yu. N and Shenkman, B. S and Nemirovskaya, T. L
Doklady Biochemistry and Biophysics, ISSN 1607-6729, 01/2015, Volume 460, Issue 1, p. 1
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
11. Full Text Structure-function relationships in calpains
by Campbell, Robert L and Davies, Peter L
Biochemical Journal, ISSN 0264-6021, 11/2012, Volume 447, Issue 3, pp. 335 - 351
Calpains are a family of complex multi-domain intracellular enzymes that share a calcium-dependent cysteine protease core. These are not degradative enzymes,... 
X-ray crystallography | Domain structure | Proteolysis | Calcium-binding | Proteinase | Inhibitor complex | Enzyme activation | enzyme activation | inhibitor complex | calcium-binding | CRYSTAL-STRUCTURE | EF-HAND | BIOCHEMISTRY & MOLECULAR BIOLOGY | domain structure | GIRDLE MUSCULAR-DYSTROPHY | ACTIVATED NEUTRAL PROTEASE | SKELETAL-MUSCLE | proteinase | MUSCLE-SPECIFIC CALPAIN | CA-2&-ACTIVATED PROTEASE | MU-CALPAIN | CA2+ REQUIREMENT | proteolysis | CALCIUM-DEPENDENT PROTEASE | Calcium-Binding Proteins - chemistry | Humans | Recombinant Proteins - chemistry | Terminology as Topic | Recombinant Proteins - genetics | Structure-Activity Relationship | Calpain - genetics | Calpain - chemistry | Protein Isoforms - physiology | Calpain - physiology | Animals | Protein Isoforms - chemistry | Calcium-Binding Proteins - physiology | Protein Conformation | Protein Subunits - chemistry | Enzyme Activation | Protein Subunits - physiology | Calcium Signaling | Calpain - antagonists & inhibitors | Protein Isoforms - genetics | Protein Subunits - genetics
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
12. Calpain methods and protocols
by Elce, John S
2000, Methods in molecular biology, ISBN 9780896036321, Volume 144
Calpain
Web Resource
Details down arrow
13. Full Text Tenderness – An enzymatic view
by Kemp, Caroline M and Sensky, Paul L and Bardsley, Ronald G and Buttery, Peter J and Parr, Tim
Meat Science, ISSN 0309-1740, 2010, Volume 84, Issue 2, pp. 248 - 256
One of the most common causes of unacceptability in meat quality is toughness. Toughness is attributed to a range of factors including the amount of... 
Calpains | Meat tenderisation | Calpastatin | Caspases | Post-mortem proteolysis | MEAT TENDERNESS | PORCINE LONGISSIMUS MUSCLE | FOOD SCIENCE & TECHNOLOGY | CALPASTATIN PROMOTERS | CALPAIN SYSTEM | BOVINE SKELETAL-MUSCLE | MESSENGER-RNA | POSTMORTEM PROTEOLYSIS | MU-CALPAIN | MYOFIBRILLAR STRUCTURES | CASPASE ACTIVITY | Calcium-Binding Proteins - metabolism | Muscle, Skeletal - enzymology | Calpain - metabolism | Food Technology | Humans | Muscle, Skeletal - physiology | Animals | Caspases - metabolism | Cathepsins - metabolism | Chemical Phenomena | Taste | Meat - standards | Postmortem Changes | Calpain - antagonists & inhibitors | Peptide Hydrolases - metabolism | Proteolysis | Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
14. Full Text Calpain involvement in the remodeling of cytoskeletal anchorage complexes
by Lebart, Marie‐Christine and Benyamin, Yves
The FEBS Journal, ISSN 1742-464X, 08/2006, Volume 273, Issue 15, pp. 3415 - 3426
Cells offer different types of cytoskeletal anchorages: transitory structures such as focal contacts and perennial ones such as the sarcomeric cytoskeleton of... 
calpain | adhesion | cytoskeleton | muscle | focal complexes | ischemia | Calpain | Cytoskeleton | Muscle | Ischemia | Focal complexes | Adhesion | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEDIATED PHOSPHORYLATION | SKELETAL-MUSCLE | CALPAIN/CALPASTATIN NETWORK | FOCAL ADHESION PROTEINS | MUSCLE-SPECIFIC CALPAIN | CELL-MIGRATION | EPIDERMAL-GROWTH-FACTOR | POSTMORTEM PROTEOLYSIS | MU-CALPAIN | CALCIUM-DEPENDENT PROTEASE | Calpain - physiology | Animals | Calpain - metabolism | Humans | Cytoskeleton - metabolism | Protein Conformation | Calpain - chemistry | Life Sciences | Biochemistry, Molecular Biology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
15. Full Text Calpastatin binds to a calmodulin-binding site of cardiac Cav1.2 Ca.sup.2+ channels
by Saud, Zahangir A and Minobe, Etsuko and Wang, Wu-Yang and Han, Dong-Yun and Horiuchi, Masahisa and Hao, Li-Ying and Kameyama, Masaki
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 12/2007, Volume 364, Issue 2, p. 372
Calpastatin is an endogenous inhibitor of calpain and composed of domain L (CS.sub.L), which interacts with the Cav1.2 channels, and four repetitive calpain... 
Calpain
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
16. Full Text Regulation and physiological roles of the calpain system in muscular disorders
by Sorimachi, Hiroyuki and Ono, Yasuko
Cardiovascular Research, ISSN 0008-6363, 10/2012, Volume 96, Issue 1, pp. 11 - 22
Calpains, a family of Ca-2-dependent cytosolic cysteine proteases, can modulate their substrates structure and function through limited proteolytic activity.... 
Calpain | Calcium | Intracellular proteolysis | Sarcomere | Transgenic mice | CARDIAC & CARDIOVASCULAR SYSTEMS | ANKYRIN REPEAT PROTEIN | REDUCES INFARCT SIZE | SMALL-SUBUNIT GENE | ACTIVATED NEUTRAL PROTEASE | SKELETAL-MUSCLE | TROPONIN-I DEGRADATION | MUSCLE-SPECIFIC CALPAIN | MU-CALPAIN | KAPPA-B PATHWAY | CALCIUM-DEPENDENT PROTEASE | Muscle, Skeletal - enzymology | Myocardium - enzymology | Animals | Calpain - metabolism | Muscular Diseases - enzymology | Humans | Enzyme Activation | Cardiovascular Diseases - enzymology | Reviews | Focus on the Calpain Family in the Cardiovascular System
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
17. Full Text The Calpain System
by GOLL, DARREL E and THOMPSON, VALERY F and LI, HONGQI and WEI, WEI and CONG, JINYANG
Physiological Reviews, ISSN 0031-9333, 07/2003, Volume 83, Issue 3, pp. 731 - 801
Muscle Biology Group, University of Arizona, Tucson, Arizona Goll, Darrel E., Valery F. Thompson, Hongqi Li, Wei Wei, and Jinyang Cong. The Calpain System.... 
BOVINE SKELETAL-MUSCLE | PHYSIOLOGY | TRAUMATIC BRAIN-INJURY | MUSCLE-SPECIFIC CALPAIN | GIRDLE MUSCULAR-DYSTROPHY | ACTIVATED NEUTRAL PROTEASE | SITE-DIRECTED MUTAGENESIS | CALMODULIN-LIKE DOMAIN | ACTIN-BINDING-PROTEIN | ELECTRON-MICROSCOPIC LOCALIZATION | CALCIUM-DEPENDENT PROTEASE | Calcium-Binding Proteins - metabolism | Animals | Calpain - metabolism | Humans | Substrate Specificity | Protein Conformation | Calpain - genetics | Calpain - chemistry | Proteases | Analysis | Physiological aspects | Calpain | Genetic aspects | Research | Calcium-binding proteins | Statistics | Protein binding
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
18. Calpain
: pharmacology and toxicology of calcium-dependent protease
by Wang, Kevin K. W and Yuen, Po-Wai
1999, ISBN 9781560327134, xiv, 448
physiology | Calpain | Pathophysiology | Physiological effect | pharmacology
Book
Details down arrow
19. Full Text Calpain chronicle-an enzyme family under multidisciplinary characterization
by SORIMACHI, Hiroyuki and HATA, Shoji and ONO, Yasuko
Proceedings of the Japan Academy, Series B, ISSN 0386-2208, 2011, Volume 87, Issue 6, pp. 287 - 327
Calpain is an intracellular Ca2+-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02) discovered in 1964. It was also called CANP (Ca2+-activated... 
calpainopathy | calpain | calcium ion | muscular dystrophy | gastropathy | intracellular proteolysis | Calpain | Calpainopathy | Calcium ion | Intracellular proteolysis | Gastropathy | Muscular dystrophy | YEAST YARROWIA-LIPOLYTICA | PHOSPHORYLASE B KINASE | CHICKEN SKELETAL-MUSCLE | PH SIGNAL-TRANSDUCTION | MULTIDISCIPLINARY SCIENCES | ELEGANS SEX DETERMINATION | ACTIVATED NEUTRAL PROTEASE | MUSCLE-SPECIFIC CALPAIN | STOMACH-SPECIFIC CALPAIN | TYPE-2 DIABETES-MELLITUS | CALCIUM-DEPENDENT PROTEASE | Protein Structure, Tertiary | Amino Acid Sequence | Calpain - classification | Animals | Calpain - metabolism | Disease | Humans | Molecular Sequence Data | Enzyme Activation | Calpain - genetics | Organ Specificity | Calpain - chemistry | Enzymes | Calcium (intracellular) | Calcium | Proteolysis | Diabetes mellitus | Cysteine proteinase | Genomes | Lethality | Models | Structure-function relationships | Review
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights